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2',3'-CMP + H2O
?
-
-
-
-
?
2',3'-UMP + H2O
?
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
2'-CMP + H2O
cytidine + phosphate
-
-
-
-
?
2'-deoxyadenosine 5'-monophosphate + H2O
?
2'-GMP + H2O
guanosine + phosphate
-
-
-
-
?
2'-UMP + H2O
uridine + phosphate
-
-
-
-
?
2'-[2-benzthiazole]-6'-hydroxybenzthiazole phosphate + H2O
2'-[2-benzthiazole]-6'-hydroxybenzthiazole + phosphate
-
weakly fluorescent substrate
highly fluorescent product
?
2,4-dinitrophenyl phosphate + H2O
2,4-dinitrophenol + phosphate
-
-
-
-
?
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate + H2O
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenol + phosphate
-
CDP-star
-
-
?
2-glycerol phosphate + H2O
glycerol + phosphate
-
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
2-naphtyl phosphate + H2O
2-naphthol + phosphate
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
3'-AMP + H2O
adenosine + phosphate
3'-CMP + H2O
cytidine + phosphate
-
-
-
-
?
3'-GMP + H2O
guanosine + phosphate
-
-
-
-
?
3'-ITP + H2O
?
-
51.5% of the activity with 4-nitrophenyl phosphate
-
-
?
3'-UMP + H2O
uridine + phosphate
-
-
-
-
?
3-nitrobenzyl phosphate + H2O
3-nitrobenzoate + phosphate
-
-
-
?
3-nitrophenyl phosphate + H2O
3-nitrophenol + phosphate
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
4-aminophenyl phosphate + H2O
4-aminophenol + phosphate
-
-
-
?
4-methoxy-4-(3-phosphatephenyl)spiro [1,2-dioxetane-3,2'-adamantane] disodium salt + H2O
?
-
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
5'-CMP + H2O
cytidine + phosphate
5'-dAMP + H2O
?
-
-
-
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
80% of activity with p-nitrophenyl phosphate
-
-
?
5'-dGMP + H2O
?
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
5'-IMP + H2O
inosine + phosphate
5'-TMP + H2O
thymidine + phosphate
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
5-bromo-4-chloro-3-indolyl phosphate + H2O
5-bromo-4-chloro-indole + phosphate
-
-
-
?
5-bromo-4-chloro-3-indolyl phosphate + H2O
?
5-bromo-4-chloro-3-indolyl phosphate + nitroblue tetrazolium
?
-
i.e. BCIP/NBT system
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
?
-
-
-
-
?
acyl-CoA:cholesterol acyltransferase + H2O
?
-
-
-
-
?
adenosine 5'-(beta-glucosyl)diphosphate + H2O
?
-
29.8% of the activity with 4-nitrophenyl phosphate
-
-
?
adenosine 5'-diphosphate + H2O
AMP + phosphate
-
77% of the activity with 4-nitrophenyl phosphate
-
-
?
adenosine 5'-monophosphate + H2O
?
306.1% of the activity with 4-nitrophenyl phosphate
-
-
?
adenosine 5'-triphosphate + H2O
?
257.4% of the activity with 4-nitrophenyl phosphate
-
-
?
adenosine 5'-triphosphate + H2O
AMP + phosphate
-
61% of the activity with 4-nitrophenyl phosphate
-
-
?
ADP + H2O
AMP + phosphate
alpha-glycerol phosphate + H2O
glycerol + phosphate
-
-
-
?
alpha-glycerophosphate + H2O
glycerol + phosphate
alpha-naphthyl acid phosphate + H2O
?
88.6% of the activity with 4-nitrophenyl phosphate
-
-
?
alpha-naphthyl phosphate + H2O
1-naphthol + phosphate
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
AMP + H2O
adenosine + phosphate
arginine phosphate + H2O
Arg + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
beta-glycerol phosphate + H2O
glycerol + phosphate
-
-
-
?
beta-glycerophosphate + H2O
?
-
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
beta-glyceryl phosphate + H2O
glycerol + phosphate
bis(p-nitrophenyl) phosphate + H2O
?
bis(p-nitrophenyl)phosphate + H2O
?
-
-
-
-
?
bis-4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
bis-p-nitrophenyl phosphate + H2O
?
CMP + H2O
cytidine + phosphate
cysteamine S-phosphate + H2O
cysteamine + phosphate
-
-
-
-
?
cytidine 5'-monophosphate + H2O
?
343.8% of the activity with 4-nitrophenyl phosphate
-
-
?
cytidine phosphate + H2O
?
-
-
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
52% of the activity with 4-nitrophenyl phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
D-glucose 1-phosphate + H2O
D-glucose + phosphate
D-glucose 6-phosphate + H2O
D-glucose + phosphate
D-ribose 5-phosphate + H2O
D-ribose + phosphate
dentine phosphoprotein + H2O
?
-
-
-
-
?
diphosphate + H2O
2 phosphate
disodium 3-(4-meth- oxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]- decan]-4-yl)phenyl phosphate + H2O
?
-
-
-
?
ethyl phosphate + H2O
ethanol + phosphate
-
-
-
?
etoposide phosphate + H2O
?
-
-
-
-
?
fructose 1,6-diphosphate + H2O
?
gamma-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
geranyl diphosphate + H2O
geraniol + ?
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
Glucose 6-phosphate + H2O
Glucose + phosphate
glycerophosphate + H2O
glycerol + phosphate
glycogen synthase + H2O
?
GMP + H2O
guanosine + phosphate
guanosine 5'-monophosphate + H2O
?
358.8% of the activity with 4-nitrophenyl phosphate
-
-
?
guanosine phosphate + H2O
?
-
-
-
-
?
histidinol phosphate + H2O
?
-
-
-
-
?
histone + H2O
?
-
32P-labelled
-
-
?
histone II-A + H2O
?
-
enzyme shows protein phosphatase activity
-
?
HMG-CoA reductase + H2O
?
-
-
-
-
?
indoxyl phosphate + nitroblue tetrazolium chloride
nitrioblue diformazan + phosphate
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
-
?
L-histidinyl phosphate + H2O
L-histidinol + phosphate
linear DNA fragment + H2O
dephosphorylated linear DNA fragment + phosphate
the enzyme has a dephosphorylation efficiency of 92.9% to dephosphorylate linear DNA fragments of plasmid pUC18
-
-
?
methyl 3-nitrophenyl phosphate + H2O
methyl phosphate + 3-nitrophenol
-
-
-
?
methyl 4-nitrophenyl phosphate + H2O
methyl phosphate + 4-nitrophenol
-
-
-
?
methyl 4-nitrophenyl phosphorothioate + H2O
4-nitrophenol + methyl phosphorothioate
only the R-enantiomer is detectably hydrolyzed by the enzyme
-
-
?
methyl p-nitrophenyl phosphate + H2O
methanol + p-nitrophenol + phosphate
-
-
-
-
?
methyl p-nitrophenyl phosphorothioate + H2O
methanol + p-nitrophenol + phosphorothioate
-
-
-
-
?
methyl phosphate + H2O
methanol + phosphate
methylphenyl phosphate + H2O
methyl phosphate + phenol
-
-
-
?
N-acetylcysteamine S-phosphate + H2O
N-acetylcysteamine + phosphate
-
-
-
-
?
NADP+ + H2O
?
-
20% of activity with p-nitrophenyl phosphate
-
-
?
NADPH-cytochrome reductase + H2O
?
-
-
-
-
?
o-carboxyphenyl phosphate + H2O
o-carboxyphenol + phosphate
-
-
-
-
?
O-phospho-DL-serine + H2O
DL-serine + phosphate
-
-
-
?
O-phospho-DL-tyrosine + H2O
DL-tyrosine + phosphate
-
-
-
?
O-phosphoserine + H2O
serine + phosphate
O-phosphothreonine + H2O
threonine + phosphate
O-phosphotyrosine + H2O
tyrosine + phosphate
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
p-toluidinium 5-bromo-4-chloro-3-indolyl phosphate + H2O
?
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
phospho-DL-Thr + H2O
phosphate + Thr
-
-
-
-
?
phospho-DL-Tyr + H2O
phosphate + Tyr
-
-
-
-
?
phospho-Ser histone + H2O
?
phospho-Ser-casein + H2O
?
phospho-Tyr angiotensin + H2O
angiotensin + phosphate
-
-
-
-
?
phospho-Tyr-casein + H2O
?
-
-
-
-
?
phospho-Tyr-histone + H2O
?
phosphocholine + H2O
choline + phosphate
-
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
phosphoethanolamine + H2O
phosphate + ethanolamine
phosphorylase kinase + H2O
?
phosphorylated acetyl-CoA carboxylase + H2O
acetyl-CoA carboxylase + phosphate
phosphorylcholine + H2O
phosphate + choline
phosphoserine + H2O
phosphate + Ser
phosphothreonine + H2O
phosphate + Thr
-
22.1% of the activity with 4-nitrophenyl phosphate
-
-
?
phosphotyrosine + H2O
phosphate + Tyr
-
23.7% of the activity with 4-nitrophenyl phosphate
-
-
?
poly(I) + H2O
?
-
-
-
-
?
polymetaphosphate + H2O
?
-
-
-
-
?
polyphosphate PP-25 + H2O
?
-
-
-
-
?
propargyl phosphate + H2O
prop-1-yne + phosphate
-
-
-
?
protamine + H2O
?
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
-
-
?
Raytide + H2O
?
-
-
-
-
?
riboflavin 5'-phosphate + H2O
riboflavin + phosphate
-
-
-
-
?
S-(carboxymethyl)phosphorothioate + H2O
?
-
-
-
-
?
S-[2-(methoxy carbonyl)ethyl] phosphorothioate + H2O
?
-
-
-
-
?
spermidine N'-acetyltransferase + H2O
?
-
-
-
-
?
thiamin diphosphate + H2O
thiamin phosphate + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
tyrosine phosphate + H2O
tyrosine + phosphate
-
-
-
-
?
UDP-glucose + H2O
?
-
20% of activity with p-nitrophenyl phosphate
-
-
?
UMP + H2O
uridine + phosphate
uridine 5'-monophosphate + H2O
?
388.6% of the activity with 4-nitrophenyl phosphate
-
-
?
uridine phosphate + H2O
?
-
-
-
-
?
[(4-chlorophenyl)thio](10-methyl-9(10H)-acridinylidene)-methanol 1-(dihydrogenphosphate) disodium salt + H2O
?
-
-
-
?
additional information
?
-
2',3'-GMP + H2O
?
-
-
-
-
?
2',3'-GMP + H2O
?
-
-
-
-
?
2',3-AMP + H2O
?
-
-
-
-
?
2',3-AMP + H2O
?
-
20% of activity with p-nitrophenyl phosphate
-
-
?
2'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
2'-deoxyadenosine 5'-monophosphate + H2O
?
113.3% of the activity with 4-nitrophenyl phosphate
-
-
?
2'-deoxyadenosine 5'-monophosphate + H2O
?
113.3% of the activity with 4-nitrophenyl phosphate
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
-
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
-
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
53.7% of the activity with 4-nitrophenyl phosphate
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
hydrolyzed by isoenzyme III, weak activity with isoenzyme I and II
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
wild-type activity is 16.9% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 16.3fold higher than activity from wild-type enzyme
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
-
hydrolyzed by isoenzyme III, weak activity with isoenzyme II, no activity with isoenzyme I
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
-
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
-
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
-
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
-
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
-
-
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
-
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
-
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
664559, 665025, 693244, 693398, 695120, 707733, 713744, 714329, 714864, 729818, 750048 -
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
reaction is at least partially diffusion-controlled
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
non-specific, phosphoseryl intermediate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
strong support for a model in which electrostatic interactions between the bimetallo Zn2+ site and a nonbridging phosphate ester oxygen atom make a significant contribution to the large rate enhancement observed for alkaline phosphatase-catalyzed phosphate monoester hydrolysis
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
hydrolysis of 4-nitrophenylphosphate is nonlinear with time when the enzyme is microinjected into reversed micelles (of hexadecyltrimethylammoniumbromide in cyclohexane, with 1-butanol as cosurfactant) that contain substrate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
hydrolysis of 4-nitrophenylphosphate is nonlinear with time when the enzyme is microinjected into reversed micelles (of hexadecyltrimethylammoniumbromide in cyclohexane, with 1-butanol as cosurfactant) that contain substrate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
allosteric mechanism
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
activity with mutant os-1 enzyme is 12.2fold higher than activity from wild-type enzyme
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
strongest affinity substrate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
best substrate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
non-specific, via phosphoseryl intermediate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
5'-ADP + H2O
?
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
90% of activity with p-nitrophenyl phosphate
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
90% of activity with p-nitrophenyl phosphate
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-ATP + H2O
?
-
-
-
-
?
5'-ATP + H2O
?
-
weak
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
80% of activity with p-nitrophenyl phosphate
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
-
?
5'-dCMP + H2O
?
-
-
-
-
?
5'-dCMP + H2O
?
-
-
-
-
?
5'-dTMP + H2O
?
-
-
-
-
?
5'-dTMP + H2O
?
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
40% of activity with p-nitrophenyl phosphate
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
-
?
5'-IMP + H2O
inosine + phosphate
-
-
-
-
?
5'-IMP + H2O
inosine + phosphate
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
30% of activity with p-nitrophenyl phosphate
-
-
?
5'-UMP + H2O
uridine + phosphate
-
30% of activity with p-nitrophenyl phosphate
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
-
?
5-bromo-4-chloro-3-indolyl phosphate + H2O
?
50.3% of the activity with 4-nitrophenyl phosphate
-
-
?
5-bromo-4-chloro-3-indolyl phosphate + H2O
?
50.3% of the activity with 4-nitrophenyl phosphate
-
-
?
ADP + H2O
?
antarctic bacterium
-
-
-
-
?
ADP + H2O
?
antarctic bacterium HK47
-
-
-
-
?
ADP + H2O
?
-
alkaline phosphatase F I
-
-
?
ADP + H2O
?
-
alkaline phosphatase F II
-
-
?
ADP + H2O
?
-
20% of activity with p-nitrophenyl phosphate
-
-
?
ADP + H2O
?
-
20% of activity with p-nitrophenyl phosphate
-
-
?
ADP + H2O
AMP + phosphate
-
wild-type activity is 16.9% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 1.2fold lower than activity from wild-type enzyme
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
alpha-glycerophosphate + H2O
glycerol + phosphate
-
60% of activity with p-nitrophenyl phosphate
-
-
?
alpha-glycerophosphate + H2O
glycerol + phosphate
-
low activity with alpha-isomer
-
?
alpha-naphthyl phosphate + H2O
1-naphthol + phosphate
-
hydrolyzed by isoenzyme II and III, no activity with isoenzyme I
-
-
?
alpha-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
-
?
alpha-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
-
?
alpha-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
-
?
alpha-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
-
?
alpha-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
-
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
-
-
-
-
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
-
-
-
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
-
-
-
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
-
-
-
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
-
-
-
?
AMP + H2O
adenosine + phosphate
antarctic bacterium
-
-
-
-
?
AMP + H2O
adenosine + phosphate
antarctic bacterium HK47
-
-
-
-
?
AMP + H2O
adenosine + phosphate
-
alkaline phosphatase F I
-
-
?
AMP + H2O
adenosine + phosphate
-
alkaline phosphatase F II
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
-
?
AMP + H2O
adenosine + phosphate
-
wild-type activity is 9.6% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 18.2fold higher than activity from wild-type enzyme
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
?
ATP + H2O
?
-
57.8% of the activity with 4-nitrophenyl phosphate
-
-
?
ATP + H2O
?
-
alkaline phosphatase F I
-
-
?
ATP + H2O
?
-
alkaline phosphatase F II
-
-
?
ATP + H2O
?
-
10% of activity with p-nitrophenyl phosphate
-
-
?
ATP + H2O
?
-
10% of activity with p-nitrophenyl phosphate
-
-
?
ATP + H2O
?
-
wild-type activity is 15.4% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 6.9fold higher than activity from wild-type enzyme
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
20% of activity with p-nitrophenyl phosphate
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
20% of activity with p-nitrophenyl phosphate
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
uranium precipitation assay: uranyl carbonate solution in carbonate-bicarbonate buffer, supplemented with beta-glycerophosphate as the substrate at 30°C under static nongrowing conditions in a final volume of 5 ml
-
-
?
beta-glyceryl phosphate + H2O
glycerol + phosphate
-
-
-
?
beta-glyceryl phosphate + H2O
glycerol + phosphate
-
-
-
?
bis(p-nitrophenyl) phosphate + H2O
?
6.1% of the activity with 4-nitrophenyl phosphate
-
-
?
bis(p-nitrophenyl) phosphate + H2O
?
6.1% of the activity with 4-nitrophenyl phosphate
-
-
?
bis-p-nitrophenyl phosphate + H2O
?
-
-
-
?
bis-p-nitrophenyl phosphate + H2O
?
-
-
-
?
bis-p-nitrophenyl phosphate + H2O
?
-
weak activity
-
-
?
casein + H2O
?
-
-
-
-
?
casein + H2O
?
-
enzyme shows protein phosphatase activity
-
?
casein + H2O
?
-
enzyme shows protein phosphatase activity
-
?
CMP + H2O
cytidine + phosphate
-
alkaline phosphatase F I
-
-
?
CMP + H2O
cytidine + phosphate
-
alkaline phosphatase F II
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
36% of the activity with 4-nitrophenyl phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
5.2% of the activity with 4-nitrophenyl phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
wild-type activity is 2.2% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 52fold higher than activity from wild-type enzyme
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
32% of the activity with 4-nitrophenyl phosphate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
wild-type activity is 9.6% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 21fold higher than activity from wild-type enzyme
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
60% of the activity with 4-nitrophenyl phosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
19.4% of the activity with 4-nitrophenyl phosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
wild-type activity is 6.6% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 34.5fold higher than activity from wild-type enzyme
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
alkaline phosphatase F I
-
-
?
diphosphate + H2O
2 phosphate
-
alkaline phosphatase F II
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
weak activity
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
no activity
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
weak activity
-
-
?
fructose 1,6-diphosphate + H2O
?
-
-
-
-
?
fructose 1,6-diphosphate + H2O
?
-
-
-
-
?
fructose 1,6-diphosphate + H2O
?
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
-
93% of the activity with 4-nitrophenyl phosphate
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
alkaline phosphatase F I
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
alkaline phosphatase F II
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
glycerophosphate + H2O
?
248.7% of the activity with 4-nitrophenyl phosphate
-
-
?
glycerophosphate + H2O
?
248.7% of the activity with 4-nitrophenyl phosphate
-
-
?
glycerophosphate + H2O
glycerol + phosphate
-
63% of the activity with 4-nitrophenyl phosphate
-
-
?
glycerophosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycogen synthase + H2O
?
-
-
-
-
?
glycogen synthase + H2O
?
-
-
-
-
?
glycogen synthase + H2O
?
-
-
-
-
?
GMP + H2O
guanosine + phosphate
-
alkaline phosphatase F I
-
-
?
GMP + H2O
guanosine + phosphate
-
alkaline phosphatase F II
-
-
?
GMP + H2O
guanosine + phosphate
-
-
-
-
?
GTP + H2O
?
antarctic bacterium
-
-
-
-
?
GTP + H2O
?
antarctic bacterium HK47
-
-
-
-
?
L-histidinyl phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-histidinyl phosphate + H2O
L-histidinol + phosphate
-
-
-
?
methyl phosphate + H2O
methanol + phosphate
-
-
-
?
methyl phosphate + H2O
methanol + phosphate
-
-
-
-
?
NAD+ + H2O
?
-
alkaline phosphatase F I
-
-
?
NAD+ + H2O
?
-
alkaline phosphatase F II
-
-
?
O-phosphoserine + H2O
serine + phosphate
-
-
-
?
O-phosphoserine + H2O
serine + phosphate
-
-
-
?
O-phosphoserine + H2O
serine + phosphate
-
wild-type activity is 14.0% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 10.9fold higher than activity from wild-type enzyme
-
-
?
O-phosphothreonine + H2O
threonine + phosphate
-
-
-
?
O-phosphothreonine + H2O
threonine + phosphate
-
wild-type activity is 21.3% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 9.8fold higher than activity from wild-type enzyme
-
-
?
O-phosphotyrosine + H2O
tyrosine + phosphate
-
-
-
?
O-phosphotyrosine + H2O
tyrosine + phosphate
-
-
-
?
O-phosphotyrosine + H2O
tyrosine + phosphate
-
wild-type activity is 68.3% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 8.6fold higher than activity from wild-type enzyme
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
antarctic bacterium
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
antarctic bacterium HK47
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
hydrolyzed by isoenzyme I, II or III
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
activities towards tyrosine phosphatase substrate ENCpYINASL and calcineurin substrate DLDVPIPGRDFRRVpSVAAE were also detected, further substrates: ATP, sn-glycerol 3-phosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
94563, 94564, 94568, 94573, 94575, 94582, 94609, 94616, 94623, 94627, 94630 -
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
-
-
-
-
?
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phospho-Ser histone + H2O
?
-
-
-
-
?
phospho-Ser histone + H2O
?
-
-
-
-
?
phospho-Ser histone + H2O
?
-
-
-
-
?
phospho-Ser-casein + H2O
?
-
-
-
-
?
phospho-Ser-casein + H2O
?
-
-
-
-
?
phospho-Ser-casein + H2O
?
-
-
-
-
?
phospho-Tyr-histone + H2O
?
-
-
-
-
?
phospho-Tyr-histone + H2O
?
-
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
-
-
-
?
phosphoethanolamine + H2O
phosphate + ethanolamine
-
hydrolyzed by isoenzyme III, weak activity with isoenzyme II, no activity with isoenzyme I
-
-
?
phosphoethanolamine + H2O
phosphate + ethanolamine
-
-
-
-
?
phosphoethanolamine + H2O
phosphate + ethanolamine
-
-
-
-
?
phosphoethanolamine + H2O
phosphate + ethanolamine
-
-
-
-
?
phosphorylase kinase + H2O
?
-
-
-
-
?
phosphorylase kinase + H2O
?
-
-
-
-
?
phosphorylated acetyl-CoA carboxylase + H2O
acetyl-CoA carboxylase + phosphate
-
-
-
-
?
phosphorylated acetyl-CoA carboxylase + H2O
acetyl-CoA carboxylase + phosphate
-
-
-
-
?
phosphorylcholine + H2O
phosphate + choline
-
hydrolyzed by isoenzyme III, no activity with isoenzyme I and II
-
-
?
phosphorylcholine + H2O
phosphate + choline
-
-
-
-
?
phosphoserine + H2O
phosphate + Ser
-
9.3% of the activity with 4-nitrophenyl phosphate
-
-
?
phosphoserine + H2O
phosphate + Ser
-
hydrolyzed by isoenzyme II, weak activity with isoenzyme I and II
-
-
?
phosphoserine + H2O
phosphate + Ser
-
-
-
-
?
phosphoserine + H2O
phosphate + Ser
-
-
-
-
?
phosphoserine + H2O
phosphate + Ser
-
-
-
-
?
phosphoserine + H2O
phosphate + Ser
-
-
-
-
?
phosvitin + H2O
?
-
-
-
-
?
phosvitin + H2O
?
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
?
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
?
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
?
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
?
-
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
-
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
-
-
-
-
?
UDP + H2O
?
-
-
-
-
?
UMP + H2O
uridine + phosphate
-
alkaline phosphatase F I
-
-
?
UMP + H2O
uridine + phosphate
-
alkaline phosphatase F II
-
-
?
UMP + H2O
uridine + phosphate
-
-
-
-
?
UTP + H2O
?
antarctic bacterium
-
-
-
-
?
UTP + H2O
?
antarctic bacterium HK47
-
-
-
-
?
UTP + H2O
?
-
67% of the activity with 4-nitrophenyl phosphate
-
-
?
additional information
?
-
-
the purified alkaline phosphatase removes the 5'-phosphate group of a linearized plasmid without showing DNAase activity
-
-
?
additional information
?
-
-
motion required for the formation of the enzyme-phosphate complex is minimal on the part of alkaline phosphatase
-
-
?
additional information
?
-
-
TNAP is an essential component of serum calcification activity and that its role in the shotgun mechanism is to activate the serum nucleator of apatite crystal formation
-
-
?
additional information
?
-
-
enzmye exclusively phosphomonoesters as a substrate, and not phosphodiesters
-
-
?
additional information
?
-
-
alkaline phosphatase activity is decreased during vitamin C deficiency. The decreased expression of collagen, alkaline phosphatase, and osteocalcin can explain the defects in bone caused by scurvy
-
-
?
additional information
?
-
-
involvement of the enzyme in sugar metabolism
-
-
?
additional information
?
-
-
could be a component of muscle regulatory mechanism at the biochemical level secondary to hyper-regulation of Chasmagnathus granulatus
-
-
?
additional information
?
-
-
the enzyme is involved in the biochemical amplification process of excitation or adaption
-
-
?
additional information
?
-
-
the enzyme also catalyses the transfer of the phosphoryl group to alcohols
-
?
additional information
?
-
-
the enzyme is involved in recovering of phosphate esters when free phosphate is depleted
-
?
additional information
?
-
-
the enzyme catalyzes the oxidation of phosphite to phosphate and molecular H2: H2PO3 + H2O = H3PO4 + H2
-
-
?
additional information
?
-
-
HcALP is a Cry1Ac binding protein
-
-
?
additional information
?
-
-
enzyme is impportant in bone formation and mineralization
-
?
additional information
?
-
-
the enzyme is necessary for the initiation of mineralization by osteoblast-derived matrix vesicles but not for the continuation of the processes
-
?
additional information
?
-
-
hypophosphatasia is an inherited disorder caused by mutations in the bone alkaline phosphatase gene
-
-
?
additional information
?
-
-
hypophosphatasia is caused by deficiency of activity of the tissue-nonspecific alkaline phosphatase, resulting in a defect of bone mineralization
-
-
?
additional information
?
-
-
involvement of androgen receptor positive chondrocytes in thyroid cartilage mineralization, probably by a testosterone-linked stimulation of alkaline phosphatase
-
-
?
additional information
?
-
-
strong correlations between ALP activity and lipid accumulation. These data suggest that ALP and fat storage are tightly linked during preadipocyte maturation
-
-
?
additional information
?
-
-
IAP possesses lipopolysaccharide-dephosphorylating activity
-
-
?
additional information
?
-
-
enzyme is important in bone formation and mineralization
-
?
additional information
?
-
-
the enzyme is involved in the regulation of mineralization of cartilage matrix
-
?
additional information
?
-
-
strong correlations between ALP activity and lipid accumulation. These data suggest that ALP and fat storage are tightly linked during preadipocyte maturation
-
-
?
additional information
?
-
-
levamisole-insensitive alkaline phosphatase activity could be a component of muscle regulatory mechanism at the biochemical level secondary to hyper-regulation of Chasmagnathus granulatus
-
-
?
additional information
?
-
-
no hydrolysis of diphosphate
-
-
?
additional information
?
-
-
enzyme with limited substrate specificity, no dephosphorylation of ATP, PEP, glucose 6-phosphate, phosphoinositol 4',5'-bisphosphate, phosphoproteins
-
-
?
additional information
?
-
-
the enzyme is a nonspecific phosphomonoesterase that functions through a phosphoseryl intermediate to produce free inorganic phosphate or to transfer the phosphoryl group to other alcohols
-
?
additional information
?
-
-
a low level of high-molecular weight alkaline phosphatase is produced constitutively, low-molecular weight alkaline phosphatase is produced only after induction
-
-
?
additional information
?
-
-
important enzyme in the final stages of cell division when Pseudomonas aeruginosa is cultured in inorganic phosphate-limiting media
-
-
?
additional information
?
-
-
high-molecular weight alkaline phosphatase is active as phosphomonoesterase, low-molecular weight alkaline phosphatase is active as phosphomonoesterase and phosphodiesterase
-
-
?
additional information
?
-
-
a low level of high-molecular weight alkaline phosphatase is produced constitutively, low-molecular weight alkaline phosphatase is produced only after induction
-
-
?
additional information
?
-
-
high-molecular weight alkaline phosphatase is active as phosphomonoesterase, low-molecular weight alkaline phosphatase is active as phosphomonoesterase and phosphodiesterase
-
-
?
additional information
?
-
the enzyme also dephosphorylizes cohesive and blunt ends of DNA fragments, cohesive ends are slightly preferred
-
?
additional information
?
-
-
the enzyme also dephosphorylizes cohesive and blunt ends of DNA fragments, cohesive ends are slightly preferred
-
?
additional information
?
-
-
enzyme is impportant in bone formation and mineralization
-
?
additional information
?
-
-
non-specific enzyme, wide substrate specificity, no phosphate transfer with alcohols, except for Tris
-
?
additional information
?
-
-
the product of the PHO8 gene is repressible by phosphate in the medium
-
-
?
additional information
?
-
-
non-specific enzyme, wide substrate specificity, no phosphate transfer with alcohols, except for Tris
-
?
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BaCl2
-
10 mM, 3.4fold increase in activity
CaCl2
-
1 mM, 1.6fold increase in activity
Fe3+
Fe(III) and Zn(II) binuclear centre
Magnesium
-
enzyme contains magnesium
MgCl2
-
10 mM, 2.1fold increase in activity
MnCl2
-
10 mM, activity is enhanced to 138% of control
phosphate
-
enzyme contains one or two phosphate ions
Sr2+
-
2 mM, 4fold increase in activity
sulfate
-
the rate of irreversible thermal inactivation is strongly reduced by addition of kosmotropic anions like sulfate (half-life increases from 8 to 580 min at 60 °C)
Zinc
-
enzyme contains zinc
Al3+
inhibitory effect
Al3+
-
inhibits high molecular weight and low molecular weight alkaline phosphatase non-competitively
Al3+
-
activates only the extracellular form
Ba2+
-
2 mM, 2.2fold increase in activity
Ca2+
-
2 mM, 4.95fold increase in activity
Ca2+
-
activates isoenzyme I, weak activation of isoenzyme III
Ca2+
115% activity at 5 mM
Ca2+
-
required for activity
Ca2+
-
requires Ca2+ and not Zn2+ ions for its activity.Optimal Ca2+ concentration for enzymatic activity is 3.4 mM
Ca2+
activates. D527 of PhoX might be the ligand bound to the catalytic calcium
Ca2+
-
125% activity at 2 mM
Ca2+
-
5 mM, 102% of initial activity
Ca2+
-
partly restores enzymatic activity after EDTA treatment. When Mg2+ is combined with Zn2+, it enhances the catalytic activity up to 3fold
Ca2+
-
20-25% stimulation
Co2+
-
2 mM, 2.6fold increase in activity
Co2+
-
enzyme exhibits 1.4fold activation in the presenece of 1 mM Co2+
Co2+
108% activity at 5 mM
Co2+
required. In the absence of Co2+ in the lysis buffer, activity of extracts is only 10% of the normal value
Co2+
a divalent cation is essential, with a combination of Mg2+ and Co2+ or Zn2+ preferred
Co2+
-
26% stimulation of hydrolysis of 4-nitrophenyl phosphate. KM: 0.0022 mM for wild-type enzyme, 0.00051 mM for mutant os-1 enzyme
Co2+
-
50fold increase in activity compared with activity before EDTA treatment
Co2+
-
metalloenzyme, dependent on, can partially be substituted by Mg2+ and Mn2+
Co2+
-
enhances activity, twice as active than with either Zn2+ or Mn2+
Co2+
0.1 mM, 2.4fold increase in activity
Co2+
-
activity is dependent on metal ion, Co2+ is the most active stimulator and has unique effect at high temperature
Cu2+
112% activity at 2 mM
Fe2+
-
2 mM, 2.8fold increase in activity
Fe2+
0.1 mM, 1.25fold increase in activity
K+
-
0.1 M, stimulates
K+
-
the kinetic behaviour is determined by the ratio between concentration of Mn2+ and concentration of Na+ or K+. When the Mn2+ increases and Na+ or K+ decreases, the kinetics show cooperative behaviour
KCl
0.1-0.2 M of NaCl or KCl, 2fold activation
KCl
-
the enzyme is more active in NaCl than with KCl
KCl
-
enzyme exhibits highest activity in presence of 100 mM KCl
Mg2+
-
2 mM, 4.3fold increase in activity
Mg2+
-
metalloenzyme containing Mg2+ and Zn2+ with a molar ratio of 1:2, enzyme exhibits 1.6fold activation in the presenece of 1 mM Co2+
Mg2+
-
10 mM MgSO4, activity is enhanced to 239% of control
Mg2+
-
activation of isoenzyme II and III
Mg2+
-
activates alkaline phosphatase F I
Mg2+
-
activates alkaline phosphatase F II
Mg2+
Mg2+ (5 mM) enhances the enzyme activity by 72%
Mg2+
-
isoenzyme C1, C2, and B2 contain 6 gatoms of Zn per dimer, removal results in loss of activity
Mg2+
-
stimulates, required for maintenance of activity at high concentrations of Na+
Mg2+
required for activity
Mg2+
-
enzyme contains 1 Mg2+ ion per monomer, located near the active site, interacting with phosphate
Mg2+
removal of a third metal ion site near the bimetallo site, containing Mg2+, suggests that the Mg2+ ion participates in general base catalysis. Mg2+ ion stabilizes the transferred phosphoryl group in the transition state, and this interaction is distinct from those mediated by the Zn2+ bimetallo site. Positioning of charged or polar groups to interact with all three nonbridging oxygen atoms of the transferred phosphoryl group is important for catalysis of phosphate monoester hydrolysis
Mg2+
-
bivalent metal ions required, maximal enhancement in presence of Mg2+
Mg2+
a divalent cation is essential, with a combination of Mg2+ and Co2+ or Zn2+ preferred
Mg2+
-
2 mM, 2.1fold stimulation
Mg2+
metal-binding site M3, consisting of residues Asp12, Thr118 and Glu264. Metal-binding site M5 site is composed of at least five chelating O atoms, from the main chain of Gly103, O1 of Asp255 and O2 of Asp257 and two O atoms from water molecules, weakly chelating Mg2+
Mg2+
-
stimulates glycogen synthase phosphatase activity
Mg2+
-
strongly activates hydrolysis of p-nitrophenyl phosphate
Mg2+
metalloenzyme, metal binding site structure
Mg2+
-
80% stimulation of hydrolysis of 4-nitrophenyl phosphate. KM: 0.0036 mM for wild-type enzyme, 0.0084 mM for mutant os-1 enzyme
Mg2+
-
non-essential mixed-type activator, half-maximal effect at 0.007 mM
Mg2+
-
123% activity at 1 mM
Mg2+
-
enhances activity to a lesser extent than Mg2+
Mg2+
-
5 mM, 126% of initial activity
Mg2+
-
partly restores enzymatic activity after EDTA treatment. When Mg2+ is combined with Zn2+, it enhances the catalytic activity up to 3fold
Mg2+
-
20-25% stimulation
Mg2+
-
5 mM, 30-44% stimulation
Mg2+
-
metalloprotein contains Zn2+ and Mg2+, both of which are necessary for catalytic function
Mg2+
-
stimulates activity of extra- and intracellular form
Mg2+
-
2fold activation at 10 mM, dependent on, if 4-nitrophenyl phosphate is used as a substrate, protein phosphatase activity is not Mg2+-dependent
Mg2+
-
activity is greatly enhanced by simultaneous addition of Mg2+ and Zn2+. Maximal specific activity in presence of 20 mM MgCl2 and 5 mM ZnCl2
Mg2+
shrimp
-
metalloenzyme, 1 magnesium ion per monomer, binding structure
Mg2+
-
MgCl2, stimulates slightly
Mg2+
-
metalloenzyme, can partially substitute for Co2+
Mg2+
1 mM, 10fold activation
Mg2+
0.1 mM, 1.3fold increase in activity. 2 mM, 1.6fold increase in activity
Mg2+
-
activity is dependent on metal ion, Co2+, Mg2+ and Zn2+ are the main activators
Mg2+
-
wild-type enzyme most likely has one Mg2+ in the active site in addition to three Mg2+ that bind elsewhere. At 18°C with 10 mM Mg2+, the enzyme activity is completely stable over 160 min. With no Mg2+ in solution, the activity drops to 20% of the initial activity after 160 min
Mg2+
-
contains 1 Mg2+ ion
Mn2+
-
activates alkaline phosphatase F I
Mn2+
-
activates alkaline phosphatase F II
Mn2+
Mn2+ (2 mM) enhances the enzyme activity by 26%
Mn2+
-
the kinetic behaviour is determined by the ratio between concentration of Mn2+ and concentration of Na+ or K+. When the Mn2+ increases and Na+ or K+ decreases, the kinetics show cooperative behaviour
Mn2+
-
2 mM, 1.7fold stimulation
Mn2+
-
stimulates glycogen synthase phosphatase activity
Mn2+
-
5 mM, 133% of initial activity
Mn2+
-
fully restores enzymatic activity after EDTA treatment
Mn2+
-
stimulates activity of extra- and intracellular form
Mn2+
-
metalloenzyme, can partially substitute for Co2+
Mn2+
1 mM, slight activation
Mn2+
0.1 mM, 1.3fold increase in activity
Na+
-
0.1 M, stimulates
Na+
-
the kinetic behaviour is determined by the ratio between concentration of Mn2+ and concentration of Na+ or K+. When the Mn2+ increases and Na+ or K+ decreases, the kinetics show cooperative behaviour
Na+
-
gel filtration fraction is converted to the native structure by Na2SO4 suggesting the importance of Na ion
Na+
-
stimulates activity of extra- and intracellular form
Na+
-
slight activation at 10 mM
NaCl
-
10 mM, activity is enhanced to 151% of control
NaCl
0.1-0.2 M of NaCl or KCl, 2fold activation
NaCl
-
required, the enzyme is more active in NaCl than with KCl
Ni2+
-
2 mM, 1-3fold increase in activity
Ni2+
-
23% stimulation of hydrolysis of 4-nitrophenyl phosphate. KM: 0.0019 mM for wild-type enzyme, 0.0037 mM for mutant os-1 enzyme
Ni2+
-
partly restores enzymatic activity after EDTA treatment
Zn
-
enzyme contains Zn
Zn
-
contains 2 Zn per dimer
Zn
-
enzyme from intestine and kidney contains 4 Zn per dimer
Zn
-
one molecule of enzyme contains 2 atoms of zinc
Zn
-
enzyme from placenta conains 2-3 Zn per dimer
Zn
Micrococcus sodonensis
-
enzyme contains Zn
Zn2+
-
2 mM, 2.1fold increase in activity
Zn2+
-
metalloenzyme containing Mg2+ and Zn2+ with a molar ratio of 1:2
Zn2+
-
activates alkaline phosphatase F I
Zn2+
-
activates alkaline phosphatase F II
Zn2+
118% activity at 5 mM
Zn2+
-
calf enzyme contains 0.2% Zn2+
Zn2+
Fe(III) and Zn(II) binuclear centre
Zn2+
required for activity
Zn2+
-
enzyme contains 2 Zn2+ ions per monomer, located near the active site, interacting with phosphate
Zn2+
metalloenzyme, mutant T59A contains sn amount similar to the wild-type enzyme, while mutant T59R has almost undetectable amounts of bound metal
Zn2+
-
the enzyme employs a binuclear metallocenter of two Zn2+ ions approximately 4 A apart to facilitate catalysis of phosphate monoester hydrolysis. Alkaline phosphatase catalysis is ultrasensitive to charge sequestered between the active site zinc ions
Zn2+
-
strong support for a model in which electrostatic interactions between the bimetallo Zn2+ site and a nonbridging phosphate ester oxygen atom make a significant contribution to the large rate enhancement observed for alkaline phosphatase-catalyzed phosphate monoester hydrolysis
Zn2+
removal of a third metal ion site near the bimetallo site, containing Mg2+, suggests that the Mg2+ ion participates in general base catalysis. Mg2+ ion stabilizes the transferred phosphoryl group in the transition state, and this interaction is distinct from those mediated by the Zn2+ bimetallo site. Positioning of charged or polar groups to interact with all three nonbridging oxygen atoms of the transferred phosphoryl group is important for catalysis of phosphate monoester hydrolysis
Zn2+
-
required for activity
Zn2+
a divalent cation is essential, with a combination of Mg2+ and Co2+ or Zn2+ preferred
Zn2+
metal-binding site M1 site consists of residues Asp269, His273 and His461, in which Zn2+ is chelated by three O and two N atoms with distances of 2.12.5 A. In the metal-binding site M2 residues Asp12, Ser65, Asp311 and His312 Zn2+ is chelated by five O atoms and one N atom with distances of 2.0-2.1 A
Zn2+
-
1 mM, 13% activation
Zn2+
-
the enzyme contains 0.15% Zn2+
Zn2+
-
Zn2+-metalloenzyme
Zn2+
metalloenzyme, metal binding site structure
Zn2+
-
enhances activity to a lesser extent than Mg2+
Zn2+
-
fully restores enzymatic activity after EDTA treatment
Zn2+
-
metalloprotein contains Zn2+ and Mg2+, both of which are necessary for catalytic function
Zn2+
-
stimulates activity of extra- and intracellular form
Zn2+
-
inhibition at 10 mM, activation at 1 mM
Zn2+
-
activity is greatly enhanced by simultaneous addition of Mg2+ and Zn2+. Maximal specific activity in presence of 20 mM MgCl2 and 5 mM ZnCl2
Zn2+
shrimp
-
metalloenzyme, 2 zinc ions per monomer, binding structure
Zn2+
-
metalloenzyme, 0.3 mol zinc per mol of monomer, binding structure
Zn2+
-
can partly substitute for Co2+
Zn2+
1 mM, slight activation
Zn2+
-
activity is dependent on metal ion, Co2+, Mg2+ and Zn2+ are the main activators
Zn2+
-
wild-type enzyme most likely has two Zn2+. Zn2+ release from the active site coincides with total protein structure unfolding
Zn2+
-
contains 2 Zn2+ ions
additional information
enzyme does not require the presence of exogenous divalent cations
additional information
-
enzyme does not require the presence of exogenous divalent cations
additional information
-
metalloenzyme
additional information
-
three metal binding sites
additional information
-
each subunit contains an active centre with three distinct metal binding sites and one phosphorylatable Ser
additional information
-
optimal activity in absence of NaCl
additional information
metal-binding site M4 site is composed of six O atoms from the main chains of Ala45, Lys46, Gly48 and Ser481, the O atom of Ser482 and one water O atom, chelating a metal ion with distances of 2.2-2.7 A
additional information
-
enzyme does not require presence of zinc ions
additional information
-
not affected by monovalent cations
additional information
highly dependent on divalent cations
additional information
-
highly dependent on divalent cations
additional information
-
the SWISS-MODEL program is used to construct a model of isoenzyme rIAP-I. Analysis of the active site of the enzyme and the effect of various combinations of metals at the active site. The model shows the possibility of a Zn triad at the metal-binding position of the active site in rIAP-I
additional information
-
the SWISS-MODEL program is used to construct a model of isoenzyme rIAP-II. Analysis of the active site of the enzyme and the effect of various combinations of metals at the active site
additional information
-
not affected by F- at 10 mM, protein phosphatase activity is not Mg2+-dependent
additional information
-
effect of metal ions, overview
additional information
-
metalloenzyme
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(2Z)-2-(benzoylamino)-3-[2-[4-(trifluoromethyl)phenyl]-1-benzothiophen-3-yl]prop-2-enoate
-
with 0.1 mM 35% remaining activity
(4-methoxyphenyl)[2-(4-methoxyphenyl)-1-benzothiophen-3-yl]methanone
-
with 0.1 mM 70% remaining activity
(E)-N'-(1-(3-(4-fluorophenyl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl)ethylidene)isonicotinohydrazide
-
(E)-N'-(4'-chlorobenzylidene)isonicotinohydrazide
most potent inhibitor for intestinal alkaline phosphatase
(E)-N'-(4-hydroxy-3-methoxybenzylidene)isonicotinohydrazide
most potent inhibitor for tissue-non-specific alkaline phosphatase
1,10-phenanthroline
-
1 mM, irreversibly inactivates the enzyme
1,4-dimethoxy-2-methylbenzene
-
-
1-(2-phenyl-1-benzothiophen-3-yl)methanamine
-
with 0.4 mM 76% remaining activity
1-(3,4-dihydroxyphenyl)-2-(1H-imidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(2-ethyl-1H-imidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-benzimidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-imidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(2-phenyl-1H-imidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-imidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-pyrazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(4H-1,2,4-triazol-4-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(5,6-dimethyl-1H-benzimidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(propan-2-ylamino)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-[(4-methyl-5-phenyl-4H-1,2,4-triazol-3-yl)sulfanyl]ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-[[1-(4-methoxyphenyl)-1H-tetrazol-5-yl]sulfanyl]ethanone
-
-
1-benzothiophen-3-yl 4-fluorophenyl ether
-
with 0.4 mM 78% remaining activity
1-benzothiophen-3-yl(4-methoxyphenyl)methanone
-
with 0.1 mM 40% remaining activity
1-benzothiophen-3-yl(phenyl)methanone
-
with 0.1 mM 43% remaining activity
1-chloro-4-ethoxy-2-methylbenzene
-
-
1-chloro-4-methoxy-2-methylbenzene
-
-
1-fluoro-4-methoxybenzene
-
-
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-ethylpiperazine
-
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-methylpiperazine
-
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]azepane
-
2,4,6-Trinitrobenzenesulfonic acid
-
enzyme loses 80% of its initial activity after incubation for 30 min with 1.0 mM 2,4,6-trinitrobenzenesulfonic acid in bicarbonate buffer, pH 9.0 at 25°C. Increasing concentration can not result in more loss of activity
2,4-dichloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
-
-
2,5-dimethoxy-N-(pyridin-3-yl)benzene-1-sulfonamide
-
2,5-dimethoxy-N-(pyridin-3-yl)benzenesulfonamide
-
-
2,5-dimethoxy-N-(quinolin-3-yl)benzenesulfonamide
-
-
2-(1-benzothiophen-2-yl)aniline
-
with 0.4 mM 70% remaining activity
2-(1-methylhydrazenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(1H-benzimidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
2-(1H-benzimidazol-2-ylamino)-1-(3,4-dihydroxyphenyl)ethanone
-
-
2-(2-chlorophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 63% remaining activity
2-(2-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(2-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(2-methoxyphenyl)-7- trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(2-methylphenyl)-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 5% remaining activity
2-(2-nitrophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.4 mM 78% remaining activity
2-(3,4-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3,5-di-methoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3,5-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-chlorophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 62% remaining activity
2-(3-cyanophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-fluoromethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-formyl-1-benzothiophen-2-yl)benzonitrile
-
with 0.4 mM 79% remaining activity
2-(3-methoxy-1-benzothiophen-2-yl)benzonitrile
2-(3-methoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-nitrophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-phenylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-pyridine)-3-oxime-benzo[b]thiophene
-
with 0.4 mM 71% remaining activity
2-(4-aminophenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-bromo-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
2-(4-bromo-2-methyl-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
2-(4-chlorophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 9% remaining activity
2-(4-chlorophenyl)-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 69% remaining activity
2-(4-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-ethoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-ethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-i-propylphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-methoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-methoxyphenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 37% remaining activity
2-(4-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-trifluoromethoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]piperazin-1-yl)ethanol
-
2-(naphthalen-2-yl)-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 18% remaining activity
2-(pyridin-3-yl)-1-benzothiophene-3-carbaldehyde
-
with 0.4 mM 79% remaining activity
2-([(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)sulfonyl]amino)-N-(2,5-dimethylphenyl)acetamide
potent inhibitor with good selectivity against both placental and tissue-nonspecific alkaline phosphatase, competitive inhibition. A dose of 10 microM completley inhibits the enzyme expressed by transfected COS-1 cells
2-allylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-chloro-1,4-dimethoxybenzene
-
-
2-chloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
-
-
2-cyano-6-methoxy-N-(pyridin-3-yl)benzene-1-sulfonamide
-
2-di-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-ethoxy-5-methyl-N-(pyridin-3-yl)benzenesulfonamide
-
-
2-methoxy-4-nitro-N-(pyridin-3-yl)benzenesulfonamide
-
-
2-methoxy-4-nitro-N-(quinolin-3-yl)benzenesulfonamide
-
-
2-methoxy-5-methyl-N-(pyridin-3-yl)benzene-1-sulfonamide
-
2-methoxy-5-methyl-N-(pyridin-3-yl)benzenesulfonamide
-
-
2-methoxy-5-methyl-N-(quinolin-3-yl)benzenesulfonamide
-
-
2-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-n-pentylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-n-propylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-phenyl-1-benzothiophene-3-carbaldehyde
2-phenyl-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 76% remaining activity
2-phenyl-3-oxime-benzo[b]thiophene
2-phenyl-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-phenyl-benzo[b]thiophene-3-carboxylic acid
-
with 0.4 mM 78% remaining activity
2-[2-(dimethylamino)ethyl]amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-[3-(2,2,2-trifluoroethyl)-1-benzothiophen-2-yl]benzonitrile
-
with 0.1 mM 70% remaining activity
2-[3-(4-chlorophenoxy)-1-benzothiophen-2-yl]benzonitrile
-
with 0.4 mM 79% remaining activity
2-[3-(4-fluorophenoxy)-1-benzothiophen-2-yl]benzonitrile
-
with 0.1 mM 66% remaining activity
2-[4-(1-benzothiophen-3-yl)piperazin-1-yl]phenol
-
with 0.1 mM 49% remaining activity
2-[4-(trifluoromethyl)phenyl]-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 30% remaining activity
2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl]-4-(methoxymethyl)-6-methylpyridine-3-carbonitrile
-
-
3,5-dinitro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
-
-
3-(2,4-dichloro-5-fluorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichloro-5-fluorophenyl)-N,N-dimethyl-1H-pyrazole-5-carboxamide
-
3-(2,4-dichloro-5-fluorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichloro-5-fluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichloro-5-fluorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-1H-pyrazole-5-carbohydrazide
-
3-(2,4-dichlorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N,N-diethyl-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N,N-dimethyl-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(2-methoxyethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(2-methylpropyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(3-methylbutyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(4-hydroxybutyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-difluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
-
3-(3-methoxy-1-benzothiophen-2-yl)pyridine
-
with 0.4 mM 44% remaining activity
3-(3-methoxy-1-benzothiophen-2-yl)quinoline
-
with 0.1 mM 64% remaining activity
3-(4-fluorophenoxy)-1-benzothiophene 1-oxide
-
with 0.4 mM 79% remaining activity
3-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
-
3-methoxy-2-(2-methylphenyl)-1-benzothiophene
-
with 0.1 mM 73% remaining activity
3-methoxy-2-(4-methoxyphenyl)-1-benzothiophene
-
with 0.1 mM 78% remaining activity
3-methoxy-2-[(pyridin-3-yl)sulfamoyl]benzamide
-
3-methoxy-N-(pyridin-3-yl)[1,1'-biphenyl]-2-sulfonamide
-
3-[2-(3,4-dihydroxyphenyl)-2-oxoethyl]-6,7-dimethoxy-2-benzofuran-1(3H)-one
-
-
4-(1-benzothiophen-3-yloxy)benzaldehyde
-
with 0.1 mM 9% remaining activity
4-(4-aminophenylazo)-phenylarsonic acid
-
-
4-bromo-2,5-dimethoxy-N-(pyridin-3-yl)benzenesulfonamide
-
-
4-chloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
-
-
4-chloroanilidophosphonate
-
-
4-fluoro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
-
-
4-methoxy-1,2-dimethylbenzene
-
-
4-methoxy-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
-
-
4-[(1-oxido-1-benzothiophen-3-yl)oxy]benzonitrile
-
with 0.4 mM 67% remaining activity
4-[[(4,6-dimethylpyrimidin-2-yl)amino]methyl]benzene-1,2-diol
-
-
4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]morpholine
-
5-((5-chloro-2-methoxyphenyl)sulfonamido)nicotinamide
SBI-425, potent inhibitor
5-bromo-2-methoxy-N-(quinolin-3-yl)benzenesulfonamide
-
-
5-chloro-2-ethoxy-N-(pyridin-3-yl)benzenesulfonamide
-
-
5-chloro-2-methoxy-N-(pyridin-3-yl)benzene-1-sulfonamide
-
5-chloro-2-methoxy-N-[5-(2-methylphenyl)pyridin-3-yl]benzene-1-sulfonamide
-
5-chloro-2-methoxy-N-[5-(3-methylphenyl)pyridin-3-yl]benzene-1-sulfonamide
-
5-chloro-2-methoxy-N-[5-(4-methoxyphenyl)pyridin-3-yl]benzene-1-sulfonamide
-
5-chloro-2-methoxy-N-[5-(4-methylphenyl)pyridin-3-yl]benzene-1-sulfonamide
-
5-chloro-2-methoxy-N-[5-(4-methylpiperazine-1-carbonyl)pyridin-3-yl]benzene-1-sulfonamide
-
5-chloro-N-[5-(4-chlorophenyl)pyridin-3-yl]-2-methoxybenzene-1-sulfonamide
-
5-methyl-3-[3-[3-(trifluoromethyl)phenyl]prop-2-yn-1-yl]oxolan-2-one
-
5-[(5-bromo-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxamide
-
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]-N-ethylpyridine-3-carboxamide
-
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]-N-methylpyridine-3-carboxamide
-
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]-N-phenylpyridine-3-carboxamide
-
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxamide
SBI-425, potent inhibitor
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxylic acid
-
5-[(5-fluoro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxamide
-
5-[[2-methoxy-5-(trifluoromethoxy)benzene-1-sulfonyl]amino]pyridine-3-carboxamide
-
5-[[5-chloro-2-(trifluoromethoxy)benzene-1-sulfonyl]amino]pyridine-3-carboxamide
-
6-(1-benzofuran-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
-
6-(1-benzothiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
-
with 0.4 mM 19% remaining activity
6-(1-benzothiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole
-
with 0.4 mM 11% remaining activity
6-(5-nitro-1-benzothiophen-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
-
6-(thiophen-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
-
6-(thiophen-2-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
-
6-(thiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
-
6-(thiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
-
6-(thiophen-3-yl)-2,3-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
-
6-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
-
6-(thiophen-3-yl)imidazo[2,1-b][1,3]thiazole hydrochloride
-
-
Ag2+
-
1 mM, complete inactivation
alendronate
-
0.01-0.1 mM, coincubation with excess Zn2+ or Mg2+ completely abolish inhibition
artemether
-
6 mg/l artemether has significant inhibitory effects on extracellular enzyme activity
aspirin
-
2 mM, 84% inhibition
bis(1,1,1-trifluoroacetylacetonato)oxovanadium(IV)
-
-
bis(3-chloroacetylacetonato)oxovanadium(IV)
-
-
bis(3-chloroacetylacetonato)oxovanadium(IV)(4-Mepy)
-
-
bis(3-methylacetylacetonato)oxovanadium(IV)
-
-
bis(acetylacetonato)oxovanadium(IV)
-
-
bis(acetylacetonato)oxovanadium(IV)(4-Mepy)
-
-
bis(benzoylacetonato)oxovanadium(IV)
-
-
butanol
-
reversible noncompetitive
CaCl2
-
1 mM, 32% inhibition
Caffeine
-
uncompetitive inhibition
CN-
-
complete inhibition at 10 mM
CO2
-
enzyme in buffer can be inactivated by COS treatment at atmospheric pressure, increasing inactivation, when temperature increases from 20°C to 50°C, 16% loss of activity after 30 min at 20°C, 81% loss of activity after 30 min at 50°C. Change in activity dependent on CO2 treatment is not observed in raw milk mainly due to strong buffering capacity of milk
Cry1Ac toxin
environment friendly insecticidal crystal proteins encoded by the spore-forming bacteria Bacillus thuringiensis. Competitive inhibitor; environment friendly insecticidal crystal proteins encoded by the spore-forming bacteria Bacillus thuringiensis. Competitive inhibitor
-
CuCl2
-
10 mM, 24% inhibition
CuSO4
-
10 mM, 71% inhibition
diethyl-p-nitrophenyl phosphate
-
-
dihydroartemisinin
-
24 mg/l dihydroartemisinin has significant inhibitory effects on extracellular enzyme activity
ethanol
-
reversible noncompetitive
ethylene glycol
-
reversible noncompetitive
Glutaraldehyde
-
1%, 65% inactivation
guanidine hydrochloride
-
inactivation of the enzyme by GuHCl (guanidine hydrochloride) is a slow, reversible reaction with fractional remaining activity. The microscopic rate constants are determined. The enzyme is protected by the substrate to a certain extent during guanidine denaturation. The changes of conformation of the enzyme in different concentrations of GuHCl are studied. The inactivation occurs before the noticeable conformational changes of the enzyme molecule as a whole can be detected, which suggests that the active site of the enzyme has more flexibility than the whole enzyme molecule
heparin
-
histone phosphatase activity
imidazole
-
uncompetitive inhibition
Imipenem
inhibition is time dependent reaching about 98% in 30 min on ice at 1.2 mM and 95% at 0.24 mM
K+
-
90% residual activity at 4 mM
KNO3
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
KPF6
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
L-amino acids
specific uncompetitive inhibition, molecular mechanism involves Arg166 and Glu429
lansoprazole
-
uncompetitive
lectin
5 g/L, precipitation by lectin: 100%; 5 g/L, precipitation by lectin: 100%; 5 g/L, precipitation by lectin: 100%, bone isoenzyme; 5 g/L, precipitation by lectin: 58%, isoenzyme rTI2B; 5 g/L, precipitation by lectin: 76%, isoenzyme rTI2A
-
Leu
-
L-Leu, uncompetitive, D-Leu with greatly decreased efficiencies
Li+
-
83% residual activity at 5 mM
methyl (2E)-2-(benzoylamino)-3-[2-(4-methoxyphenyl)-1-benzothiophen-3-yl]prop-2-enoate
-
with 0.1 mM 77% remaining activity
methyl 3-(1-benzothiophen-3-yl)-N-benzoylalaninate
-
with 0.4 mM 74% remaining activity
methyl 3-methoxy-2-[(pyridin-3-yl)sulfamoyl]benzoate
-
methyl 5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxylate
-
methyl N-benzoyl-3-[2-[4-(trifluoromethyl)phenyl]-1-benzothiophen-3-yl]alaninate
-
with 0.1 mM 63% remaining activity
MnO4-
-
competitive inhibition
N'-[(Z)-(2-hydroxyphenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(3-nitrophenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(4-bromophenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(4-fluorophenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(4-methoxyphenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(pyridin-3-yl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(pyridin-4-yl)methylidene]pyridine-4-carbohydrazide
-
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)acetamide
-
-
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)butyramide
-
-
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)heptanamide
-
-
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)octanamide
-
-
N-(2-hydroxyethyl)-3-(2,3,4-trichlorophenyl)-1H-pyrazole-5-carboxamide
N-(2-hydroxyethyl)-3-(2,4,5-trifluorophenyl)-1H-pyrazole-5-carboxamide
-
N-(3-cyanophenyl)-3-([(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)sulfonyl]amino)propanamide
potent inhibitor with good selectivity against both placental and tissue-nonspecific alkaline phosphatase
N-([3,3'-bipyridin]-5-yl)-2,5-dimethoxybenzene-1-sulfonamide
-
N-([3,3'-bipyridin]-5-yl)-5-chloro-2-methoxybenzene-1-sulfonamide
-
N-([3,4'-bipyridin]-5-yl)-2,5-dimethoxybenzene-1-sulfonamide
-
N-([3,4'-bipyridin]-5-yl)-5-chloro-2-methoxybenzene-1-sulfonamide
-
N-tert-butyl-3-(2,4-dichlorophenyl)-1H-pyrazole-5-carboxamide
-
Na+
-
91% residual activity at 5 mM
Na2SO4
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
Na2[W2O3(O2)4(glycyl-glycine)2](3H2O)
-
-
Na2[W2O3(O2)4(glycyl-leucine)2](3H2O)
-
-
NaBF4
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
NaNO3
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
NaWO4
-
1 mM NaWO4, 35% inhibition of isoenzyme I, 80% inhibition of isoenzyme II, 14% inhibition of isoenzyme III
Na[VO(O2)2(asparagine)]H2O
-
-
Na[VO(O2)2(glutamine)]H2O
-
-
Na[VO(O2)2(glycyl-glycine)(H2O)]H2O
-
-
Na[VO(O2)2(triglycine)]3H2O
-
-
p-chloromercuribenzoate
-
0.1-0.2 mM, 85%-100% inhibition
p-nitrophenyl phosphorothioate
-
-
pamidronate
-
0.01-0.1 mM, coincubation with excess Zn2+ or Mg2+ completely abolish inhibition
PCMB
-
1 mM, 54% inhibition of isoenzyme I, 33% inhibition of isoenzyme II, 9% inhibition of isoenzyme III
Phenylglyoxal
-
1.0 mM, complete irreversible inactivation after 30 min in bicarbonate buffer, pH 9.0, at 25°C
phenylphosphonate
-
10 mM, 47% inhibition of p-nitrophenyl phosphate hydrolysis, 80% inhibition of dephosphorylation of P-labelled histones
polylysine
-
histone phosphatase activity
polyphenol-rich beverages
-
21% inhibition
-
progesterone
-
0.5 mM, 29% inhibition
Propanol
-
reversible noncompetitive
protamine
-
histone phosphatase activity
SH-group blocking agents
-
-
-
Sodium acetate
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
Sodium citrate
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
sodium deoxycholate
-
1 mM, 20% inhibition
thymidine 5'-O-phosphorothioate
-
-
uridine 5'-O-phosphorothioate
-
-
VO3-
-
1 mM, 78% inhibition
WO4 3-
-
competitive inhibition, product analogue
zoledronate
-
0.01-0.1 mM, coincubation with excess Zn2+ or Mg2+ completely abolish inhibition
[WO(O2)2(glycyl-glycine)(H2O)]3H2O
-
-
[WO(O2)2(glycyl-glycine)](3H2O)
-
-
[WO(O2)2(glycyl-leucine)](3H2O)
-
-
[WO(O2)2(triglycine)]3H2O
-
-
1-bromotetramisole
-
-
2-(3-methoxy-1-benzothiophen-2-yl)benzonitrile
-
with 0.1 mM 57% remaining activity
2-(3-methoxy-1-benzothiophen-2-yl)benzonitrile
-
with 0.4 mM 79% remaining activity
2-iodo-1-benzothiophene
-
with 0.1 mM 41% remaining activity
2-iodo-1-benzothiophene
-
with 0.4 mM 54% remaining activity
2-mercaptoethanol
-
the P2 isoenzyme is more sensitive to 2-mercaptoethanol than P1
2-mercaptoethanol
-
10 mM, 70% decrease in activity
2-mercaptoethanol
68% inhibition at 1 mM, 86% inhibition at 10 mM
2-phenyl-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 41% remaining activity
2-phenyl-1-benzothiophene-3-carbaldehyde
-
with 0.4 mM 77% remaining activity
2-phenyl-3-oxime-benzo[b]thiophene
-
with 0.1 mM 1% remaining activity
2-phenyl-3-oxime-benzo[b]thiophene
-
with 0.4 mM 68% remaining activity
arsenate
-
1 mM Na2HAsO4, 80% inhibition of isoenzyme I, 22% inhibition of isoenzyme II, 40% inhibition of isoenzyme III
arsenate
-
irreversible inhibitor
Ba2+
-
1 mM, 95% inhibition of isoenzyme I
Ba2+
30% residual activity at 5 mM
Be2+
-
-
Borate
-
1 mM H3BO4, 16% inhibition of isoenzyme I, 13% inhibition of isoenzyme II, 8% inhibition of isoenzyme III
Ca2+
-
weak inhibition of isoenzyme II
Ca2+
-
1 mM, 50% inhibition
Ca2+
-
10 mM, glycogen synthase phosphatase activity
Ca2+
-
in presence of 0.005 mM Mg2+, Ca2+ acts as an uncompetitive inhibitor, at 0.1 mM Mg2+, Ca2+ inhibits non-competitively
Ca2+
-
83% residual activity at 5 mM
Ca2+
17% inhibition at 1 mM
Ca2+
2 mM, 16% inhibition
Cd2+
-
5 mM, 30% inhibition
Cd2+
-
1 mM, complete inactivation
Cd2+
-
5 mM, 16% residual activity
Cd2+
-
chronic cadmium exposure (32.5 ppm Cd2+ in purified water over 3 months) leads to noncompetitive inhibition of serum and hepatic enzyme activity. The addition of 5 mM of Zn2+ shows almost 58% reactivation of the enzyme
Cd2+
-
39% inhibition of the enzyme at 1 mM in the gills, but not in digestive gland
Cd2+
-
non-competitive inhibition
Co2+
-
5 mM, 60% inhibition
Co2+
-
1 mM, 54% inhibition
Co2+
-
5 mM, 20% residual activity
Co2+
2 mM, 25% inhibition
corticosterone
-
2 mM, 13% inhibition
corticosterone
-
5 mM, 90% inhibition of alkaline phosphatase grown in high phosphate medium, no effect is observed with alkaline phosphatase grown in low phosphate medium
Cu2+
-
2 mM, 21% inhibition
Cu2+
-
1 mM, 87% inhibition of isoenzyme I, 10% inhibition of isoenzyme III
Cu2+
-
5 mM, 40% inhibition
Cu2+
-
1 mM, 70% inhibition
Cu2+
-
1.0 mM, 82% inhibition, levamisole-insensitive alkaline phosphatase activity; 1.0 mM, almost complete inhibition, levamisole-sensitive alkaline phosphatase activity
Cu2+
-
complete inhibition at 2 mM
Cu2+
-
5 mM, 2% residual activity
Cu2+
28% inhibition at 1 mM
Cu2+
2 mM, 29% inhibition
Cys
-
L-Cys
Cys
-
uncompetitive inhibition of phosphatase activity, mixed-competitive inhibition of inorganic pyrophosphatase activity. Inorganic pyrophosphatase activity is inhibited more than phosphatase activity. Ca2+ and Mg2+ ion concentrations may regulate this inhibition
dithiothreitol
-
-
dithiothreitol
-
10 mM, 95% decrease in activity
DTT
-
-
DTT
nearly complete inhibition at 2 mM
EDTA
-
-
EDTA
antarctic bacterium
-
0.1 mM, 50% inhibition
EDTA
-
10 mM, 71% inhibition
EDTA
-
inhibition of isoenzyme I and II
EDTA
-
alkaline phosphatase F I; alkaline phosphatase F II
EDTA
-
1 mM, 83% inhibition
EDTA
10 mM, 99% inhibition
EDTA
-
5 mM, 70% inhibition
EDTA
-
1 mM, complete inactivation
EDTA
-
optimal reactivation by Zn2+ or Co2+. The Zn2+-reactivated enzyme is stable, the Co2+-apoenzyme is not
EDTA
0.01 mM, complete inhibition. Ca2+ is the best metal ion to reconstitute enzyme activity, followed by Co2+, Ni2+, Mn2+, and Mg2+. Zn2+, in contrast, failed to restore enzyme activity
EDTA
-
5 mM, 27% inhibition
EDTA
-
inhibition is reversed by divalent cations
EDTA
90% inhibition at 1 mM
EDTA
-
completely deactivates the enzyme
EDTA
-
90% inhibition at 1 mM and 25°C, complete inhibition at 0.1 mM EDTA and 90°C
EDTA
-
inactivation of the native, but not of the recombinant enzyme, inhibition of the native enzyme is reversible by divalent metal ions, best effect with Co2+
EDTA
-
inactivation after 1 h at 1 mM
EGTA
-
-
EGTA
82% inhibition at 1 mM
F-
-
1 mM NaF, 74% inhibition of isoenzyme I, 15% inhibition of isoenzyme II
F-
-
50 mM KF, 13% inhibition of p-nitrophenyl phosphate hydrolysis, 50% inhibition of dephosphorylation of P-labelled histones
Fe2+
10% residual activity at 5 mM
Fe2+
2 mM, 89% inhibition
glycerol
-
concentrations of 10%, 20% and 40% inhibit the activity by 35%, 60%, and 90%
glycerol
complete inhibition at 30% (v/v)
Hg2+
-
1 mM nearly complete inhibition of isoenzyme I, II and III
Hg2+
-
1 mM, complete inactivation
Hg2+
-
complete inhibition at 2 mM
Hg2+
-
1 mM, 82% loss of activity
HgCl2
-
10 mM, 74%inhibition
HgCl2
-
alkaline phosphatase F I; alkaline phosphatase F II
histidine
-
-
inorganic phosphate
-
isatin
-
competitive
KCl
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
KCl
90% remaining activity
L-homoarginine
-
83% inhibition at 10 mM for all three isozymes
L-homoarginine
-
high sensitivity of the liver/bone/kidney isoenzyme
L-homoarginine
-
marked inhibition of the liver enzyme at concentrations which produce only slight inhibition of placental enzyme
L-homoarginine
-
inhibition of an isozyme from the lower part of intestine
L-homoarginine
-
powerful inhibitor of the bone/liver/kidney isoenzyme and for the osteosarcoma cell enzyme
L-leucine
-
allozyme D is highly sensitive and shows uncompetitive inhibition, allozymes S and F are less sensitive, allozymes SD and FD, mixed type, respond in an intermediate fashion to inhibition
L-leucine
-
uncompetitive inhibition
L-Phe
-
1 mM, 13% inhibition
L-Phe
-
mixed-type inhibition
L-Phe
-
maximal ainhibition at 1 mM. D-Phe has no effect
L-Phe-Gly-Gly
-
high sensitivity of the intestinal and placental isoenzyme
L-Phe-Gly-Gly
-
marked inhibition of the placental enzyme at concentrations which produce only slight inhibition of liver enzyme
L-phenylalanine
-
L-phenylalanine
-
the P2 isoenzyme is more sensitive to L-phenylalanine than P1
L-phenylalanine
inhibitor of intestinal alkaline phosphatase
L-phenylalanine
10 mM, 100% inhibition; 10 mM, 100% inhibition; 10 mM, 37% inhibition; 10 mM, 37% inhibition, bone isoenzyme; 10 mM, 62% inhibition, isoenzyme rTI2A; 10 mM, 70% inhibition, isoenzyme rTI2B
L-phenylalanine
-
2 mM, 24% inhibition
L-phenylalanine
-
uncompetitive inhibition
levamisole
-
levamisole
-
complete inhibition of the seminal plasma enzyme at 4.2 mM
levamisole
-
noncompetitive
levamisole
-
96-98% inhibition at 1 mM for all three isozymes
levamisole
inhibitor of tissue non-specific alkaline phosphatase
levamisole
-
10 mM, 94% inhibition of p-nitrophenyl phosphate hydrolysis, 82% inhibition of dephosphorylation of P-labelled histones
levamisole
-
inhibits brush border membrane enzyme activity in the upper villus but is less effective in the middle villus and has no effect on alkaline phosphatase activity in the mucus gel
levamisole
-
0.5 mM, 91% inhibition
levamisole
-
hydrolysis of pyrophosphate by rat aortic rings is inhibited about half by the nonspecific alkaline phosphatase inhibitor levamisole. Hydrolysis is increased in aortic rings from uremic rats and all of this increase is inhibited by levamisole
levamisole
-
with 0.4 mM 10% remaining activity
Mg2+
-
weak inhibition of isoenzyme I
Mg2+
-
1 mM, 19% inhibition
Mg2+
-
93% residual activity at 5 mM
Mn2+
-
2 mM, 24% inhibition
Mn2+
-
1 mM 90% inhibition of isoenzyme I, 64% inhibition of isoenzyme II, 39% inhibition of isoenzyme III
Mn2+
-
1 mM, 43% inhibition
Mn2+
2 mM, 32% inhibition
Mo2+
-
1 mM, 50% inhibition
Mo2+
-
5 mM, 61% residual activity
molybdate
-
-
molybdate
-
10 mM, activity of heat-shocked induced phosphatase: -33%
molybdate
slight inhibition at 10 mM
N-(2-hydroxyethyl)-3-(2,3,4-trichlorophenyl)-1H-pyrazole-5-carboxamide
-
N-(2-hydroxyethyl)-3-(2,3,4-trichlorophenyl)-1H-pyrazole-5-carboxamide
-
NaCl
-
reduces enzymatic activity and significantly decreased Vmax/Km ratio
NaCl
-
2.0 M, 71% loss of activity
NaCl
2 M, 60% remaining activity
NaCl
-
1 M, inhibition of enzyme form CAPase
NaCl
-
200 mM, 30% inhibition
NaCN
-
-
NaF
-
alkaline phosphatase F I; alkaline phosphatase F II
NEM
-
-
Ni2+
-
Ni2+
-
5 mM, 27% inhibition
Ni2+
56% inhibition at 1 mM
orthovanadate
-
-
orthovanadate
-
70% inhibition at 1 mM, competitive
p-hydroxymercuribenzoate
-
reactivation by DTT and 2-mercaptoethanol
p-hydroxymercuribenzoate
-
-
Pb2+
30% residual activity at 5 mM
Pb2+
-
complete inhibition at 2 mM
Phe
-
-
Phe
-
enzyme from intestine is inhibited, enzyme from liver not
Phe
-
marked inhibition of the placental enzyme at concentrations which produce only slight inhibition of liver enzyme
Phe
-
L-Phe, uncompetitive, D-Phe with greatly decreased efficiencies
Phe
-
20 mM, 82-99% inhibition of the soluble enzyme form, 68-95% inhibition of the particulate enzyme form
phenyl phosphonate
-
-
phenyl phosphonate
-
competitive
phosphate
-
competitive inhibitor
phosphate
-
1 mM Na2HPO4, 74% inhibition of isoenzyme I, 15% inhibition of isoenzyme II, 2% inhibition of isoenzyme III; competitive
phosphate
-
competitive inhibitor
phosphate
-
2.5 mM, activity of heat-shocked induced phosphatase: -64%
phosphate
-
competitive inhibition
phosphate
competitive inhibitor
phosphate
-
competitive inhibition of both enzyme forms
phosphate
-
product inhibition
phosphate
-
competitive inhibition
SDS
-
-
SDS
complete inhibition at 5% (w/v)
Sr2+
-
1 mM, 88% inhibition of isoenzyme I
Tartrate
-
weak inhibition at 10 mM
Tartrate
-
5.9% inhibition at 1 mM
theophylline
-
theophylline
-
reversible non-competitive inhibitor
theophylline
-
2 mM, 77% inhibition
thioglycolic acid
-
combined treatment with thioglycolic acid, 0.175%, and 6 M urea leads to reduction of disulfide bonds, loss of activity and separation into subunits
tungstate
-
-
tungstate
competitive inhibitor
Urea
-
combined treatment with thioglycolic acid, 0.175%, and 6 M urea leads to reduction of disulfide bonds, loss of activity and separation into subunits
Urea
-
reversible inactivation. At low concentrations of urea, the first detected alteration in properties is an increase in the activity of the enzyme. This is followed by inactivation and the release of half of the zinc content when the amount of urea reaches levels of 2 M. Intrinsic tryptophan fluorescence and circular dichroism ellipticity change in the range 2.5 to 8 M urea, signalling dimer dissociation, followed by one major monomer unfolding transition at 6-8 M urea as indicated by ANS fluorescence and KI fluorescence quenching
Urea
3 mM, 100% inhibition; 3 mM, 100% inhibition; 3 mM, 68% inhibition, bone isoenzyme; 3 mM, 70% inhibition, isoenzyme rTI2B; 3 mM, 71% inhibition; 3 mM, 80% inhibition, isoenzyme rTI2A
vanadate
-
-
vanadate
10 mM, 89% inhibition
vanadate
-
1 mM, 22% inhibition of alkaline phosphatase grown in high phosphate medium
Zn2+
antarctic bacterium
-
-
Zn2+
-
1 mM, 98% inhibition of isoenzyme I
Zn2+
-
5 mM, complete inhibition
Zn2+
-
1 mM, 67% inhibition
Zn2+
-
mutant H412Y in presence of a phosphoryl group acceptor and Zn2+ at 0.1 mM
Zn2+
-
non-competitive inhibition
Zn2+
-
2 mM, 90% inhibition
Zn2+
-
5 mM, 5% residual activity
Zn2+
-
inhibition at 10 mM, activation at 1 mM
Zn2+
-
about 30% inhibition at 1 mM in gill, mantle, and siphon
Zn2+
2 mM, 51% inhibition
Zn2+
-
complete inhibition at 15 mM
ZnCl2
-
10 mM, 58% inhibition
ZnCl2
-
0.01 mM, activity of heat-shocked induced phosphatase: -82%
ZnCl2
-
1 mM, 16% inhibition
additional information
-
iodoacetamide and NaN3 at 2-10 mM concentration have no effect on activity
-
additional information
not inhibitory: EDTA
-
additional information
-
not inhibitory: EDTA
-
additional information
-
tartrate-rsistant
-
additional information
Zn2+ and Mg2+ do not affect the mutant T59R enzyme
-
additional information
-
Zn2+ and Mg2+ do not affect the mutant T59R enzyme
-
additional information
enzyme is resistant to urea and dithioreitol
-
additional information
-
enzyme is resistant to urea and dithioreitol
-
additional information
-
no inhibition at 10 mM by L-phenylalanine at 10 mM for all three isozymes
-
additional information
-
enzyme is sensitive to environmental salinity
-
additional information
-
with increase in concentration of the inhibitor complexes from 0.005 to 0.04 mM, an increase in Km value is observed. Each of the inhibitors serves as a mixed type of inhibitor of ALP, combining competitive and noncompetitive modes of inhibition
-
additional information
-
highly resistant to okadaic acid
-
additional information
no inhibition by molybdate and vanadate
-
additional information
-
no inhibition by molybdate and vanadate
-
additional information
-
inhibition level is tissue-dependent
-
additional information
not inhibitory: ertapenem, meropenem, ampicillin or penicillin G
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.01 - 0.177
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate
0.026 - 0.078
2-naphthyl phosphate
0.037 - 0.1159
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
0.00000001 - 49.7
4-nitrophenyl phosphate
0.44
Alpha-naphthyl phosphate
-
pH 8.9, 37°C
0.3 - 3.35
beta-Glycerophosphate
2.46
beta-glyceryl phosphate
-
pH 8.9, 37°C
2.22 - 4.8
glucose 1-phosphate
1.49
glucose 6-phosphate
-
-
0.47
L-histidinyl phosphate
-
pH 8.9, 37°C
0.806
O-Phosphotyrosine
-
0.0094 - 5.02
p-nitrophenyl phosphate
0.348
paraoxon
-
pH 7.4, 37°C
6.1 - 23.81
Phenyl phosphate
0.39 - 0.9
phospho-DL-Thr
0.4 - 0.72
phospho-DL-Tyr
0.38 - 0.68
phospho-L-Ser
0.145
phosphoenolpyruvate
-
2.9
Phosphoethanolamine
-
-
0.12
pyridoxal 5'-phosphate
-
allozyme D, pH 7.5, 37°C, in presence of Mg2+ and Zn2+
0.2 - 0.37
pyridoxal phosphate
1.47
trehalose 6-phosphate
-
-
additional information
4-nitrophenyl phosphate
0.01
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate
-
-
0.085
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate
-
-
0.177
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate
-
-
0.026
2-naphthyl phosphate
-
purified enzyme
0.078
2-naphthyl phosphate
-
membrane-bound enzyme enzyme
0.037
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
layer-by-layer single-stack, immobilized ALP
0.04
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
direct physical adsorption, immobilized ALP
0.04
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
immobilized ALP
0.05
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
free ALP
0.1058
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
layer-by-layer multi-stack, immobilized ALP
0.114
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
glutaraldehyde X-link DAH, immobilized ALP
0.1159
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
glutaraldehyde X-link, immobilized ALP
0.00000001
4-nitrophenyl phosphate
-
Vmax (mmol/min mg of protein): 1.8 (dimer), 0.42 (tetramer)
0.00000035
4-nitrophenyl phosphate
-
-
0.00000035
4-nitrophenyl phosphate
pH: 8.5
0.00026
4-nitrophenyl phosphate
-
-
0.0003
4-nitrophenyl phosphate
-
at pH 11.0 and 25°C
0.00034
4-nitrophenyl phosphate
-
-
0.00036
4-nitrophenyl phosphate
wild type enzyme, at pH 8.0 and 25°C
0.0005
4-nitrophenyl phosphate
mutant enzyme E332Y, at pH 8.0 and 25°C
0.0021
4-nitrophenyl phosphate
mutant enzyme R166S/E322Y/K328A, at pH 8.0 and 25°C
0.0022
4-nitrophenyl phosphate
mutant enzyme E322Y/K328A, at pH 8.0 and 25°C
0.0024
4-nitrophenyl phosphate
mutant enzyme D153A/K328A, at pH 8.0 and 25°C
0.0026
4-nitrophenyl phosphate
mutant enzyme D153A, at pH 8.0 and 25°C
0.0035
4-nitrophenyl phosphate
-
mutant S105L, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.0036
4-nitrophenyl phosphate
mutant enzyme D101A, at pH 8.0 and 25°C
0.0048
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A, at pH 8.0 and 25°C
0.005
4-nitrophenyl phosphate
-
mutant T155M, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.005
4-nitrophenyl phosphate
mutant enzyme R166S, at pH 8.0 and 25°C
0.0053
4-nitrophenyl phosphate
mutant enzyme R166S/D153A, at pH 8.0 and 25°C
0.0054
4-nitrophenyl phosphate
mutant enzyme K328A, at pH 8.0 and 25°C
0.0062
4-nitrophenyl phosphate
mutant enzyme D101A/D153A, at pH 8.0 and 25°C
0.0073
4-nitrophenyl phosphate
-
mutant H412Y, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.0073
4-nitrophenyl phosphate
-
25°C, pH 8, mutant enzyme T81A
0.0078
4-nitrophenyl phosphate
-
25°C, pH 8, wild-type enzyme
0.0083
4-nitrophenyl phosphate
-
IAPase
0.0084
4-nitrophenyl phosphate
mutant enzyme D101A/R166S, at pH 8.0 and 25°C
0.0094
4-nitrophenyl phosphate
-
wild-type enzyme, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.0095
4-nitrophenyl phosphate
-
mutant E341K, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.0097
4-nitrophenyl phosphate
-
mutant S105L, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.011
4-nitrophenyl phosphate
-
mutant E322K, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.011
4-nitrophenyl phosphate
mutant enzyme D101A/D153A/K328A, at pH 8.0 and 25°C
0.012
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A/E322Y, at pH 8.0 and 25°C
0.0145
4-nitrophenyl phosphate
-
pH 8, 25°C, in the presence of phosphate acceptor (1 M Tris-HCl buffer)
0.0156
4-nitrophenyl phosphate
-
37°C, pH 7.4, 1 mM Ca2+
0.0176
4-nitrophenyl phosphate
-
mutant D369N, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.019
4-nitrophenyl phosphate
-
37°C, pH 7.4, with Ca2+ and Mg2+
0.019
4-nitrophenyl phosphate
-
at pH 9.0 and 25°C
0.0211
4-nitrophenyl phosphate
-
wild-type enzyme, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.0218
4-nitrophenyl phosphate
pH 8.0, 25°C, recombinant wild-type enzyme
0.0221
4-nitrophenyl phosphate
-
mutant E322K, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.0249
4-nitrophenyl phosphate
pH 8.0, 25°C, recombinant mutant T59A
0.025
4-nitrophenyl phosphate
-
at pH 8.0 and 25°C
0.026
4-nitrophenyl phosphate
-
with 0.5 M NaCl, at pH 8.0 and 25°C
0.027
4-nitrophenyl phosphate
-
37°C, pH 7.4, 1 mM Ca2+, 1 mM Mg2+
0.027
4-nitrophenyl phosphate
mutant enzyme R166S/E322Y, at pH 8.0 and 25°C
0.028
4-nitrophenyl phosphate
-
isozyme B2, pH 8.8
0.02982
4-nitrophenyl phosphate
single-chain Fv antibody fusion protein
0.0315
4-nitrophenyl phosphate
-
0.034
4-nitrophenyl phosphate
75°C
0.034
4-nitrophenyl phosphate
-
isozyme B1, pH 8.8
0.035
4-nitrophenyl phosphate
-
37°C, pH 7.4, 1 mM Mg2+
0.037
4-nitrophenyl phosphate
-
-
0.0374
4-nitrophenyl phosphate
-
mutant E341K, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.038
4-nitrophenyl phosphate
-
isozyme B/I, pH 8.8
0.039
4-nitrophenyl phosphate
-
25°C, pH 8.0, mutant enzyme G51C
0.039
4-nitrophenyl phosphate
80°C, pH 12
0.0392
4-nitrophenyl phosphate
pH 8.0, 25°C, recombinant mutant T59R
0.045
4-nitrophenyl phosphate
25°C, pH 18.0, Tris-HCl buffer
0.046
4-nitrophenyl phosphate
-
25°C, pH 8.0, mutant enzyme I50C
0.05
4-nitrophenyl phosphate
-
-
0.05
4-nitrophenyl phosphate
-
-
0.052
4-nitrophenyl phosphate
mutant enzyme D153A/E322Y, at pH 8.0 and 25°C
0.057
4-nitrophenyl phosphate
-
CAPase
0.057
4-nitrophenyl phosphate
-
mutant T155M, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.058
4-nitrophenyl phosphate
-
25°C, pH 8.0, mutant enzyme S52C
0.059
4-nitrophenyl phosphate
-
25°C, pH 8.0, mutant enzyme S53C
0.0597
4-nitrophenyl phosphate
-
mutant D369N, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.06
4-nitrophenyl phosphate
-
10°C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
0.061
4-nitrophenyl phosphate
-
with 0.5 M NaCl, at pH 9.0 and 25°C
0.062
4-nitrophenyl phosphate
-
pH 9.5, 70°C, wild-type enzyme
0.063
4-nitrophenyl phosphate
mutant enzyme R166S/K328A, at pH 8.0 and 25°C
0.0691
4-nitrophenyl phosphate
-
mutant D434E, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.07
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.05 M diethanolamine
0.074
4-nitrophenyl phosphate
-
in absence of Mg2+
0.078
4-nitrophenyl phosphate
mutant enzyme D101A/E322Y/K328A, at pH 8.0 and 25°C
0.081
4-nitrophenyl phosphate
at pH 10.5 and 70°C
0.082
4-nitrophenyl phosphate
-
pH 9.5, 37°C, Vmax: 0.96 nmol/min/mg enzyme, CIAP immobilized enzyme reactor (in excellent agreement with a Km value of calf ALP enzyme using a 96-well microplate reader)
0.087
4-nitrophenyl phosphate
pH 9.5, 50°C, Vmax: 0.049 micromol/min/mg
0.09
4-nitrophenyl phosphate
-
in presence of Mg2+
0.09
4-nitrophenyl phosphate
-
pH 10.5, mutant V406A
0.09
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.05 M methylamine
0.093
4-nitrophenyl phosphate
-
pH 8.0, 65°C
0.11
4-nitrophenyl phosphate
-
allozyme D, pH 9.8, in presence of Mg2+ and Zn2+
0.11
4-nitrophenyl phosphate
-
37°C, native enzyme
0.11
4-nitrophenyl phosphate
-
25°C, pH 8.0, wild-.type enzyme
0.12
4-nitrophenyl phosphate
-
37°C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
0.13
4-nitrophenyl phosphate
-
37°C, native enzyme
0.14
4-nitrophenyl phosphate
mutant enzyme D101A/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.14
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/K328A, at pH 8.0 and 25°C
0.15
4-nitrophenyl phosphate
mutant enzyme D101A/E322Y, at pH 8.0 and 25°C
0.16
4-nitrophenyl phosphate
-
25°C, pH 8, wild-type enzyme
0.16
4-nitrophenyl phosphate
at pH 9.8 and 37°C
0.16
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.17
4-nitrophenyl phosphate
-
57°C, native enzyme
0.175
4-nitrophenyl phosphate
-
pH 8.0, 25°C
0.18
4-nitrophenyl phosphate
-
57°C, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.18
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.2 M N-methylethanolamine
0.194
4-nitrophenyl phosphate
-
mutant enzyme W475F, at pH 9.8 and 10°C
0.194
4-nitrophenyl phosphate
-
wild type enzyme, at pH 9.8 and 10°C
0.198
4-nitrophenyl phosphate
-
mutant H412Y, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.2
4-nitrophenyl phosphate
-
37°C, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.2
4-nitrophenyl phosphate
-
37°C, pH 9.5, mutant os-1 enzyme, without MgCl2
0.21
4-nitrophenyl phosphate
-
pH 10.5, wild-type
0.212
4-nitrophenyl phosphate
-
mutant enzyme W512F, at pH 9.8 and 10°C
0.218
4-nitrophenyl phosphate
-
mutant enzyme F355W, at pH 9.8 and 10°C
0.218
4-nitrophenyl phosphate
-
mutant enzyme W155F, at pH 9.8 and 10°C
0.22
4-nitrophenyl phosphate
-
-
0.22
4-nitrophenyl phosphate
-
intracellular form
0.22
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.23
4-nitrophenyl phosphate
-
37°C, native enzyme, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.23
4-nitrophenyl phosphate
-
25°C, pH 8, mutant enzyme T81A
0.238
4-nitrophenyl phosphate
-
pH 7.4, 37°C
0.239
4-nitrophenyl phosphate
-
mutant enzyme W301F, at pH 9.8 and 10°C
0.24
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.1 M triethanolamine
0.252
4-nitrophenyl phosphate
-
mutant enzyme W460Y, at pH 9.8 and 10°C
0.26
4-nitrophenyl phosphate
-
10°C, native enzyme
0.27
4-nitrophenyl phosphate
-
37°C, pH 9.5, wild-type enzyme, without MgCl2
0.27
4-nitrophenyl phosphate
-
without Mg2+
0.28
4-nitrophenyl phosphate
-
intracellular form
0.29
4-nitrophenyl phosphate
-
fusion protein with ZZ protein, pH not specified in the publication, temperature not specified in the publication
0.29
4-nitrophenyl phosphate
-
native enzyme, pH not specified in the publication, temperature not specified in the publication
0.3
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.05 M ethanolamine
0.3
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M ethanolamine
0.3
4-nitrophenyl phosphate
25°C, pH 18.0, diethanolamine buffer
0.31
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M triethanolamine
0.31
4-nitrophenyl phosphate
-
conjugate between enzyme and ZZ protein, pH not specified in the publication, temperature not specified in the publication
0.32
4-nitrophenyl phosphate
-
isozyme B/I, pH 10.0
0.35
4-nitrophenyl phosphate
-
isozyme B2, pH 10.0
0.35
4-nitrophenyl phosphate
-
pH 8.9, 37°C
0.35
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.02 M dimethylamine
0.35
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.02 M ethylamine
0.35
4-nitrophenyl phosphate
mutant enzyme D153A/E322Y/K328A, at pH 8.0 and 25°C
0.354
4-nitrophenyl phosphate
-
mutant enzyme W460F, at pH 9.8 and 10°C
0.4
4-nitrophenyl phosphate
-
37°C, pH 9.5, mutant os-1 enzyme, 2 mM MgCl2
0.4
4-nitrophenyl phosphate
-
37°C, pH 9.5, glycine-NaOH buffer
0.41
4-nitrophenyl phosphate
-
with Mg2+
0.43
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M ethylamine
0.44
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/E322Y, at pH 8.0 and 25°C
0.45
4-nitrophenyl phosphate
pH 10.5, 20°C, 4 M NaCl
0.462
4-nitrophenyl phosphate
-
mutant enzyme W274F, at pH 9.8 and 10°C
0.48
4-nitrophenyl phosphate
-
isozyme B1, pH 10.0
0.484
4-nitrophenyl phosphate
-
at pH 10.5 and 25°C
0.5
4-nitrophenyl phosphate
-
pH 9.2, 45°C, Vmax: 0.02 mM/min
0.56
4-nitrophenyl phosphate
-
37°C, pH 9.8
0.59
4-nitrophenyl phosphate
-
at pH 9.0 and 47°C
0.59
4-nitrophenyl phosphate
-
pH 9.0, 47°C
0.62
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M methylamine
0.65
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M dimethylamine
0.69
4-nitrophenyl phosphate
-
pH 10, 37°C, Vmax: 0.02 mM/min
0.7
4-nitrophenyl phosphate
-
-
0.76
4-nitrophenyl phosphate
-
37°C, pH 11, Tris-HCl buffer
0.83
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M diethanolamine
0.833
4-nitrophenyl phosphate
-
at pH 9.5 and 37°C
0.85
4-nitrophenyl phosphate
-
37°C, native enzyme, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.95
4-nitrophenyl phosphate
-
pH 9.8, 37°C
0.96
4-nitrophenyl phosphate
-
pH 10.0, 25°C
1.07
4-nitrophenyl phosphate
-
pH 10.5, 37°C, free-enzyme
1.2
4-nitrophenyl phosphate
-
37°C, pH 9.5, wild-type enzyme, 2 mM MgCl2
1.37
4-nitrophenyl phosphate
-
pH not specified, 37°C, Vmax: 0.011 mM/min, in the presence of 0.8 M NaN3
1.43
4-nitrophenyl phosphate
-
pH 9.5, 70°C, Co2+-combined enzyme
1.48
4-nitrophenyl phosphate
-
with 0.5 M NaCl, at pH 10.5 and 25°C
1.51
4-nitrophenyl phosphate
-
pH 9.5, 30°C, foot
1.58
4-nitrophenyl phosphate
-
1.91
4-nitrophenyl phosphate
-
pH 9.5, 37°C, Vmax: 0.029 mM/min, in the presence of 0.8 M KNO3
2.44
4-nitrophenyl phosphate
-
pH 10.5, 37°C, enzyme immobilized by phosphatase-polyresorcinol complex
2.48
4-nitrophenyl phosphate
-
pH 8.5, 30°C, digestive gland and siphon
2.48
4-nitrophenyl phosphate
-
40% sucrose, -4.5°C, frozen
2.5 - 3
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M N-methylethanolamine
2.52
4-nitrophenyl phosphate
-
pH 9.5, 37°C, Vmax: 0.023 mM/min, in the presence of 0.8 M KCl
2.54
4-nitrophenyl phosphate
-
pH 10, 37°C, Vmax: 0.018 mM/min, in the presence of 0.8 M NaAc
2.73
4-nitrophenyl phosphate
-
pH 9.25, 37°C, Vmax: 0.02 mM/min, in the presence of 0.8 M KPF6
2.8
4-nitrophenyl phosphate
-
pH 10, 30°C
2.86
4-nitrophenyl phosphate
-
pH 9.7, 37°C
2.88
4-nitrophenyl phosphate
-
pH 8.5, 30°C, mantle
2.9
4-nitrophenyl phosphate
25°C, pH 10.3, Tris-HCl buffer
2.96
4-nitrophenyl phosphate
at pH 10.0 and 50°C
2.97
4-nitrophenyl phosphate
-
40% sucrose, -4.5°C, unfrozen
3.43
4-nitrophenyl phosphate
-
pH 9.25, 37°C, Vmax: 0.021 mM/min, in the presence of 0.8 M NaNO3
3.6
4-nitrophenyl phosphate
-
pH 8, 25°C, without phosphate acceptor
4.4
4-nitrophenyl phosphate
-
pH 9, 37°C, Vmax: 0.016 mM/min, in the presence of 0.8 M NaBF4
4.42
4-nitrophenyl phosphate
-
pH 9.5, 37°C, Vmax: 0.028 mM/min, in the presence of 0.8 M NaCl
4.52
4-nitrophenyl phosphate
-
pH 8.5, 30°C, gills
4.59
4-nitrophenyl phosphate
-
pH 9.8, recombinant enzyme expressed in Tn-5B1-4 cells
4.7
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 384 mM NaCl, without Mn2+
4.9
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM NaCl, without Mn2+
6.4
4-nitrophenyl phosphate
-
40% sucrose, 25°C
6.76
4-nitrophenyl phosphate
-
pH 9.8, recombinant enzyme expressed in Sf-9 cells
6.87
4-nitrophenyl phosphate
-
pH 9, 37°C, Vmax: 0.022 mM/min, in the presence of 0.8 M Na2SO4
7.32
4-nitrophenyl phosphate
-
pH not specified, 37°C, Vmax: 0.019 mM/min, in the presence of 0.8 M Na citrate
8.6
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM NaCl, 2.5 mM Mn2+
9
4-nitrophenyl phosphate
-
-
9
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 384 mM K+, 2.5 mM MnCl2
9.7
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM K+, 2.5 mM MnCl2
11.6
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 384 mM NaCl, 2.5 mM Mn2+
13.2
4-nitrophenyl phosphate
25°C, pH 10.3, diethanolamine buffer
13.9
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 192 mM NaCl, 2.5 mM Mn2+
14.4
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM NaCl, 5 mM Mn2+
16.7
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 192 mM NaCl, without Mn2+
16.8
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM NaCl, 8 mM Mn2+
25.4
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 192 mM K+, 2.5 mM MnCl2
49.7
4-nitrophenyl phosphate
-
pH 9.8, native placental enzyme
2.26
ADP
-
pH 7.4, 37°C
0.1
ATP
-
-
0.39
ATP
-
membranous enzyme form
0.48
ATP
-
soluble enzyme form
0.3
beta-Glycerophosphate
-
soluble enzyme form
0.38
beta-Glycerophosphate
-
membranous enzyme form
1.4
beta-Glycerophosphate
-
-
1.5
beta-Glycerophosphate
-
purified enzyme
1.9
beta-Glycerophosphate
-
pH 7.4, 37°C
3
beta-Glycerophosphate
-
membrane-bound enzyme
3.35
beta-Glycerophosphate
-
-
0.12
diphosphate
-
purified enzyme
0.21
diphosphate
-
membrane-bound enzyme
1.4
diphosphate
-
allozyme D, pH 7.5, 37°C, in presence of Mg2+ and Zn2+
2.22
glucose 1-phosphate
-
-
4.8
glucose 1-phosphate
-
-
0.0094
p-nitrophenyl phosphate
-
wild type enzyme, in absence of a phosphate acceptor
0.0154
p-nitrophenyl phosphate
-
MOPS buffer
0.02
p-nitrophenyl phosphate
-
pH 9.0, hydrophilic and amphiphilic enzyme form
0.021
p-nitrophenyl phosphate
25°C, pH 8.0, wild-type enzyme
0.02124
p-nitrophenyl phosphate
-
wild type enzyme, in presence of a phosphate acceptor
0.034
p-nitrophenyl phosphate
-
and a second Km value of 0.056 mM
0.037
p-nitrophenyl phosphate
-
pH 9.2, absence of divalent metal ions
0.056
p-nitrophenyl phosphate
-
and a second Km value of 0.034 mM
0.05972
p-nitrophenyl phosphate
-
mutant enzyme D369N, in presence of a phosphate acceptor
0.08
p-nitrophenyl phosphate
-
25°C, pH 9.8, wild-type enzyme
0.081
p-nitrophenyl phosphate
-
-
0.088
p-nitrophenyl phosphate
-
purified enzyme
0.11
p-nitrophenyl phosphate
-
isoenzyme III
0.176
p-nitrophenyl phosphate
-
mutant enzyme D369N, in absence of a phosphate acceptor
0.183
p-nitrophenyl phosphate
-
-
0.19
p-nitrophenyl phosphate
-
25°C, pH 9.8, mutant enzyme W274K
0.22
p-nitrophenyl phosphate
-
isoenzyme II
0.22
p-nitrophenyl phosphate
-
pH 10.2, in presence of 1 mM Mn2+
0.252
p-nitrophenyl phosphate
-
-
0.28
p-nitrophenyl phosphate
-
-
0.33
p-nitrophenyl phosphate
-
0.39
p-nitrophenyl phosphate
-
membrane-bound enzyme
0.44
p-nitrophenyl phosphate
-
membranous enzyme form
0.45
p-nitrophenyl phosphate
-
soluble enzyme form
0.62
p-nitrophenyl phosphate
-
-
0.8
p-nitrophenyl phosphate
-
-
0.8
p-nitrophenyl phosphate
-
-
0.94
p-nitrophenyl phosphate
-
-
1.114
p-nitrophenyl phosphate
-
-
1.25
p-nitrophenyl phosphate
-
25°C, pH 9.8, mutant enzyme H116D
1.3
p-nitrophenyl phosphate
-
-
1.3
p-nitrophenyl phosphate
-
-
1.44
p-nitrophenyl phosphate
-
25°C, pH 9.8, mutant enzyme H116D/W274K
2
p-nitrophenyl phosphate
-
isoenzyme I
2.5
p-nitrophenyl phosphate
-
-
2.6
p-nitrophenyl phosphate
-
-
2.941
p-nitrophenyl phosphate
-
mutant enzyme D369A, in absence of a phosphate acceptor
4.48
p-nitrophenyl phosphate
-
pH 10.3, hydrophilic enzyme form
5.02
p-nitrophenyl phosphate
-
pH 10.3, amphiphilic enzyme form
6.1
Phenyl phosphate
-
-
6.67
Phenyl phosphate
-
enzyme from small intestine
10.2
Phenyl phosphate
-
-
11.63
Phenyl phosphate
-
enzyme from 8 day pseudopregant deciduae
11.9
Phenyl phosphate
-
enzyme from 20 day term fetal placentae
12.3
Phenyl phosphate
-
-
12.4
Phenyl phosphate
-
-
13.1
Phenyl phosphate
-
enzyme from 8 day pregnant deciduae
16.2
Phenyl phosphate
-
-
23.81
Phenyl phosphate
-
enzyme from anestrus uterus
0.39
phospho-DL-Thr
-
purified enzyme
0.9
phospho-DL-Thr
-
membrane-bound enzyme
0.4
phospho-DL-Tyr
-
purified enzyme
0.72
phospho-DL-Tyr
-
membrane-bound enzyme
0.38
phospho-L-Ser
-
purified enzyme
0.68
phospho-L-Ser
-
membrane-bound enzyme
0.2
pyridoxal phosphate
-
purified enzyme
0.37
pyridoxal phosphate
-
membrane-bound enzyme
additional information
4-nitrophenyl phosphate
-
the Km values increase with increasing concentrations of diethanolamine and N-methylethanolamine, but not triethanolamine
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetic characterization of the homodimeric complementation mutants, and heterodimeric hybrid formation
-
additional information
additional information
-
kinetics at several temperatures and pH-value combinations
-
additional information
additional information
-
kinetics of other allozymes of PALP
-
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33
2'-[2-benzthiazole]-6'-hydroxybenzthiazole phosphate
-
-
0.000029 - 28300
4-nitrophenyl phosphate
244
diphosphate
-
allozyme D, pH 7.5, 37°C, in presence of Mg2+ and Zn2+
138.1
O-Phosphotyrosine
-
0.01 - 1580
p-nitrophenyl phosphate
14.1
phosphoenolpyruvate
-
92
pyridoxal 5'-phosphate
-
allozyme D, pH 7.5, 37°C, in presence of Mg2+ and Zn2+
additional information
additional information
-
0.000029
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.000057
4-nitrophenyl phosphate
mutant enzyme R166S/E322Y/K328A, at pH 8.0 and 25°C
0.00021
4-nitrophenyl phosphate
pH 8.0, 25°C, recombinant mutant T59R
0.00024
4-nitrophenyl phosphate
mutant enzyme D101A/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.00032
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A/E322Y, at pH 8.0 and 25°C
0.00073
4-nitrophenyl phosphate
mutant enzyme D153A/E322Y/K328A, at pH 8.0 and 25°C
0.00089
4-nitrophenyl phosphate
mutant enzyme D101A/E322Y/K328A, at pH 8.0 and 25°C
0.00096
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/E322Y/K328A, at pH 8.0 and 25°C
0.0014
4-nitrophenyl phosphate
mutant enzyme D153A/E322Y, at pH 8.0 and 25°C
0.0026
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/K328A, at pH 8.0 and 25°C
0.0034
4-nitrophenyl phosphate
mutant enzyme E322Y/K328A, at pH 8.0 and 25°C
0.0083
4-nitrophenyl phosphate
mutant enzyme R166S/D153A/E322Y, at pH 8.0 and 25°C
0.016
4-nitrophenyl phosphate
-
mutant E322K, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.016
4-nitrophenyl phosphate
mutant enzyme R166S/K328A, at pH 8.0 and 25°C
0.027
4-nitrophenyl phosphate
-
mutant E322K, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.037 - 0.23
4-nitrophenyl phosphate
-
37°C, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.042
4-nitrophenyl phosphate
-
mutant E341K, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.052
4-nitrophenyl phosphate
-
mutant T155M, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.059
4-nitrophenyl phosphate
-
mutant H412Y, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.061
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A/K328A, at pH 8.0 and 25°C
0.067
4-nitrophenyl phosphate
-
mutant H412Y, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.07
4-nitrophenyl phosphate
mutant enzyme R166S/D153A, at pH 8.0 and 25°C
0.083
4-nitrophenyl phosphate
mutant enzyme D101A/R166S/D153A, at pH 8.0 and 25°C
0.1
4-nitrophenyl phosphate
-
mutant E341K, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.3
4-nitrophenyl phosphate
pH 8.0, 25°C, mutant R166A
0.32
4-nitrophenyl phosphate
-
mutant T155M, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
0.39
4-nitrophenyl phosphate
-
mutant D369N, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
0.5
4-nitrophenyl phosphate
pH 8.0, 25°C, mutant R166S
0.5
4-nitrophenyl phosphate
mutant enzyme R166S, at pH 8.0 and 25°C
0.55
4-nitrophenyl phosphate
-
10°C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
0.65
4-nitrophenyl phosphate
pH 8.0, 25°C, mutant R166K
1.1
4-nitrophenyl phosphate
mutant enzyme D153A/K328A, at pH 8.0 and 25°C
1.5
4-nitrophenyl phosphate
pH 8.0, 25°C, recombinant mutant T59A
1.6
4-nitrophenyl phosphate
mutant enzyme D101A/D153A/K328A, at pH 8.0 and 25°C
2.2
4-nitrophenyl phosphate
mutant enzyme D101A/D153A, at pH 8.0 and 25°C
2.3
4-nitrophenyl phosphate
pH 8.0, 25°C, recombinant wild-type enzyme
2.4
4-nitrophenyl phosphate
-
mutant D369N, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
3 - 6
4-nitrophenyl phosphate
mutant enzyme D101A, at pH 8.0 and 25°C
3.4
4-nitrophenyl phosphate
-
25°C, pH 8, mutant enzyme T81A
3.4
4-nitrophenyl phosphate
mutant enzyme K328A, at pH 8.0 and 25°C
3.8
4-nitrophenyl phosphate
-
mutant S105L, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
4.2
4-nitrophenyl phosphate
mutant enzyme D101A/R166S, at pH 8.0 and 25°C
4.6
4-nitrophenyl phosphate
mutant enzyme D101A/E322Y, at pH 8.0 and 25°C
5.8
4-nitrophenyl phosphate
-
mutant S105L, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
6.08
4-nitrophenyl phosphate
at pH 10.5 and 70°C
7.6
4-nitrophenyl phosphate
mutant enzyme D153A, at pH 8.0 and 25°C
12
4-nitrophenyl phosphate
pH 8.0, 25°C, wild-type
12
4-nitrophenyl phosphate
wild type enzyme, at pH 8.0 and 25°C
14.67
4-nitrophenyl phosphate
-
10°C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
16
4-nitrophenyl phosphate
-
pH 8.0, 25°C
16
4-nitrophenyl phosphate
at pH 10.0 and 50°C
18
4-nitrophenyl phosphate
-
25°C, pH 10.5, mutant enzyme T81A
20 - 50
4-nitrophenyl phosphate
-
57°C, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
24.39
4-nitrophenyl phosphate
-
25°C, pH 10.5, mutant enzyme T81A
26
4-nitrophenyl phosphate
-
25°C, pH10.5, wild-type enzyme
29.9
4-nitrophenyl phosphate
-
pH 8, 25°C, in the presence of phosphate acceptor (1 M Tris-HCl buffer)
30
4-nitrophenyl phosphate
pH 10.0, 15°C, mutant S86A/G87A
34
4-nitrophenyl phosphate
-
25°C, pH 8, wild-type enzyme
34
4-nitrophenyl phosphate
-
pH 10.5, mutant V406A
35.6
4-nitrophenyl phosphate
-
at pH 8.0 and 25°C
36.98
4-nitrophenyl phosphate
-
25°C, pH 8, mutant enzyme T81A
42.55
4-nitrophenyl phosphate
-
37°C, pH 9.5, glycine-NaOH buffer
44
4-nitrophenyl phosphate
-
mutant enzyme W475F, at pH 9.8 and 10°C
44.4
4-nitrophenyl phosphate
-
wild-type enzyme, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
56.3
4-nitrophenyl phosphate
pH 8.0, 25°C, recombinant mutant T59A
61.84
4-nitrophenyl phosphate
-
25°C, pH 8, wild-type enzyme
65
4-nitrophenyl phosphate
-
37°C, native enzyme
65
4-nitrophenyl phosphate
-
mutant enzyme W460F, at pH 9.8 and 10°C
65.6
4-nitrophenyl phosphate
-
mutant D434E, pH 8.0, 25°C, in absence of a phosphoryl group acceptor
70
4-nitrophenyl phosphate
pH 10.0, 15°C, mutant S42G/H135E
71
4-nitrophenyl phosphate
pH 10.0, 15°C, mutant S42G/S338T
74.7
4-nitrophenyl phosphate
pH 8.0, 25°C, recombinant wild-type enzyme
76
4-nitrophenyl phosphate
-
pH 9.5, 70°C, wild-type enzyme
77.4
4-nitrophenyl phosphate
-
37°C, native enzyme, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
78.83
4-nitrophenyl phosphate
-
37°C, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
80
4-nitrophenyl phosphate
-
at pH 10.5 and 25°C
80.5
4-nitrophenyl phosphate
-
wild-type enzyme, pH 8.0, 25°C, in presence of a phosphoryl group acceptor
82.98
4-nitrophenyl phosphate
-
37°C, pH 11, Tris-HCl buffer
87.83
4-nitrophenyl phosphate
-
57°C, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
95
4-nitrophenyl phosphate
-
at pH 11.0 and 25°C
99
4-nitrophenyl phosphate
-
with 0.5 M NaCl, at pH 10.5 and 25°C
100
4-nitrophenyl phosphate
-
pH 8.0, 65°C
100
4-nitrophenyl phosphate
pH 10.0, 15°C, mutant G87A
102
4-nitrophenyl phosphate
-
at pH 9.0 and 25°C
113.6
4-nitrophenyl phosphate
single-chain Fv antibody fusion protein
114
4-nitrophenyl phosphate
pH 10.0, 15°C, mutant S338T
115.9
4-nitrophenyl phosphate
-
37°C, native enzyme
117
4-nitrophenyl phosphate
pH 10.0, 15°C, mutant G149D
125
4-nitrophenyl phosphate
-
mutant enzyme W155F, at pH 9.8 and 10°C
132
4-nitrophenyl phosphate
-
25°C, pH 8.0, mutant enzyme G51C
133
4-nitrophenyl phosphate
pH 10.0, 15°C, mutant S42G
137
4-nitrophenyl phosphate
-
mutant enzyme W301F, at pH 9.8 and 10°C
140
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.05 M methylamine
145
4-nitrophenyl phosphate
-
with 0.5 M NaCl, at pH 8.0 and 25°C
150
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.02 M dimethylamine
153.9
4-nitrophenyl phosphate
-
37°C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
155.7
4-nitrophenyl phosphate
-
10°C, native enzyme
183.3
4-nitrophenyl phosphate
-
57°C, native enzyme
190
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.05 M diethanolamine
203
4-nitrophenyl phosphate
pH 10.0, 15°C, mutant S86A
204
4-nitrophenyl phosphate
-
25°C, pH 8.0, mutant enzyme S52C
217
4-nitrophenyl phosphate
-
25°C, pH 8.0, mutant enzyme S53C
236
4-nitrophenyl phosphate
pH 10.0, 15°C, wild-type
243
4-nitrophenyl phosphate
-
with 0.5 M NaCl, at pH 9.0 and 25°C
255
4-nitrophenyl phosphate
-
mutant enzyme F355W, at pH 9.8 and 10°C
275
4-nitrophenyl phosphate
-
mutant enzyme W460Y, at pH 9.8 and 10°C
285
4-nitrophenyl phosphate
-
conjugate between enzyme and ZZ protein, pH not specified in the publication, temperature not specified in the publication
300
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M ethanolamine
300
4-nitrophenyl phosphate
-
mutant enzyme W274F, at pH 9.8 and 10°C
302
4-nitrophenyl phosphate
-
wild type enzyme, at pH 9.8 and 10°C
303
4-nitrophenyl phosphate
pH 10.0, 15°C, mutant H135E
313
4-nitrophenyl phosphate
-
mutant enzyme W512F, at pH 9.8 and 10°C
330
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M methylamine
350
4-nitrophenyl phosphate
-
pH 10.0, 25°C
350
4-nitrophenyl phosphate
-
25°C, pH 8.0, mutant enzyme I50C
361
4-nitrophenyl phosphate
pH 10.0, 15°C, mutant H135E/G149D
370
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M dimethylamine
370
4-nitrophenyl phosphate
-
fusion protein with ZZ protein, pH not specified in the publication, temperature not specified in the publication
378
4-nitrophenyl phosphate
-
native enzyme, pH not specified in the publication, temperature not specified in the publication
379
4-nitrophenyl phosphate
-
allozyme D, pH 9.8, in presence of Mg2+ and Zn2+
400
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M ethylamine
450
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.02 M ethylamine
500
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.2 M N-methylethanolamine
610
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.05 M ethanolamine
812.3
4-nitrophenyl phosphate
-
37°C, native enzyme
840
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 0.1 M triethanolamine
971
4-nitrophenyl phosphate
-
pH 10.5, wild-type
1130
4-nitrophenyl phosphate
-
pH 9.5, 70°C, Co2+-combined enzyme
1240
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M diethanolamine
1400
4-nitrophenyl phosphate
-
at pH 9.0 and 47°C
1400
4-nitrophenyl phosphate
-
pH 9.0, 47°C
1443
4-nitrophenyl phosphate
-
37°C, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
1450
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M triethanolamine
1500
4-nitrophenyl phosphate
25°C, pH 18.0, Tris-HCl buffer
2086
4-nitrophenyl phosphate
-
25°C, pH 8.0, wild-type enzyme
2250
4-nitrophenyl phosphate
-
pH 9.8, 20°C, 1 M N-methylethanolamine
3710
4-nitrophenyl phosphate
25°C, pH 10.3, Tris-HCl buffer
7000
4-nitrophenyl phosphate
at pH 9.8 and 37°C
16230
4-nitrophenyl phosphate
-
37°C, native enzyme, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
24000
4-nitrophenyl phosphate
25°C, pH 18.0, diethanolamine buffer
28300
4-nitrophenyl phosphate
25°C, pH 10.3, diethanolamine buffer
0.01
p-nitrophenyl phosphate
-
mutant enzyme D369A, in absence of a phosphate acceptor
0.4
p-nitrophenyl phosphate
-
mutant enzyme D369N, in absence of a phosphate acceptor
38
p-nitrophenyl phosphate
25°C, pH 8.0, wild-type enzyme
44.5
p-nitrophenyl phosphate
-
wild type enzyme
80.5
p-nitrophenyl phosphate
-
wild type enzyme, in presence of a phosphate acceptor
147.9
p-nitrophenyl phosphate
-
220
p-nitrophenyl phosphate
-
25°C, pH 9.8, mutant enzyme W274K
230
p-nitrophenyl phosphate
-
mutant enzyme D369N, in presence of a phosphate acceptor
830
p-nitrophenyl phosphate
-
25°C, pH 9.8, mutant enzyme H116D
930
p-nitrophenyl phosphate
-
25°C, pH 9.8, mutant enzyme H116D/W274K
1580
p-nitrophenyl phosphate
-
25°C, pH 9.8, wild-type enzyme
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
kcat/KM (1/Msec) wild-type: 140000, mutant R166K: 20, mutant R166S: 24
-
additional information
additional information
-
kcat/KM (1/Msec) wild-type: 140000, mutant R166K: 20, mutant R166S: 24
-
additional information
additional information
wild-type enzyme: kcat/KM (1/M*sec) (4-nitrophenyl phosphate): 33000000, (3-nitrobenzyl phosphate): 18000000, (methyl phosphate): 1200000, (methyl 4-nitrophenyl phosphate): 18, (bis-4-nitrophenyl phosphate): 0.05, (4-nitrophenyl sulfate): 0.01
-
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0.00106 - 0.00398
(E)-N'-(1-(3-(4-fluorophenyl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl)ethylidene)isonicotinohydrazide
0.00067
(E)-N'-(4'-chlorobenzylidene)isonicotinohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00035 - 0.00192
(E)-N'-(4-hydroxy-3-methoxybenzylidene)isonicotinohydrazide
0.00149
1,4-dimethoxy-2-methylbenzene
Homo sapiens
-
-
0.0012 - 0.0302
1-(3,4-dihydroxyphenyl)-2-(1H-imidazol-1-yl)ethanone
0.0042
1-(3,4-dihydroxyphenyl)-2-(2-ethyl-1H-imidazol-1-yl)ethanone
Homo sapiens
-
-
0.0012 - 0.0263
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-benzimidazol-1-yl)ethanone
0.0033 - 0.0783
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-imidazol-1-yl)ethanone
0.0172
1-(3,4-dihydroxyphenyl)-2-(2-phenyl-1H-imidazol-1-yl)ethanone
Homo sapiens
-
-
0.0058 - 0.0411
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-imidazol-1-yl)ethanone
0.0027 - 0.0533
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-pyrazol-1-yl)ethanone
0.0134
1-(3,4-dihydroxyphenyl)-2-(4H-1,2,4-triazol-4-yl)ethanone
Homo sapiens
-
-
0.0058
1-(3,4-dihydroxyphenyl)-2-(5,6-dimethyl-1H-benzimidazol-1-yl)ethanone
Homo sapiens
-
-
0.0393
1-(3,4-dihydroxyphenyl)-2-(propan-2-ylamino)ethanone
Homo sapiens
-
-
0.0006 - 0.0495
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
0.0067
1-(3,4-dihydroxyphenyl)-2-[(4-methyl-5-phenyl-4H-1,2,4-triazol-3-yl)sulfanyl]ethanone
Homo sapiens
-
-
0.002 - 0.008
1-(3,4-dihydroxyphenyl)-2-[[1-(4-methoxyphenyl)-1H-tetrazol-5-yl]sulfanyl]ethanone
0.00069
1-chloro-4-ethoxy-2-methylbenzene
Homo sapiens
-
-
0.00051
1-chloro-4-methoxy-2-methylbenzene
Homo sapiens
-
-
0.00129
1-fluoro-4-methoxybenzene
Homo sapiens
-
-
0.000488
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-ethylpiperazine
Bos taurus
-
0.000828
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-methylpiperazine
Bos taurus
-
0.00145
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]azepane
Bos taurus
-
0.000344
2,4-dichloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.0103
2,5-dimethoxy-N-(pyridin-3-yl)benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.00106
2,5-dimethoxy-N-(pyridin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00019
2,5-dimethoxy-N-(quinolin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00202 - 0.00222
2-(1-methylhydrazenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.0008 - 0.018
2-(1H-benzimidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
0.0062 - 0.0938
2-(1H-benzimidazol-2-ylamino)-1-(3,4-dihydroxyphenyl)ethanone
0.00452 - 0.1
2-(2-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.1
2-(2-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00348 - 0.1
2-(2-methoxyphenyl)-7- trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00054 - 0.00175
2-(3,4-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00076 - 0.00115
2-(3,5-di-methoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00046 - 0.00052
2-(3,5-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00056 - 0.00112
2-(3-cyanophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00052 - 0.00068
2-(3-fluoromethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00074 - 0.00139
2-(3-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00038 - 0.00044
2-(3-methoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00048 - 0.00062
2-(3-nitrophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00112 - 0.00167
2-(3-phenylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00033 - 0.00071
2-(4-aminophenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.0158 - 0.0475
2-(4-bromo-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
0.0049 - 0.0087
2-(4-bromo-2-methyl-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
0.00079 - 0.00093
2-(4-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00158 - 0.00202
2-(4-ethoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00455 - 0.1
2-(4-ethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00198 - 0.0315
2-(4-i-propylphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00028 - 0.00048
2-(4-methoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00036 - 0.00106
2-(4-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00024 - 0.1
2-(4-trifluoromethoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.000375
2-(4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]piperazin-1-yl)ethanol
Bos taurus
-
0.00054
2-([(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)sulfonyl]amino)-N-(2,5-dimethylphenyl)acetamide
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.00029 - 0.00089
2-allylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00113
2-chloro-1,4-dimethoxybenzene
Homo sapiens
-
-
0.003458
2-chloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.000322
2-cyano-6-methoxy-N-(pyridin-3-yl)benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.00153 - 0.00463
2-di-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00113
2-ethoxy-5-methyl-N-(pyridin-3-yl)benzenesulfonamide
Homo sapiens
-
-
18
2-glycerophosphate
Physarum polycephalum
-
-
0.00316
2-methoxy-4-nitro-N-(pyridin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00074
2-methoxy-4-nitro-N-(quinolin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.000896
2-methoxy-5-methyl-N-(pyridin-3-yl)benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.00185
2-methoxy-5-methyl-N-(pyridin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00065
2-methoxy-5-methyl-N-(quinolin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00071 - 0.00088
2-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00061 - 0.00076
2-n-pentylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00031 - 0.00144
2-n-propylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00021 - 0.00043
2-phenyl-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00045 - 0.00375
2-[2-(dimethylamino)ethyl]amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.0022 - 0.0048
2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl]-4-(methoxymethyl)-6-methylpyridine-3-carbonitrile
0.000896
3,5-dinitro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.000127
3-(2,4-dichloro-5-fluorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000324
3-(2,4-dichloro-5-fluorophenyl)-N,N-dimethyl-1H-pyrazole-5-carboxamide
Bos taurus
-
0.00485
3-(2,4-dichloro-5-fluorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.0001
3-(2,4-dichloro-5-fluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000056
3-(2,4-dichloro-5-fluorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000044
3-(2,4-dichlorophenyl)-1H-pyrazole-5-carbohydrazide
Bos taurus
-
0.000047
3-(2,4-dichlorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000285
3-(2,4-dichlorophenyl)-N,N-diethyl-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000119
3-(2,4-dichlorophenyl)-N,N-dimethyl-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000051
3-(2,4-dichlorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000044
3-(2,4-dichlorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000046
3-(2,4-dichlorophenyl)-N-(2-methoxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000082
3-(2,4-dichlorophenyl)-N-(2-methylpropyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000031
3-(2,4-dichlorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000459
3-(2,4-dichlorophenyl)-N-(3-methylbutyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000035
3-(2,4-dichlorophenyl)-N-(4-hydroxybutyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000035
3-(2,4-difluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.8
3-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
0.00149
3-methoxy-2-[(pyridin-3-yl)sulfamoyl]benzamide
Mus musculus
pH and temperature not specified in the publication
0.000876
3-methoxy-N-(pyridin-3-yl)[1,1'-biphenyl]-2-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.003 - 0.0292
3-[2-(3,4-dihydroxyphenyl)-2-oxoethyl]-6,7-dimethoxy-2-benzofuran-1(3H)-one
0.00155
4-bromo-2,5-dimethoxy-N-(pyridin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.000251
4-chloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.001547
4-fluoro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.00168
4-methoxy-1,2-dimethylbenzene
Homo sapiens
-
-
0.003291
4-methoxy-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.0512
4-[[(4,6-dimethylpyrimidin-2-yl)amino]methyl]benzene-1,2-diol
Homo sapiens
-
-
0.000574
4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]morpholine
Bos taurus
-
0.00012
5-bromo-2-methoxy-N-(quinolin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00054
5-chloro-2-ethoxy-N-(pyridin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00417
5-chloro-2-methoxy-N-(pyridin-3-yl)benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000178
5-chloro-2-methoxy-N-[5-(2-methylphenyl)pyridin-3-yl]benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.00016
5-chloro-2-methoxy-N-[5-(3-methylphenyl)pyridin-3-yl]benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000023
5-chloro-2-methoxy-N-[5-(4-methoxyphenyl)pyridin-3-yl]benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000147
5-chloro-2-methoxy-N-[5-(4-methylphenyl)pyridin-3-yl]benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000671
5-chloro-2-methoxy-N-[5-(4-methylpiperazine-1-carbonyl)pyridin-3-yl]benzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000198
5-chloro-N-[5-(4-chlorophenyl)pyridin-3-yl]-2-methoxybenzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000183
5-methyl-3-[3-[3-(trifluoromethyl)phenyl]prop-2-yn-1-yl]oxolan-2-one
Mus musculus
pH and temperature not specified in the publication
0.000014
5-[(5-bromo-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000193
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]-N-ethylpyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000109
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]-N-methylpyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.00031
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]-N-phenylpyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000016
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000134
5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxylic acid
Mus musculus
pH and temperature not specified in the publication
0.000019
5-[(5-fluoro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000131
5-[[2-methoxy-5-(trifluoromethoxy)benzene-1-sulfonyl]amino]pyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000432
5-[[5-chloro-2-(trifluoromethoxy)benzene-1-sulfonyl]amino]pyridine-3-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000084
6-(1-benzofuran-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
Mus musculus
pH and temperature not specified in the publication
0.000043
6-(5-nitro-1-benzothiophen-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
Mus musculus
pH and temperature not specified in the publication
0.8
6-(thiophen-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
0.26 - 0.331
6-(thiophen-2-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
0.000038
6-(thiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
Mus musculus
pH and temperature not specified in the publication
0.192 - 0.408
6-(thiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
0.8
6-(thiophen-3-yl)-2,3-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
0.042 - 0.084
6-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
0.8
6-(thiophen-3-yl)imidazo[2,1-b][1,3]thiazole hydrochloride
2.26
EDTA
Cyrtograpsus angulatus
-
IC50: 2.26 mM
0.044
Imipenem
Vibrio sp.
pH 7.0, temperature not specified in the publication
0.004137
KH2PO4
Bos taurus
-
at pH 9.5 and 37°C
0.08 - 0.0802
L-phenylalanine
0.0192 - 0.093
levamisole
0.00151
methyl 3-methoxy-2-[(pyridin-3-yl)sulfamoyl]benzoate
Mus musculus
pH and temperature not specified in the publication
0.000065
methyl 5-[(5-chloro-2-methoxybenzene-1-sulfonyl)amino]pyridine-3-carboxylate
Mus musculus
pH and temperature not specified in the publication
0.00144
N'-[(Z)-(2-hydroxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00182 - 0.00734
N'-[(Z)-(3-nitrophenyl)methylidene]pyridine-4-carbohydrazide
0.00413 - 0.00972
N'-[(Z)-(4-bromophenyl)methylidene]pyridine-4-carbohydrazide
0.00226 - 0.0175
N'-[(Z)-(4-fluorophenyl)methylidene]pyridine-4-carbohydrazide
0.00056 - 0.00174
N'-[(Z)-(4-methoxyphenyl)methylidene]pyridine-4-carbohydrazide
0.00146 - 0.00243
N'-[(Z)-(pyridin-3-yl)methylidene]pyridine-4-carbohydrazide
0.00246
N'-[(Z)-(pyridin-4-yl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.004256
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)acetamide
Bos taurus
-
at pH 9.5 and 37°C
0.001636
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)butyramide
Bos taurus
-
at pH 9.5 and 37°C
0.000492
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)heptanamide
Bos taurus
-
at pH 9.5 and 37°C
0.001704
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)octanamide
Bos taurus
-
at pH 9.5 and 37°C
0.000005 - 0.000026
N-(2-hydroxyethyl)-3-(2,3,4-trichlorophenyl)-1H-pyrazole-5-carboxamide
0.000134
N-(2-hydroxyethyl)-3-(2,4,5-trifluorophenyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.00182
N-(3-cyanophenyl)-3-([(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)sulfonyl]amino)propanamide
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.00012
N-([3,3'-bipyridin]-5-yl)-2,5-dimethoxybenzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000073
N-([3,3'-bipyridin]-5-yl)-5-chloro-2-methoxybenzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000073
N-([3,4'-bipyridin]-5-yl)-2,5-dimethoxybenzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000073
N-([3,4'-bipyridin]-5-yl)-5-chloro-2-methoxybenzene-1-sulfonamide
Mus musculus
pH and temperature not specified in the publication
0.000398
N-tert-butyl-3-(2,4-dichlorophenyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.0129
Na2[W2O3(O2)4(glycyl-glycine)2](3H2O)
Oryctolagus sp.
-
pH 10, 30°C
0.01267
Na2[W2O3(O2)4(glycyl-leucine)2](3H2O)
Oryctolagus sp.
-
pH 10, 30°C
49
NaF
Physarum polycephalum
-
-
0.015
Na[VO(O2)2(asparagine)]H2O
Oryctolagus cuniculus
-
pH 10, 30°C
0.0165
Na[VO(O2)2(glutamine)]H2O
Oryctolagus cuniculus
-
pH 10, 30°C
0.0118
Na[VO(O2)2(glycyl-glycine)(H2O)]H2O
Oryctolagus cuniculus
-
pH 10, 30°C
0.0025
Na[VO(O2)2(triglycine)]3H2O
Oryctolagus cuniculus
-
pH 10, 30°C
0.03168
tungstate
Oryctolagus sp.
-
pH 10, 30°C
0.02534
tungstate/H2O2
Oryctolagus sp.
-
pH 10, 30°C
-
0.01584
[WO(O2)2(glycyl-glycine)(H2O)]
Oryctolagus sp.
-
pH 10, 30°C
-
0.0142
[WO(O2)2(glycyl-glycine)(H2O)]3H2O
Oryctolagus cuniculus
-
pH 10, 30°C
0.0198
[WO(O2)2(glycyl-leucine)(H2O)]
Oryctolagus sp.
-
pH 10, 30°C
-
0.0049
[WO(O2)2(triglycine)]3H2O
Oryctolagus cuniculus
-
pH 10, 30°C
additional information
additional information
Sus scrofa
-
aus tab
-
0.00106
(E)-N'-(1-(3-(4-fluorophenyl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl)ethylidene)isonicotinohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00398
(E)-N'-(1-(3-(4-fluorophenyl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl)ethylidene)isonicotinohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00035
(E)-N'-(4-hydroxy-3-methoxybenzylidene)isonicotinohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00192
(E)-N'-(4-hydroxy-3-methoxybenzylidene)isonicotinohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.0012
1-(3,4-dihydroxyphenyl)-2-(1H-imidazol-1-yl)ethanone
Homo sapiens
-
-
0.0021
1-(3,4-dihydroxyphenyl)-2-(1H-imidazol-1-yl)ethanone
Homo sapiens
-
-
0.0302
1-(3,4-dihydroxyphenyl)-2-(1H-imidazol-1-yl)ethanone
Homo sapiens
-
-
0.0012
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-benzimidazol-1-yl)ethanone
Homo sapiens
-
-
0.0263
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-benzimidazol-1-yl)ethanone
Homo sapiens
-
-
0.0033
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-imidazol-1-yl)ethanone
Homo sapiens
-
-
0.0646
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-imidazol-1-yl)ethanone
Homo sapiens
-
-
0.0783
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-imidazol-1-yl)ethanone
Homo sapiens
-
-
0.0058
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-imidazol-1-yl)ethanone
Homo sapiens
-
-
0.0411
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-imidazol-1-yl)ethanone
Homo sapiens
-
-
0.0027
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-pyrazol-1-yl)ethanone
Homo sapiens
-
-
0.0533
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-pyrazol-1-yl)ethanone
Homo sapiens
-
-
0.0006
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
Homo sapiens
-
-
0.0025
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
Homo sapiens
-
-
0.0086
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
Homo sapiens
-
-
0.0495
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
Homo sapiens
-
-
0.002
1-(3,4-dihydroxyphenyl)-2-[[1-(4-methoxyphenyl)-1H-tetrazol-5-yl]sulfanyl]ethanone
Homo sapiens
-
-
0.008
1-(3,4-dihydroxyphenyl)-2-[[1-(4-methoxyphenyl)-1H-tetrazol-5-yl]sulfanyl]ethanone
Homo sapiens
-
-
0.00202
2-(1-methylhydrazenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00222
2-(1-methylhydrazenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.0008
2-(1H-benzimidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
Homo sapiens
-
-
0.0027
2-(1H-benzimidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
Homo sapiens
-
-
0.0148
2-(1H-benzimidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
Homo sapiens
-
-
0.018
2-(1H-benzimidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
Homo sapiens
-
-
0.0062
2-(1H-benzimidazol-2-ylamino)-1-(3,4-dihydroxyphenyl)ethanone
Homo sapiens
-
-
0.0091
2-(1H-benzimidazol-2-ylamino)-1-(3,4-dihydroxyphenyl)ethanone
Homo sapiens
-
-
0.0938
2-(1H-benzimidazol-2-ylamino)-1-(3,4-dihydroxyphenyl)ethanone
Homo sapiens
-
-
0.00452
2-(2-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.1
2-(2-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
IC50 above 0.1 mM, intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.1
2-(2-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
IC50 above 0.1 mM, intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.1
2-(2-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
IC50 above 0.1 mM, tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00348
2-(2-methoxyphenyl)-7- trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.1
2-(2-methoxyphenyl)-7- trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
IC50 above 0.1 mM, intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00054
2-(3,4-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00175
2-(3,4-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00076
2-(3,5-di-methoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00115
2-(3,5-di-methoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00046
2-(3,5-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00052
2-(3,5-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00056
2-(3-cyanophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00112
2-(3-cyanophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00052
2-(3-fluoromethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00068
2-(3-fluoromethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00074
2-(3-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00139
2-(3-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00038
2-(3-methoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00044
2-(3-methoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00048
2-(3-nitrophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00062
2-(3-nitrophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00112
2-(3-phenylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00167
2-(3-phenylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00033
2-(4-aminophenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00071
2-(4-aminophenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.0158
2-(4-bromo-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
Homo sapiens
-
-
0.0475
2-(4-bromo-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
Homo sapiens
-
-
0.0049
2-(4-bromo-2-methyl-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
Homo sapiens
-
-
0.0087
2-(4-bromo-2-methyl-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
Homo sapiens
-
-
0.00079
2-(4-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00093
2-(4-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00158
2-(4-ethoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00202
2-(4-ethoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00455
2-(4-ethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.1
2-(4-ethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
IC50 above 0.1 mM, tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00198
2-(4-i-propylphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.0315
2-(4-i-propylphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00028
2-(4-methoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00048
2-(4-methoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00036
2-(4-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00106
2-(4-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00024
2-(4-trifluoromethoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.1
2-(4-trifluoromethoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
IC50 above 0.1 mM, tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00029
2-allylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00089
2-allylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00153
2-di-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00463
2-di-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00071
2-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00088
2-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00061
2-n-pentylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00076
2-n-pentylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00031
2-n-propylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00144
2-n-propylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00021
2-phenyl-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00043
2-phenyl-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.00045
2-[2-(dimethylamino)ethyl]amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.00375
2-[2-(dimethylamino)ethyl]amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.0022
2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl]-4-(methoxymethyl)-6-methylpyridine-3-carbonitrile
Homo sapiens
-
-
0.0048
2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl]-4-(methoxymethyl)-6-methylpyridine-3-carbonitrile
Homo sapiens
-
-
0.8
3-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C, value higher than 0.8 mM
0.8
3-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C, value higher than 0.8 mM
0.003
3-[2-(3,4-dihydroxyphenyl)-2-oxoethyl]-6,7-dimethoxy-2-benzofuran-1(3H)-one
Homo sapiens
-
-
0.0292
3-[2-(3,4-dihydroxyphenyl)-2-oxoethyl]-6,7-dimethoxy-2-benzofuran-1(3H)-one
Homo sapiens
-
-
0.8
6-(thiophen-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C, value higher than 0.8 mM
0.8
6-(thiophen-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C, value higher than 0.8 mM
0.26
6-(thiophen-2-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C
0.331
6-(thiophen-2-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C
0.192
6-(thiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C
0.408
6-(thiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C
0.8
6-(thiophen-3-yl)-2,3-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C, value higher than 0.8 mM
0.8
6-(thiophen-3-yl)-2,3-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C, value higher than 0.8 mM
0.042
6-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C
0.084
6-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C
0.8
6-(thiophen-3-yl)imidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 10.4, 37°C, value higher than 0.8 mM
0.8
6-(thiophen-3-yl)imidazo[2,1-b][1,3]thiazole hydrochloride
Sus scrofa
-
pH 7.8, 37°C, value higher than 0.8 mM
0.08
L-phenylalanine
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.0802
L-phenylalanine
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.0192
levamisole
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
0.0192
levamisole
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.078
levamisole
Sus scrofa
-
pH 7.8, 37°C
0.093
levamisole
Sus scrofa
-
pH 10.4, 37°C
0.00182
N'-[(Z)-(3-nitrophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00734
N'-[(Z)-(3-nitrophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00413
N'-[(Z)-(4-bromophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00972
N'-[(Z)-(4-bromophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00226
N'-[(Z)-(4-fluorophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.0175
N'-[(Z)-(4-fluorophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00056
N'-[(Z)-(4-methoxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00174
N'-[(Z)-(4-methoxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00146
N'-[(Z)-(pyridin-3-yl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00243
N'-[(Z)-(pyridin-3-yl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.000005
N-(2-hydroxyethyl)-3-(2,3,4-trichlorophenyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000026
N-(2-hydroxyethyl)-3-(2,3,4-trichlorophenyl)-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
2.8
phosphate
Escherichia coli
-
pH 10.5, 37°C, free-enzyme
4
phosphate
Escherichia coli
-
pH 10.5, 37°C, enzyme immobilized by phosphatase-polyresorcinol complex
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D25A
-
mutant exhibits a slight increase in activity
D460A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
D505A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
E445A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
H216A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
H464A
-
mutant is almost inactive in 1 M Tris buffer, but has an increased activity in 0.1 M Mops buffer
H506A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
H566A
-
mutant is almost inactive in 1 M Tris buffer, but has an increased activity in 0.1 M Mops buffer
R229A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
S165A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
T218A
-
activity is significantly decreased in the presence or absence of a phosphate acceptor
G149D
mutant shows increased activity after thermal inactivation at 60°C, 120 min: 11.4%, kcat (1/sec) (4-nitrophenyl phosphate): 117
G87A
mutant shows increased activity after thermal inactivation at 60°C, 120 min: 11.4%, kcat (1/sec) (4-nitrophenyl phosphate): 100
H135E
double mutant shows decreased activity after thermal inactivation at 60°C, 120 min: 0.4%, kcat (1/sec) (4-nitrophenyl phosphate): 303
H135E/G149D
double mutant shows decreased activity after thermal inactivation at 60°C, 120 min: 1%, kcat (1/sec) (4-nitrophenyl phosphate): 361
S338T
double mutant shows decreased activity after thermal inactivation at 60°C, 120 min: 0.6%, kcat (1/sec) (4-nitrophenyl phosphate): 114
S42G
double mutant shows decreased activity after thermal inactivation at 60°C, 120 min: 0%, kcat (1/sec) (4-nitrophenyl phosphate): 133
S42G/H135E
double mutant shows decreased activity after thermal inactivation at 60°C, 120 min: 0%, kcat (1/sec) (4-nitrophenyl phosphate): 70
S42G/S338T
double mutant shows decreased activity after thermal inactivation at 60°C, 120 min: 0%, kcat (1/sec) (4-nitrophenyl phosphate): 71
S86A
mutant shows increased activity after thermal inactivation at 60°C, 120 min: 15.6%, kcat (1/sec) (4-nitrophenyl phosphate): 203
S86A/G87A
double mutant shows increased activity after thermal inactivation at 60°C, 120 min: 39.4%, kcat (1/sec) (4-nitrophenyl phosphate): 30
biotechnology
aqueous suspendible polymer nanostructures are prepared by simple microtome processing of electrospun nylon 6 nanofibers and are used to immobilize calf intestinal ALP by either covalent or noncovalent bioconjugation chemistries. Noncovalent immobilization of ALP to the mechanically cut nanofibers using a multi-stacked, layer-by-layer approach with the cationic polymer Sapphire II results in the highest enzyme loading. In terms of the overall catalytic performance of the various immobilized ALP systems, a single-stacked layer-by-layer assembly approach resulted in the highest level of enzymatic activity (30.1%) per unit mass of nanofiber support
D199A
metal-ligating residue, no activity at pH 8.5
H237A
non-metal linking residue, no activity at pH 8.5
Y202A
metal-ligating residue, no activity at pH 8.5
D101A
the mutant shows 64fold decreased catalytic efficiency compared to the wild type enzyme
D101A/D153A
the mutant shows 190fold decreased catalytic efficiency compared to the wild type enzyme
D101A/D153A/E322Y
the mutant shows 48000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/D153A/E322Y/K328A
the mutant shows 320000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/D153A/K328A
the mutant shows 5300fold decreased catalytic efficiency compared to the wild type enzyme
D101A/E322Y
the mutant shows 20000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/E322Y/K328A
the mutant shows 570000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/K328A
the mutant shows 23000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S
the mutant shows 11000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/D153A
the mutant shows 32000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/D153A/E322Y
the mutant shows 670000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/D153A/E322Y/K328A
the mutant shows 3700000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/D153A/K328A
the mutant shows 120000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/E322Y
the mutant shows 15000000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/E322Y/K328A
the mutant shows more than 30000000000fold decreased catalytic efficiency compared to the wild type enzyme
D101A/R166S/K328A
the mutant shows 2300000fold decreased catalytic efficiency compared to the wild type enzyme
D101S
weaker phosphate binding can be attributed to the increased flexibility of the Arg166 side chain, faster phosphate release is responsible for the 35fold higher activity
D153A
the mutant shows 230fold decreased catalytic efficiency compared to the wild type enzyme
D153A/E322Y
the mutant shows 270000fold decreased catalytic efficiency compared to the wild type enzyme
D153A/E322Y/K328A
the mutant shows 2000000fold decreased catalytic efficiency compared to the wild type enzyme
D153A/K328A
the mutant shows 1400fold decreased catalytic efficiency compared to the wild type enzyme
D153H
reduced magnesium affinity, maximual activity is only achieved with the addition of exogenous magnesium
D153H/K328A
reduced magnesium affinity, maximal activity is only achieved with the addition of exogenous magnesium
D153H/K328W
mutant enzyme containing Co2+ has higher catalytic efficiency than the wild-type enzyme containing cobalt
D369A
-
mutant enzyme shows reduced turnover rates and increased Km-value
D434E
-
site-directed mutagenesis, reduced activity, increased kcat and Km compared to the wild-type enzyme
E22Y
kcat/KM (1/M*sec) (4-nitrophenyl phosphate): 7200, (3-nitrobenzyl phosphate): 31, (methyl phosphate): 1.6, (methyl 4-nitrophenyl phosphate): 35, (bis-4-nitrophenyl phosphate): 0.07, (4-nitrophenyl sulfate): 0.0000029
E322K
-
site-directed mutagenesis, highly reduced activity
E322Y/K328A
the mutant shows 420000fold decreased catalytic efficiency compared to the wild type enzyme
E332Y
the mutant shows 88000fold decreased catalytic efficiency compared to the wild type enzyme
E341K
-
site-directed mutagenesis, highly reduced activity
H412Y
-
site-directed mutagenesis, highly reduced activity
K328C
lower phosphate affinity, alteration in the rate-limiting step
K328H
lower phosphate affinity, alteration in the rate-limiting step
R166K
kcat (1/sec) (substrate: 4-nitrophenyl phosphate): 0.65
R166Q
mutation has very little effect on turnover number, in presence of phosphate acceptor the substrate binding decreases over 50fold
R166S/D153A
the mutant shows 49000fold decreased catalytic efficiency compared to the wild type enzyme
R166S/D153A/E322Y
the mutant shows 33000000fold decreased catalytic efficiency compared to the wild type enzyme
R166S/D153A/E322Y/K328A
the mutant shows 140000000fold decreased catalytic efficiency compared to the wild type enzyme
R166S/D153A/K328A
the mutant shows 180000fold decreased catalytic efficiency compared to the wild type enzyme
R166S/E322Y/K328A
the mutant shows 1600000000fold decreased catalytic efficiency compared to the wild type enzyme
R166S/K328A
the mutant shows 2600000fold decreased catalytic efficiency compared to the wild type enzyme
S102A
activity is significantly less than that of the wild-type enzyme, but 100000-10000000fold greater than the non-enzymatic reaction,1000-10000fold reduction in the turnover number
S102C
activity is significantly less than that of the wild-type enzyme, but 100000-10000000fold greater than the non-enzymatic reaction, 100fold reduction in turnover number
S102G
activity is significantly less than that of the wild-type enzyme, but 100000-10000000fold greater than the non-enzymatic reaction, 1000-10000fold reduction in the turnover number
S102G/D101A/D153A/R166S/E322Y/K328A
inactive
S102L
activity is significantly less than that of the wild-type enzyme, but 100000-10000000fold greater than the non-enzymatic reaction, 1000-10000fold reduction in the turnover number
S105L
-
site-directed mutagenesis, reduced activity
T155M
-
site-directed mutagenesis, highly reduced activity
T59A
site-directed mutagenesis, exists as a dimer, shows catalytic activity and metal content similar to the wild-type enzyme
T59R
site-directed mutagenesis, exists as a monomer, shows 10000fold reduced activity compared to the wild-type, highly reduced metal content, highly reduced thermal stability
T81A
-
the T81A mutant displays a somewhat lower affinity than the wild-type enzyme for both substrate and phosphate, while kcat does not change significantly
W322A
kcat/KM (1/M*sec) (4-nitrophenyl phosphate): 8900, (3-nitrobenzyl phosphate): not determined, (methyl phosphate): not determined, (methyl 4-nitrophenyl phosphate): 18, (bis-4-nitrophenyl phosphate): 0.037, (4-nitrophenyl sulfate): not determined
A115V
-
activity in U2OS cells after 48h after transfection: 0.1%
A116T
-
mutant responsible for hypophosphatasia shows negligible alkaline phosphatase activity and a weak dominant negative effect when co-expressed with the wild-type enzyme, mutant exists as a monomer and heterogeneously associated aggregates covalently linked via disulfide bonds in contrast to wild-type enzyme which exists as a homodimer
A16V
-
in combination with P275T the mutation causes infantile hypophosphatasia, 7.2% of wild-type activity
C201Y
mutation identified in patient diagnosed with perinatal hypophosphatasia. Mutants exhibit a diminished alkaline phosphatase activity in the cells, where a 66 kDa immature form is predominant with a marginal amount of a 80 kDa mature form. The 66 kDa form exists as a monomer in contrast to a dimer form of wild-type. Only a small fraction of the mutant protein reaches cell surface as the 80 kDa mature form, most of the 66 kDa form is found to be endo-beta-N-acetylglucosaminidase H sensitive and rapidly degraded in proteasome following polyubiquitination
C489S
mutation identified in patient diagnosed with perinatal hypophosphatasia. Mutants exhibit a diminished alkaline phosphatase activity in the cells, where a 66 kDa immature form is predominant with a marginal amount of a 80 kDa mature form
G420A
naturally occuring mutant, reported in perinatal and childhood hypophosphatasia. Mutant lacks its alkaline phosphatase activity
G420S
naturally occuring mutant, reported in perinatal and childhood hypophosphatasia. Mutant lacks its alkaline phosphatase activity, although mutant protein is anchored to the cell surface lipid bilayers by glycosylphosphatidylinositol as an 80 kDa mature form bearing complex-type oligosaccharides similar to wild-type. Mutant G420S largely fails to assemble into the homodimer in contrast to wild-type
M278T
-
lethal mutation, 8.5% of wild-type activity
N417D
mutation abolishes the dimerization without perturbing its cell surface localization
N417E
mutation abolishes the dimerization without perturbing its cell surface localization
N417S
mutation associated with severe hypophosphatasia, mutants lack enzymic activity. Mutant undergoes N-linked oligosaccharide processing and appears on the cell surface similar to wild-type. Mutant fails to assemble into a dimer structure, which is needed for the catalytic function
P108L
inactive, the mutation is associated with dominant odontohypophosphatasia
P275T
-
in combination with A16V mutation causes infantile hypophosphatasia, 4% of wild-type activity
R119H
-
in combination with Y280D the mutation causes childhood hypophosphatasia, 33.4% of wild-type activity
R166A
-
mutation changes the inhibition mechanism of the mutant enzyme to a more complex mixed-type inhibition with decreased affinities for L-Leu and L-Phe
R206W
-
lethal mutation, 2.8% of wild-type activity
R255H
-
mutation (homozygote) causes infantile hypophosphatasia, 6.8% of wild-type activity
R54A
-
activity in U2OS cells after 48h after transfection: 0.1%
T394
-
lethal mutation, 0.3% of wild-type activity
V406A
-
mutant protein shows a markedly reduced alkaline phosphatase activity. Mutant is conveyed to the Golgi apparatus and incorporated into a cold detergent insoluble fraction (raft) at a rate similar to that of the wild-type. Mutant shows increased susceptibility to digestion by trypsin or proteinase K. When purified as a glycosylphosphatidylinositol-anchorless soluble form, mutant protein exhibits a remarkably lower Kcat /Km value compared with that of the wild-type TNSALP
V406F
-
replacement with phenylalanine results in a low enzyme activity, even though TNSALP (V406F) is processed to the 80 kDa mature form similarly to TNSALP (V406A) and appears on the cell surface like the wild-type protein
V406I
-
similar to wild-type, leucine and isoleucine can be successfully substituted for the valine residue
V406L
-
similar to wild-type, leucine and isoleucine can be successfully substituted for the valine residue
Y280D
-
in combination with R119H the mutation causes childhood hypophosphatasia, 1.3% of wild-type activity
K161S/K184S
the mutant shows much higher residual specific activity after maleimide activation than the wild type enzyme
G51C
-
kcat for 4-nitrophenyl phosphate is 15.8fold lower than wild-type enzyme. Km-value for 4-nitrophenyl phosphate is 2.8fold lower than wild-type value
H116D
-
slightly less heat-stable than the wild-type enzyme. Mutant enzyme shows much reduced catalytic efficiencies as compared to the wild-type enzyme. kcat/KM is 29.7fold lower than wild-type value
H116D/W274K
-
more heat-tolerant than the wild-type enzyme. Mutant enzyme shows much reduced catalytic efficiencies as compared to the wild-type enzyme. kcat/KM is 17.1fold lower than wild-type value
I50C
-
kcat for 4-nitrophenyl phosphate is 6fold lower than wild-type enzyme. Km-value for 4-nitrophenyl phosphate is 2.4fold lower than wild-type value
S52C
-
kcat for 4-nitrophenyl phosphate is 10.2fold lower than wild-type enzyme. Km-value for 4-nitrophenyl phosphate is 1.9fold lower than wild-type value
S53C
-
kcat for 4-nitrophenyl phosphate is 9.6fold lower than wild-type enzyme. Km-value for 4-nitrophenyl phosphate is 1.9fold lower than wild-type value
W274K
-
more heat-tolerant than the wild-type enzyme. Mutant enzyme shows much reduced catalytic efficiencies as compared to the wild-type enzyme. kcat/KM is 30.6fold lower than wild-type value
F355W
-
the mutant shows slightly reduced catalytic efficiency compared to the wild type enzyme
R336L
-
the mutant shows extreme thermo-instability and its activity drops by half at 0.1 M of urea within 1.5 h
W155F
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W274F
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W301F
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W460F
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W460Y
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W475F
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W512F
-
the mutant shows wild type activity
D153G
-
the mutant has 5fold higher catalytic activity but no change in Km at pH 8.0 in 50 mM Tris-HCl. The mutation also affects Mg2+ binding, resulting in an enzyme with lower metal affinity. The mutation also affects the position of the water ligands of Mg2+ and the loop Gln152-Thr155 is shifted by 0.3 A away from the active site. The weaker Mg2+ binding of the mutant compared with the wild type is caused by an altered coordination sphere in the proximity of the Mg2+ ion and also by the loss of an electrostatic interaction, Mg2+/COO-Asp153, in the mutant
D153G
weaker phosphate binding can be attributed to the increased flexibility of the Arg166 side chain, faster phosphate release is responsible for the 5fold higher activity, reduced magnesium affinity, maximal activity is only achieved with the addition of exogenous magnesium
D369N
-
mutant enzyme shows reduced turnover rates and increased Km-value. The reaction mechanism of the mutant enzyme involves only 1 metal with the possible assistance of a His side chain
D369N
-
site-directed mutagenesis, highly reduced activity
K328A
lower phosphate affinity, alteration in the rate-limiting step
K328A
the mutant shows 840fold decreased catalytic efficiency compared to the wild type enzyme
R166A
mutation has very little effect on turnover number, in presence of phosphate acceptor the substrate binding decreases over 50fold, phosphate inhibition is reduced 50fold
R166A
kcat (1/sec) (substrate: 4-nitrophenyl phosphate): 0.3
R166S
mutation has very little effect on turnover number, in presence of phosphate acceptor the substrate binding decreases over 50fold, phosphate inhibition is reduced 50fold
R166S
kcat (1/sec) (substrate: 4-nitrophenyl phosphate): 0.5
R166S
kcat/KM (1/M*sec) (4-nitrophenyl phosphate): 100000, (3-nitrobenzyl phosphate): 2300, (methyl phosphate): 110, (methyl 4-nitrophenyl phosphate): 0.48, (bis-4-nitrophenyl phosphate): 0.05, (4-nitrophenyl sulfate): 0.000058
R166S
the mutant shows 6300fold decreased catalytic efficiency compared to the wild type enzyme
R166S/E322Y
kcat/KM (1/M*sec) (4-nitrophenyl phosphate): 1.6, (3-nitrobenzyl phosphate): below 0.2, (methyl phosphate): not determined, (methyl 4-nitrophenyl phosphate): 0.24, (bis-4-nitrophenyl phosphate): 0.021, (4-nitrophenyl sulfate): below 0.000001
R166S/E322Y
the mutant shows 39000000fold decreased catalytic efficiency compared to the wild type enzyme
additional information
-
gene disruption reveals that it is the sole alkaline phosphatase in Campylobacter jejuni
additional information
-
substitution of the conserved twin-arginine residues near the N-terminus show that they are essential for enzyme activity
additional information
alkaline phosphatase is subject to circular permutation with its novel termini at the loops near the active site, and the original termini are linked by a flexible linker. While a permutant with the termini at original residues 407 and 408 is not active, a permutant with termini at residues 90 and 94 shows significant activity. Also the addition of a randomized residue at position 91 and 93 as well as outer peptide epitopes yields several mutants with specific activity comparable to the wild-type enzyme with similar outer peptides
additional information
-
alkaline phosphatase is subject to circular permutation with its novel termini at the loops near the active site, and the original termini are linked by a flexible linker. While a permutant with the termini at original residues 407 and 408 is not active, a permutant with termini at residues 90 and 94 shows significant activity. Also the addition of a randomized residue at position 91 and 93 as well as outer peptide epitopes yields several mutants with specific activity comparable to the wild-type enzyme with similar outer peptides
additional information
the results show that the role of the arginine side chain extends beyond its positive charge, as the Arg166Lys mutant is as compromised in activity as Arg166Ser. Through measurement of individual reaction steps, a free energy profile for the hydrolysis of the enzyme-phosphate intermediate is constructed. This analysis indicates that the arginine side chain strengthens binding by approximately 3 kcal/mol and provides an additional 1-2 kcal/mol stabilization of the chemical transition state
additional information
-
the results show that the role of the arginine side chain extends beyond its positive charge, as the Arg166Lys mutant is as compromised in activity as Arg166Ser. Through measurement of individual reaction steps, a free energy profile for the hydrolysis of the enzyme-phosphate intermediate is constructed. This analysis indicates that the arginine side chain strengthens binding by approximately 3 kcal/mol and provides an additional 1-2 kcal/mol stabilization of the chemical transition state
additional information
HaALP is identified in the target insect gut brush border membrane vesicles as a receptor of the Bacillus thuringiensis coded Cry1Ac toxin. Lectin-ligand immunoblot assay detects the presence of alpha-GalNAc residue at the nonreducing terminal of the glycan structure in the membrane bound HaALP protein which mediates the toxin-receptor interaction
additional information
HaALP is identified in the target insect gut brush border membrane vesicles as a receptor of the Bacillus thuringiensis coded Cry1Ac toxin. Lectin-ligand immunoblot assay detects the presence of alpha-GalNAc residue at the nonreducing terminal of the glycan structure in the membrane bound HaALP protein which mediates the toxin-receptor interaction
additional information
-
HaALP is identified in the target insect gut brush border membrane vesicles as a receptor of the Bacillus thuringiensis coded Cry1Ac toxin. Lectin-ligand immunoblot assay detects the presence of alpha-GalNAc residue at the nonreducing terminal of the glycan structure in the membrane bound HaALP protein which mediates the toxin-receptor interaction
additional information
-
characterization of 11 novel mutations in the tissue non-specific alkaline phosphatase gene responsible for hypophosphatasia and genotype-phenotype correlations
additional information
deletion of five and nine N-terminal amino acis in TNAP reduced and abolished AP activity, respectively. The N-terminal amino acid deletions affects the rate of substrate catalysis (kcat), with a minor effect on the Michaelis constant
additional information
-
deletion of five and nine N-terminal amino acis in TNAP reduced and abolished AP activity, respectively. The N-terminal amino acid deletions affects the rate of substrate catalysis (kcat), with a minor effect on the Michaelis constant
additional information
deletion of nine N-terminal amino acid residues in PLAP reducs its AP activity and heat stability, while deletion of 25 amino acids results in an inactive enzyme. The N-terminal amino acid deletions affect the rate of substrate catalysis (kcat), with a minor effect on the Michaelis constant
additional information
-
deletion of nine N-terminal amino acid residues in PLAP reducs its AP activity and heat stability, while deletion of 25 amino acids results in an inactive enzyme. The N-terminal amino acid deletions affect the rate of substrate catalysis (kcat), with a minor effect on the Michaelis constant
additional information
-
to determine the mineralizing ability of mutant TNAP proteins, a functional assay is developed that uses U2OS osteoblast-like cells. Expression plasmids containing TNAP mutant cDNAs are constructed and introduced into U2OS cells, which are derived from a human osteosarcoma and exhibit very low alkaline phosphatase (ALP) activity and disabled mineralization. U2OS cells, in which active TNAP cDNAs are introduced, express high ALP activity and mineralized their circumstance when they are cultured with beta-glycerophosphate. An in vitro mineralization assay of U2OS cells transfected with moderate allele cDNAs shows that approximately 35% of TNAP enzymatic activity may be the threshold value for mineralization. In addition, U2OS cells transfected with wild-type TNAP and polymorphism TNAP cDNA shows PHEX (phosphate-regulating gene with homologies to endopeptidases on the X chromosome) induction as in SaOS-2 cells
additional information
-
hydrolysis of pyrophosphate by rat aortic rings is reduced about half in aortas from mice lacking TNAP
additional information
ALP is completely inactivated in the presence of 0.2 mM N-bromosuccinimide. Inactivation of purified alkaline phosphatase by N-bromosuccinimide is dependent on modification of only one of five tryptophan residues in the enzyme. Substrate protection experiments show that the tryptophan residue is not located at the substratebinding site but is involved in the catalytic activity
additional information
-
ALP is completely inactivated in the presence of 0.2 mM N-bromosuccinimide. Inactivation of purified alkaline phosphatase by N-bromosuccinimide is dependent on modification of only one of five tryptophan residues in the enzyme. Substrate protection experiments show that the tryptophan residue is not located at the substratebinding site but is involved in the catalytic activity
additional information
-
TNAP activity increases twofold in intact aortas and in aortic homogenates from rats made uremic by feeding adenine or by 5/6 nephrectomy. Immunoblotting showsS an increase in protein abundance but there is no increase in TNAP mRNA. An increase in TNAP activity and pyrophosphate hydrolysis also occurres when aortic rings from normal rats are incubated with uremic rat plasma
additional information
-
PhoX knockout mutant shows 10fold diminished compared with wild-type
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10
antarctic bacterium
-
10 min, little loss of activity
115
inactivation within 30 min
20
-
30 min, 50% loss of wild-type activity at 19.5°C
20 - 65
the enzyme remains stable after 24 h incubation between 20 and 65°C
22 - 47
-
at 22, 37, and 47°C, the enzyme retains 87, 57, and 40% of activity, respectively, after 6 h of incubation, which declines faster at 57 and 60°C
4 - 10
-
the enzyme keeps 67 and 43% of activity after 1 h at 10°C and 4°C, respectively
4 - 47
-
the enzyme retains at least 80% activity it is incubated for 1 h at temperature ranging from 4°C to 47°C
41
-
pure enzyme plus substrate is affected
47
-
sucrose-released enzyme in presence of substrate is inactivated
50 - 70
-
the half-lives for the enzyme incubated in saltfree buffer at 50°C, 60°C, and 70°C is determined to be 5.3 h, 7.9 min, and 1.7 min. All the salts tested show the ability to stabilize the enzyme when incubated at 70°C
54
-
20 min, about 45% loss of activity of the liver enzyme, about 60% loss of activity of the bone enzyme
61
-
allozyme D, half-life 10 min, in presence of Zn2+ and Mg2+, pH 9.8
69
-
t1/2: 6 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
72
-
allozyme S and F, half-life 10 min, in presence of Zn2+ and Mg2+, pH 9.8
73
-
t1/2: 4 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
87
-
half-life of the recombinant enzyme is 38 min
10 - 30
-
10 - 30
100% active for 2 h
100
-
2.5 h, 33% loss of activity. Half-life: 363 min
100
-
40 min, in presence of 40 mM Co2+, 3% loss of activity
15
antarctic bacterium
-
10 min, 40% loss of activity
25
-
stable for 10 days
25
-
t1/2: 94 min for wild-type value
30
-
pH 8, 120 min, stable
30
-
t1/2: 79 min for wild-type enzyme, 2600 min for mutant enzyme h116D
30
-
the enzyme has a half-life of less than 1 min when heated at 30°C with no additional ions in the buffer
35
-
pH 10, isoenzyme III, 120 min, stable
35
-
t1/2: 31 min for wild-type enzyme, 63 min for mutant enzyme H116D, 2200 min for mutant enzyme H116S/W274K
37
-
1 h, 25% loss of activity, 12 h, 62% loss of activity
40
antarctic bacterium
-
half-life: 2 min
40
-
pH 9-9.5, 120 min, stable
40
half-life 27 min, presence of 2 mM EDTA
40
-
t1/2: 12 min for wild-type enzyme, 231 min for mutant enzyme W274K, 30 min for mutant enzyme H116D, 217 min for mutant enzyme H116D/W274K
45
antarctic bacterium
-
15 min, 50% inactivation
45
half-life 16 min, presence of 2 mM EDTA
45
-
pH 7.5, 60 min, rapid inactivation above
45
-
t1/2: 23 min, native enzyme
45
-
1 h 45°C: 75% remaining activity
45
-
t1/2: 2.3 min for wild-type enzyme, 26 min for mutant enzyme W274K, 1.1 min for mutant enzyme H116D, 96 min for mutant enzyme H116D/W274K
50
-
enzyme rapidly inactivated at 50°C
50
antarctic bacterium
-
15 min, complete inactivation
50
-
88% loss of activity after 55 min in glycine buffer, 72% loss of activity after 120 min in pasteurized milk
50
-
t1/2: 38 min, native enzyme
50
-
30 min, aout 13% loss of activity
50
-
stable up to, 15 min
50
-
t1/2: 182 min, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction (30 min, 15 mM)
50
-
t1/2: 58 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
50
-
t1/2: 77 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
50
-
10 min, partial inactivation
50
-
denaturation follows first order kinetics with t1/2 values ranging from 3.5 min to 57.7 min
50
270 min, about 10% loss of activity
50
-
t1/2: 0.7 min for wild-type enzyme, 6 min for mutant enzyme W274K, 0.8 min for mutant enzyme H116D, 10 min for mutant enzyme H116D/W274K
53
-
t1/2: 15 min, native enzyme
53
-
t1/2: 20 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
53
-
t1/2: 26 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
55
antarctic bacterium
-
10 min, complete and irreversible inactivation
55
-
16 min, 95% inactivation
55
-
16 min, 55% inactivation
55
-
15 min, about 20% loss of activity
55
-
16 min, 61% inactivation
55
-
16 min, complete inactivation
55
-
16 min, 83% inactivation
55
-
16 min, 80% inactivation
55
-
t1/2: 2.75 min, native enzyme
55
-
t1/2: 41 min, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction (30 min, 15 mM)
55
-
16 min, 66% inactivation
55
-
90 min, 50% loss of activity
55
-
15 min, about 80% loss of activity
55
-
16 min, 92% inactivation of enzyme from 20 day term fetal placentae, 86% loss of activity of enzyme from anestrus control uteri, 30% inactivation of the enzyme from small intestine
55
-
t1/2: 1.2 min for mutant enzyme W274K, 0.2 min for mutant enzyme H116D, 5 min for mutant enzyme H116D/W274K
55
-
Tm-value for mutant enzyme H116D
56
-
-
56
-
50% inactivation of the placental enzyme after 10.9 min, 50% inactivation of the liver enzyme after 16.0 min
56
-
t1/2: 10 min, native enzyme
56
-
a monoclonal antibody based capture immunoassay is used to study the kinetics of alkaline phosphatase heat denaturation in bovine milk over a range 50-60°C for 5 to 60 min using a colorimetric quantification of the enzyme activity as a reference test. A denaturation midpoint is obtained at 56°8C for a 30 min heating
56
-
50% inactivation of the placental enzyme after 23.1 min, 50% inactivation of the liver enzyme after 14.2 min
56
-
50% inactivation of the liver and the placental enzyme after 6.6 min
56
-
50% inactivation of the placental enzyme after 12.3 min, 50% inactivation of the liver enzyme after 18.2 min
56
-
pH 10.6, 20 min, the isoenzymes from intestine, liver/bone/kidney and from term-placenta are unstable
56
-
placental enzyme is stable, 50% inactivation of the liver enzyme after 8.2 min
56
-
15 min, 3-4% remaining activity for all three isozymes
56
-
50% inactivation of the placental enzyme after 8.2 min, 50% inactivation of the liver enzyme after 18.7 min
56
-
50% inactivation of the placental enzyme after 4.4 min, 50% inactivation of the liver enzyme after 7.9 min
56
-
50% inactivation of the placental enzyme after 2.3 min, 50% inactivation of the liver enzyme after 5.8 min
56
-
50% inactivation of the placental enzyme after 10.8 min, 50% inactivation of the liver enzyme after 9.0 min
56
-
t1/2: 12 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
56
-
t1/2: 14 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
56
-
50% inactivation of the placental enzyme after 2.2 min, 50% inactivation of the liver enzyme after 5.0 min
56
15 min, 100% inactivation
56
15 min, 27% inactivation, isoenzyme rTI2B
56
15 min, 32% inactivation
56
15 min, 52% inactivation, isoenzyme rTI2A
56
15 min, 78% inactivation, bone isoenzyme
56
-
50% inactivation of the placental enzyme after 9.7 min, 50% inactivation of the liver enzyme after 3.5 min
57
-
Tm-value for mutant enzymeW274K is 57.2°C
57
-
Tm-value for wild-type enzyme is 56.5°C
58
-
t1/2: 80 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
58
-
t1/2: 84 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
58
-
15 min, about 55% loss of activity
58
-
t1/2: 1 min, native enzyme
59
-
t1/2: 6 min, native enzyme
59
-
t1/2: 6 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
59
-
t1/2: 7 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
59
-
Tm-value for mutant enzyme H116D/W274K is 58.6°C
60
-
60 min, about 5% of maximal activity
60
-
50 min, complete inactivation
60
-
complete inactivation after 50 min in glycine buffer, 15% loss of activity after 120 min in pasteurized milk
60
-
30 min, 96.5% loss of activity
60
-
pH 8.5, half-life: 1.7 min, in presence of 3 M NaCl 3.2 min
60
-
45% loss of activity
60
-
about 65% loss of activity after 1 h, complete loss of activity after 6 h
60
-
5 min, about 80% loss of activity
60
-
stable for at least 20 min
60
-
complete loss of activity
60
-
fully stable at up to 1 h
60
-
biphasic thermoinactivation, t1/2 of mutant enzyme os-1 is 31.7 min for the fast phase and 3.0 h for the slow phase. The wild-type enzyme shows t1/2 values of 4.8 min and 80.3 min, respectively
60
-
t1/2: 0.7 min, native enzyme
60
-
t1/2: 10 min, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction (30 min, 15 mM)
60
-
5 min, nearly complete loss of activity
60
-
t1/2: 0.5 min for mutant enzyme H116D/W274K
62
-
t1/2: 35 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
62
-
t1/2: 37 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
64
-
120 min, about 15% loss of activity of the cytolasmic isoenzyme, about 5% loss of activity of the nuclear isoenzyme
64
-
allozyme SD and FD, half-life 10 min, in presence of Zn2+ and Mg2+, pH 9.8
65
-
5.5 h, 15% loss of activity
65
-
50% inactivation of the placental enzyme after 1.04 min, 50% inactivation of the liver enzyme after 1.32 min
65
-
t1/2: 1 min, native enzyme
65
-
t1/2: 24 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
65
-
t1/2: 25 min, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
65
-
50% inactivation of the placental enzyme after 1.2 min, 50% inactivation of the liver enzyme after 1.31 min
65
-
50% inactivation of the placental enzyme after 0.97 min, 50% inactivation of the liver enzyme after 0.92 min
65
-
50% inactivation of the placental enzyme after 0.67 min, 50% inactivation of the liver enzyme after 0.6 min
65
-
placental enzyme is stable, 50% inactivation of the liver enzyme after 1.05 min
65
-
50% inactivation of the placental enzyme after 0.76 min, 50% inactivation of the liver enzyme after 0.45 min
65
-
50% inactivation of the placental enzyme after 0.21 min, 50% inactivation of the liver enzyme after 0.32 min
65
-
50% inactivation of the placental enzyme after 0.58 min, 50% inactivation of the liver enzyme after 0.8 min
65
-
50% inactivation of the placental enzyme after 0.52 min, 50% inactivation of the liver enzyme after 0.35 min
65
-
t1/2: 2.6 min, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction (30 min, 15 mM)
65
-
50% inactivation of the placental enzyme after 0.42 min, 50% inactivation of the liver enzyme after 0.84 min
65
-
50% inactivation of the placental enzyme after 0.91 min, 50% inactivation of the liver enzyme after 0.65 min
65
-
stable for more than 24 h
70
-
60 min, about 50% loss of activity
70
-
complete inactivation after 20 min in glycine buffer, complete inactivation after 40 min in pasteurized milk
70
-
30% loss of activity after 10 min, 98% loss of activity after 20 min
70
-
half-life 19 min in Tris-HCl, 2.3 min in CHES
70
-
1% remaining activity after 10 min
75
-
10 min, complete inactivation
75
-
addition of Co2+ after treatment with EDTA results in an enzyme that has low tolerance toward heat treatment of more than 75°C, suggesting that Co2+ destabilizes the tertiary structure of the enzyme at high temperature
80
the enzyme retains more than 60% activity at 80?C after 1 h incubation
80
-
complete inactivation after 4 min in glycine buffer, complete inactivation after 10 min in pasteurized milk
80
retains more than 50% activity after incubating for 6 h at 80ºC
80
-
half-life: 199 min, Mg2+ can increase half-life of the enzyme twice
90
-
5.5 h, 24% loss of activity. Half-life: 562 min
90
-
10 min, pH 8.5, containing 10 mM MgCl2 and 1 mM ZnSO4, about 50% loss of activity
90
80% remaining activity after 36 h
90
-
half-life: 238 min, in presence of Co2+
90
-
half-life of the native enzyme is 4 h in presence of 2 mM Co2+
95
-
in presence of 0.1 mM Mg2+, 10 min, 50% loss of activity
95
-
10 min, pH 8.5, containing 10 mM MgCl2 and 1 mM ZnSO4, aout 80% loss of activity
95
-
5 min, in absence or presence of 10 mM Mg2+, inactivation of CAPase, while IApase is relatively stable showing loss of 30% activity after 5 min and loss of 80% activity after 30 min
95
60 min, about 45% loss of activity
additional information
residual activity after after thermal inactivation at 60°C, 120 min: 2.4%
additional information
-
-
additional information
-
the thermal stabilities of the immobilized phosphatase are higher than those of the native one
additional information
enzyme gets quickly inactivated at 80°C for 15 min, exhibiting a half-life of 8 min at 70°C
additional information
-
enzyme gets quickly inactivated at 80°C for 15 min, exhibiting a half-life of 8 min at 70°C
additional information
-
Tris-HCl partly protects against heat inactivation
additional information
-
addition of lipopolysaccharide, phosphatidylethanolamine or a combination of both increases the temperature of inactivation
additional information
-
high molecular weight alkaline phosphatase is less heat and urea stable than low molecular weight alkaline phosphatase
additional information
-
low molecular weight alkaline phosphatase is more heat and urea stable than high molecular weight alkaline phosphatase
additional information
-
Mg2+ protects against thermal inactivation up to 80°C
additional information
shrimp
-
heat-labile, the enzyme is inactivated by a short rise in temperature
additional information
-
thermostability is increased 30fold by Co2+ and 23fold by Mg2+
additional information
-
Co2+ and Zn2+ increase the thernal stability by 30 and 23fold at 90°C
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