Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(Pro-Pro-Gly)5
-
at concentrations higher than 0.56 mM, substrate inhibition observed
1,2,3-trihydroxybenzene
-
-
1,2-dihydroxybenzene
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
1,3-dihydroxybenzene
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
1,4-dihydrophenanthrolin-4-one-3-carboxylic acid
1,4,DPCA
1,4-dihydrophenanthroline-4-one-3-carboxylic acid
2,4-Dihydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
2,4-pyridine dicarboxylate
-
-
2,5-Dihydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
2,6-dihydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
2,7,8-trihydroxyanthraquinone
-
50% inhibition at 0.047 mM, competitive inhibitor with respect to 2-oxoglutarate, non-competitive with regard to ascorbate, uncompetitive with regard to protocollagen. The inhibition is greatly enhanced in the absence of Fe2+, structural requirements for inhibition
2-Hydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
2-oxoadipinate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
2-oxobutyrate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
2-oxoglutarate
-
at concentrations higher than 0.5 mM, decreases activity
2-oxovalerate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
3,4,5-Trihydroxybenzoate
-
-
3,4-dihydroxybenzoic acid
-
-
3,4-dihydroxycinnamate
-
competitive with respect to 2-oxoglutarate and ascorbate
3,4-dihydroxymandelate
-
competitive with respect to 2-oxoglutarate and ascorbate and noncompetitive with respect to Fe2+
3,4-dihydroxyphenyl acetate
IC50: 0.3 mM
3,4-Dihydroxyphenylacetate
3,4-Dihydroxyphenylpropionate
3,5-Dihydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
3-carboxy-4-oxo-3,4-dihydro-1,10-phenanthroline
3-hydroxybutyrate
-
less than 10% inhibition
3-hydroxypyridine-2-carbonyl-glycine
3-oxoglutarate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
5-Azidopyridine-2-carboxylic acid
8-(N-butyl-N-ethylcarbamoyl)-1,4-dihydrophenanthrolin-4-one-3-carboxylic acid
8-hydroxyquinoline
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
adipinate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
ADP-ribose
-
weak inhibitor
antimycin A
-
18% inhibition at 0.02 mM
benzene 1,2-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Benzene 1,3-dicarboxylate
Benzene 1,4-dicarboxylate
benzoate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
benzyloxycarbonyl-Phe-Opr-Gly-benzyl ester
Benzyloxycarbonyl-Phe-oxaproline-Gly-benzyl ester
citrate
-
competitive inhibition with respect to 2-oxoglutarate
CO2
-
5% inhibition at 3.6 mM, 35% inhibition at 7.2 mM and 75% inhibition at 12 mM
cobalt chloride
-
inhibition of PHDs blocks the response of mTORC1 to amino acids
Collagen
-
product inhibitor, noncompetitive with respect to all substrates of the reaction
concanavalin A
-
partially inhibits, when the enzyme is assayed in the absence of bovine serum albumin
-
CuCl2
-
0.4 mM, 67% inhibition
Cupferron
-
28% inhibition at 0.02 mM
deferoxamine mesylate
-
-
diethyl dicarbonate
-
98% inhibition at 1 mM
diethyldithiocarbamate
-
10% inhibition at 0.02 mM
Diethylenetriaminepentaacetic acid
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
dimethyl oxalylglycine
-
DMOG, the effect is HIF-independent
dimethyloxallyl glycine
-
inhibition of PHDs blocks the response of mTORC1 to amino acids
dimethyloxalylalanine
-
50% inhibition in chicken embryo calvaria at 1 mM
dimethyloxalylglycine
-
50% inhibition in chicken embryo calvaria at 0.002 mM, inhibitor of hydroxyproline synthesis in embryonic chicken lung
epinephrine
-
competitive inhibition with respect to Fe2+
ethylpyridine-2,4-dicarboxylate
glutamyl-3,4-dehydroprolyl-bradykinin
-
H2O2
-
94% inhibition at 1 M, dissociation of the enzyme, 12% of the enzyme remains in the tetrameric form
Hg2+
-
causes a 20-30% fall in activity
HOE077
-
decrease in enzyme activity by 15%
isocitrate
-
competitive inhibition with respect to 2-oxoglutarate
L-galactono gamma-lactone
-
-
L-mimosine
-
50 mg/kg/day for 2 weeks
Lactate
-
less than 10% inhibition
levulinate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
malate
-
competitive inhibition with respect to 2-oxoglutarate
MgSO4
-
0.4 mM, 30% inhibition
Mn2+
-
causes a 20-30% fall in activity
MnSO4
-
0.4 mM, 62% inhibition
N,N'-diethylpyridine 2,4-dicarboxamide
N-((3-hydroxy-6-chloroquinolin-2-yl)carbonyl)glycine
-
-
N-(4-Azido-2-nitrophenyl)-glycyl-(Pro-Pro-Gly)5
N-Hydroxyethylenediaminetriacetic acid
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
N-oxalylglycine
-
oxaloglycine derivative, inhibitor
N-[(6-chloro-3-hydroxyquinolin-2-yl)carbonyl]glycine
-
NiCl2
-
0.4 mM, 98% inhibition
oxaloacetate
-
competitive inhibition with respect to 2-oxoglutarate
oxalyl-beta-alanine
-
competitive inhibition with respect to 2-oxoglutarate
oxalylalanine
-
inhibits purified enzyme, competitive inhibition with respect to 2-oxoglutarate, 50% inhibition of microsomal enzyme at 0.123 mM
oxalylcystine
-
competitive inhibition with respect to 2-oxoglutarate
oxalylsarcosine
-
noncompetitive inhibition with respect to 2-oxoglutarate
Pd2+
-
strong irreversible inhibition, competitive with respect to Fe2+
phosphoribosyl adenosine monophosphate
-
46% inhibition at 25 nM, 87% inhibition at 50 nM
Poly(ADP-ribose)
-
near complete inhibition at 6 nM, the effect is noncompetitive with respect to the binding of the cofactors ascorbate and alpha-ketoglutarate or of the substrate
poly(L-Pro)
0.03 mM, 50% inhibition
poly-L-hydroxyproline
-
MW: 30000, inhibitory
-
potassium bromide
-
over 80% inhibition at 500 mM
potassium chloride
-
over 80% inhibition at 500 mM
potassium fluoride
-
over 90% inhibition at 500 mM
potassium iodide
-
over 80% inhibition at 500 mM
pyridine 2,3-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Pyridine 2,4-dicarboxylate
Pyridine 2,5-dicarboxylate
pyridine 2,6-dicarboxylate
-
competitive with respect to Fe2+ and noncompetitive with respect to 2-oxoglutarate
Pyridine 3,4-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Pyridine 3,5-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
pyridine 3-carboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Pyridine 4-carboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Pyridine-2,4-dicarboxylate
Pyridine-2,5-dicarboxylate
Ribosyl-ribosyl-adenine
-
43% inhibition at 25 nM, 85% inhibition at 50 nM
Ribosyl-ribosyl-hypoxanthine
-
40% inhibition at 25 nM, 86% inhibition at 50 nM
rosiglitazone
-
decrease in enzyme activity by 32.3%
S-nitroso-N-acetylpenicillamine
-
hyperoxia attenuates the inhibitory effect of NO on HIF-1alpha prolyl hydroxylation
S-nitrosoglutathione
-
hyperoxia attenuates the inhibitory effect of NO on HIF-1alpha prolyl hydroxylation
Salicylyl hydroxamate
-
-
sodium bromide
-
over 80% inhibition at 500 mM
sodium chloride
-
over 80% inhibition at 500 mM
sodium iodide
-
over 90% inhibition at 500 mM
sodium pyrocatechol disulfonate
-
98-100% inhibition at 0.1 mM
trifluorothienylbutanedione
-
48% inhibition at 0.05 mM
ZnSO4
-
0.4 mM, 84% inhibition
(Gly-Pro-Gly)n
-
competitive inhibitors with respect to the polypeptide substrate
(Gly-Pro-Gly)n
-
competitive inhibitors with respect to the polypeptide substrate
(Pro-Ala-Gly)n
-
competitive inhibitors with respect to the polypeptide substrate
(Pro-Ala-Gly)n
-
competitive inhibitors with respect to the polypeptide substrate
1,10-phenanthroline
-
-
1,10-phenanthroline
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
1,10-phenanthroline
-
91% inhibition at 0.02 mM
1,4-dihydrophenanthroline-4-one-3-carboxylic acid
-
purified enzyme, competitive inhibitor of 2-oxoglutarate
1,4-dihydrophenanthroline-4-one-3-carboxylic acid
-
potent competitive inhibitor of collagen hydroxylation in the oestradiol-stimulated uterus in vivo
2,2'-dipyridyl
-
-
2,2'-dipyridyl
-
50% inhibition at 0.06 mM
2,2'-dipyridyl
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
2,2'-dipyridyl
-
87% inhibition at 0.02 mM
2,3-Dihydroxybenzoate
-
-
2,3-Dihydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
2,3-Dihydroxybenzoate
-
-
2-oxosuccinate
-
i.e. oxaloacetate
2-oxosuccinate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+; i.e. oxaloacetate
2-oxosuccinate
-
i.e. oxaloacetate
3,4-dihydroxybenzoate
-
-
3,4-dihydroxybenzoate
-
-
3,4-dihydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
3,4-dihydroxybenzoate
-
-
3,4-dihydroxybenzoate
-
-
3,4-dihydroxybenzoate
-
-
3,4-Dihydroxyphenylacetate
-
-
3,4-Dihydroxyphenylacetate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
3,4-Dihydroxyphenylacetate
-
-
3,4-Dihydroxyphenylacetate
-
-
3,4-Dihydroxyphenylacetate
-
-
3,4-Dihydroxyphenylacetate
-
-
3,4-Dihydroxyphenylacetate
-
-
3,4-Dihydroxyphenylpropionate
-
competitive with respect to 2-oxoglutarate and ascorbate
3,4-Dihydroxyphenylpropionate
-
-
3,4-Dihydroxyphenylpropionate
-
-
3,4-Dihydroxyphenylpropionate
-
-
3,4-Dihydroxyphenylpropionate
-
-
3-carboxy-4-oxo-3,4-dihydro-1,10-phenanthroline
-
3-carboxy-4-oxo-3,4-dihydro-1,10-phenanthroline
-
-
3-hydroxypyridine-2-carbonyl-glycine
-
3-hydroxypyridine-2-carbonyl-glycine
-
-
4-hydroxybenzoate
-
-
4-hydroxybenzoate
-
competitive with respect to 2-oxoglutarate, and noncompetitive with respect to ascorbate
4-oxo-5,6-epoxyhexanoate
-
Caenorhabditis elegans exposed to the esterified epoxy ketone displays the phenotype of a worm lacking P4H
4-oxo-5,6-epoxyhexanoate
-
-
5-Azidopyridine-2-carboxylic acid
-
incorporated in the alpha subunit of the enzyme, complete inactivation of the enzyme by incorporation of 2 mol of photoaffinity label per mol of tetramer
5-Azidopyridine-2-carboxylic acid
-
-
8-(N-butyl-N-ethylcarbamoyl)-1,4-dihydrophenanthrolin-4-one-3-carboxylic acid
-
purified enzyme, competitive inhibitor of 2-oxoglutarate
8-(N-butyl-N-ethylcarbamoyl)-1,4-dihydrophenanthrolin-4-one-3-carboxylic acid
-
potent competitive inhibitor of collagen hydroxylation in the oestradiol-stimulated uterus in vivo
alpha,alpha'-dipyridyl
-
an Fe2+ chelator
alpha,alpha'-dipyridyl
-
an Fe2+ chelator
alpha,alpha'-dipyridyl
-
an Fe2+ chelator
alpha,alpha'-dipyridyl
-
an Fe2+ chelator
alpha,alpha'-dipyridyl
-
an Fe2+ chelator
alpha,alpha'-dipyridyl
-
5 mM, potent inhibitor
alpha,alpha'-dipyridyl
-
an Fe2+ chelator
ascorbate
-
at high concentrations
ascorbate
-
the inhibition may result from competition for binding at the 2-oxoacid binding site between 2-oxoglutarate and L-ascorbate
Benzene 1,3-dicarboxylate
-
-
Benzene 1,3-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Benzene 1,4-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Benzene 1,4-dicarboxylate
-
competitive inhibition with respect to ascorbate
benzyloxycarbonyl-Phe-Opr-Gly-benzyl ester
-
50% inactivation in 1 h at 0.0008 mM, the most effective inhibitor within oxaproline peptides
benzyloxycarbonyl-Phe-Opr-Gly-benzyl ester
-
50% inactivation in 1 h at 0.0008 mM, the most effective inhibitor within oxaproline peptides
Benzyloxycarbonyl-Phe-oxaproline-Gly-benzyl ester
-
-
Benzyloxycarbonyl-Phe-oxaproline-Gly-benzyl ester
-
-
Beta-lactam antibiotics
-
-
Beta-lactam antibiotics
-
-
bradykinin analogs
-
especially those in which the proline in the -X-Pro-Gly- triplet is replaced by certain proline analogues, the addition of a glutamyl residue to the N-terminal end of 3,4-dehydroprolyl- or trans-4-hydroxyprolyl-bradykinin considerably increases their effectiveness
-
bradykinin analogs
-
especially those in which the proline in the -X-Pro-Gly- triplet is replaced by certain proline analogues, the addition of a glutamyl residue to the N-terminal end of 3,4-dehydroprolyl- or trans-4-hydroxyprolyl-bradykinin considerably increases their effectiveness
-
catechol analogues
-
inhibitor of the reaction due in part to the chelation of Fe2+
-
catechol analogues
-
inhibitor of the reaction due in part to the chelation of Fe2+
-
Cd2+
Q81LZ8
the binding of Cd2+ induces a conformational change in the enzyme structure compared to the wild-type enzyme, overview
Cd2+
-
competitive versus Fe2+
Cd2+
-
competitive versus Fe2+
Cd2+
-
competitive versus Fe2+
Cd2+
-
competitive versus Fe2+
Cd2+
-
competitive versus Fe2+
Cd2+
-
competitive versus Fe2+
ciclopirox olamine
-
an Fe2+ chelator
ciclopirox olamine
-
an Fe2+ chelator
ciclopirox olamine
-
an Fe2+ chelator
ciclopirox olamine
-
an Fe2+ chelator
ciclopirox olamine
-
an Fe2+ chelator
ciclopirox olamine
-
an Fe2+ chelator
Co2+
Q81LZ8
active site binding structure analysis, in both Co(II)-bound structures, in addition to the catalytic triad residues and 2-oxoglutarate or, malonate that coordinate cobalt, the remaining coordinate sites are occupied by water molecules thus forming a six-coordinate cobalt complex
Co2+
-
competitive versus Fe2+
Co2+
-
competitive versus Fe2+
Co2+
-
competitive versus Fe2+
Co2+
-
competitive versus Fe2+
Co2+
-
competitive versus Fe2+
Co2+
-
competitive versus Fe2+
Co2+
-
complete inhibition
CoCl2
IC50: 0.00025 mM
CoCl2
-
0.4 mM, complete inhibition
Coumalic acid
-
-
Coumalic acid
-
i.e. 2-oxo-1,2H-pyran-5-carboxylic acid
Coumalic acid
-
competitive inhibitor, potential syncatalytic inhibitor, time-dependent inactivation, increasing concentrations of Fe2+ enhance the inactivation; i.e. 2-oxo-1,2H-pyran-5-carboxylic acid
Coumalic acid
-
i.e. 2-oxo-1,2H-pyran-5-carboxylic acid
Coumalic acid
-
competitive inhibitor, potential syncatalytic inhibitor, time-dependent inactivation, increasing concentrations of Fe2+ enhance the inactivation; i.e. 2-oxo-1,2H-pyran-5-carboxylic acid
Cu2+
-
-
Cu2+
-
causes a 20-30% fall in activity
daunorubicin
-
-
daunorubicin
-
irreversible inhibitor, 50% inhibition after 1 h at 0.06 mM, effect dependent on the presence of iron ions
daunorubicin
-
irreversible inhibitor, 50% inhibition after 1 h at 0.06 mM, effect dependent on the presence of iron ions
desferrioxamine
-
an Fe2+ chelator
desferrioxamine
-
an Fe2+ chelator
desferrioxamine
-
an Fe2+ chelator
desferrioxamine
-
an Fe2+ chelator
desferrioxamine
-
an Fe2+ chelator
desferrioxamine
-
an Fe2+ chelator
dilantin
-
inhibitor of the reaction due in part to the chelation of Fe2+
dilantin
-
inhibitor of the reaction due in part to the chelation of Fe2+
dithiothreitol
-
95-100% inhibition at 0.45 mM
dithiothreitol
-
powerful inhibitor at 1 mM
doxorubicin
-
-
doxorubicin
-
irreversible inhibitor, 50% inhibition after 1 h at 0.06 mM, effect dependent on the presence of iron ions
doxorubicin
-
irreversible inhibitor, 50% inhibition after 1 h at 0.06 mM, effect dependent on the presence of iron ions
doxorubicin
-
not inhibitory at concentration up to 0.5 mM
EDTA
-
98-100% inhibition at 0.01 mM
EDTA
-
0.4 mM, 74% inhibition
EDTA
-
50% inhibition at 0.15 mM
EDTA
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
EDTA
-
64% inhibition at 0.02 mM
ethylpyridine-2,4-dicarboxylate
-
-
ethylpyridine-2,4-dicarboxylate
-
-
Fe2+
-
inhibitory at high concentrations
Fe2+
-
inhibitory at a concentration higher than 0.5 mM
fumarate
-
competitive inhibition with respect to 2-oxoglutarate
gelatin
-
commercial, inhibitor
-
gelatin
-
commercial, inhibitor
-
gelatin
-
commercial, inhibitor
-
glutamyl-3,4-dehydroprolyl-bradykinin
-
-
-
glutamyl-3,4-dehydroprolyl-bradykinin
-
-
-
Glutarate
-
-
Glutarate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
hydralazine
-
inhibitor of the reaction due in part to the chelation of Fe2+
hydralazine
-
inhibitor of the reaction due in part to the chelation of Fe2+
Ketomalonate
-
100% inhibition at 1 mM, acts by chelating ferrous ion rather than by competing with alpha-ketoglutarate
Ketomalonate
-
100% inhibition at 1 mM, acts by chelating ferrous ion rather than by competing with alpha-ketoglutarate
Ketomalonate
-
100% inhibition at 1 mM, acts by chelating ferrous ion rather than by competing with alpha-ketoglutarate
malonate
Q81LZ8
active site binding structure analysis
malonate
-
19% inhibition at 1 mM
malonate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
malonate
-
19% inhibition at 1 mM
malonate
-
19% inhibition at 1 mM
N,N'-diethylpyridine 2,4-dicarboxamide
-
-
N,N'-diethylpyridine 2,4-dicarboxamide
-
-
N-(4-Azido-2-nitrophenyl)-glycyl-(Pro-Pro-Gly)5
-
loss of enzyme activity with (Pro-Pro-Gly)5 as a substrate upon photoaffinity labeling
N-(4-Azido-2-nitrophenyl)-glycyl-(Pro-Pro-Gly)5
-
-
NaCl
-
more than 0.3 M
Ni2+
-
competitive versus Fe2+
Ni2+
-
competitive versus Fe2+
Ni2+
-
competitive versus Fe2+
Ni2+
-
competitive versus Fe2+
Ni2+
-
competitive versus Fe2+
Ni2+
-
competitive versus Fe2+
nitroblue tetrazolium
-
is capable of scavenging superoxide, competitive inhibitor with respect to O2
nitroblue tetrazolium
-
competitive inhibition with respect to O2
nitroblue tetrazolium
-
is capable of scavenging superoxide, competitive inhibitor with respect to O2
oxalate
-
34% inhibition at 1 mM
oxalate
-
34% inhibition at 1 mM
oxalate
-
34% inhibition at 1 mM
oxalylglycine
-
inhibits purified enzyme, competitive inhibition with respect to 2-oxoglutarate, 50% inhibition of microsomal enzyme at 0.023 mM
phenanthrolines
-
potent competitive inhibitors inhibitory of purified enzyme; potent competitive inhibitors of collagen hydroxylation in embryonic tendon cells in vitro
-
phenanthrolines
-
potent competitive inhibitors of collagen hydroxylation in foreskin fibroblasts in vitro
-
poly(L-proline)
-
not inhibitory
-
poly(L-proline)
-
MW: 7000 and 44000
-
poly(L-proline)
-
competitive inhibitors with respect to the polypeptide substrate, the inhibition increases with chain length
-
poly(L-proline)
-
competitive inhibitor with respect to the polypeptide substrate and uncompetitive with respect to Fe2+ and 2-oxoglutarate
-
poly(L-proline)
-
competitive inhibitors with respect to the polypeptide substrate, the inhibition increases with chain length
-
poly(L-proline)
-
inhibitory, type I enzyme tetramer, MW: 7000 and 44000
-
poly(L-proline)
type I und II enzyme
-
poly(L-proline)
-
MW: 7000 and 44000
-
poly(L-proline)
-
inhibitor, recombinant type II enzyme tetramer, MW: 7000 and 44000
-
poly(L-proline)
-
competitive inhibition
-
propyl gallate
-
100% inhibition at 2 mM
propyl gallate
-
100% inhibition at 2 mM
propyl gallate
-
100% inhibition at 2 mM
Pyridine 2,4-dicarboxylate
-
not inhibitory
Pyridine 2,4-dicarboxylate
-
recombinant enzyme, competitive inhibitor with respect to Fe2+ and 2-oxoglutarate
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Pyridine 2,4-dicarboxylate
-
uncompetitive inhibition with respect to ascorbate
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
inhibits wild-type enzyme and enzyme tetramer containing the histidine 501 to serine mutant alpha subunit
Pyridine 2,4-dicarboxylate
-
inhibitory, type I enzyme tetramer
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
inhibitory, recombinant type II enzyme tetramer
Pyridine 2,4-dicarboxylate
-
effective inhibitor
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,5-dicarboxylate
-
-
Pyridine 2,5-dicarboxylate
-
-
Pyridine 2,5-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Pyridine 2,5-dicarboxylate
-
uncompetitive inhibition with respect to ascorbate
Pyridine 2,5-dicarboxylate
-
-
Pyridine 2,5-dicarboxylate
-
-
Pyridine 2,5-dicarboxylate
-
-
pyridine 2-carboxylate
-
-
pyridine 2-carboxylate
-
-
pyridine 2-carboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
pyridine 2-carboxylate
-
uncompetitive inhibition with respect to ascorbate
Pyridine-2,4-dicarboxylate
-
competitive inhibition
Pyridine-2,4-dicarboxylate
-
-
Pyridine-2,4-dicarboxylate
-
Pyridine-2,4-dicarboxylate
0.011 mM, 50% inhibition
Pyridine-2,5-dicarboxylate
-
competitive inhibition
Pyridine-2,5-dicarboxylate
-
-
Pyridine-2,5-dicarboxylate
0.007 mM, 50% inhibition
pyruvate
-
-
pyruvate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
pyruvate
-
competitive inhibition with respect to 2-oxoglutarate
succinate
-
11.5% inhibition at 0.5 mM and 38.3% inhibition at 3 mM
succinate
-
51% inhibition at 1 mM
succinate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
succinate
-
51% inhibition at 1 mM
succinate
-
product inhibition
succinate
-
51% inhibition at 1 mM
tetracyclin
-
inhibitor of the reaction due in part to the chelation of Fe2+
tetracyclin
-
inhibitor of the reaction due in part to the chelation of Fe2+
Zn2+
-
recombinant enzyme, competitive inhibition with respect to Fe2+ and 2-oxoglutarate
Zn2+
-
competitive versus Fe2+
Zn2+
-
comptitive versus Fe2+
Zn2+
-
Zn2+ is bound at each of the four active sites, binding structure, overview
Zn2+
-
competitive versus Fe2+
Zn2+
-
competitive inhibition with respect to Fe2+, non-competitive with respect to the polypeptide substrate and 2-oxoglutarate
Zn2+
-
competitive versus Fe2+
Zn2+
-
competitive versus Fe2+
Zn2+
-
competitive versus Fe2+
Zn2+
-
complete inhibition
additional information
-
high concentrations of salts are inhibitory
-
additional information
-
synthetic peptides containing the non-physiologic amino acid 5-oxaproline in the sequence R1-Xaa-oxaproline-Gly-OR2 are specific syncatalytic inactivators, noncompetitive inhibition with respect to peptide substrate and ascorbate, compounds with aromatic substituents R1 and R2 are particularly effective when compared with those with an aliphatic group, inactivation is only observed in the presence of Fe2+ and 2-oxoglutarate
-
additional information
-
the synthesis and degradation of ADP-ribose moieties may possibly regulate prolyl hydroxylase activity in vivo
-
additional information
-
inhibition of the purified enzyme and of collagen hydroxylation in embryonic tendon fibroblast by novel phenanthrolines, structure-activity relationships
-
additional information
-
synthetic peptides containing the non-physiologic amino acid 5-oxaproline in the sequence R1-Xaa-oxaproline-Gly-OR2 are specific syncatalytic inactivators, noncompetitive inhibition with respect to peptide substrate and ascorbate, compounds with aromatic substituents R1 and R2 are particularly effective when compared with those with an aliphatic group, inactivation is only observed in the presence of Fe2+ and 2-oxoglutarate
-
additional information
-
inhibition of the secretion of procollagen in foreskin fibroblasts by novel phenanthrolines, structure-activity relationships
-
additional information
-
high concentrations of salts are inhibitory
-
additional information
-
hypoxia inhibits the enzyme
-