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adenosine 5'-O-(3-thiotriphosphate) + adenosine 5-phosphosulfate
ADP + 3'-thiophosphoadenosine 5'-phosphosulfate
-
535fold lower Vmax than with ATP
-
?
adenosine 5'-phosphosulfate + ATP
3'-phosphoadenosine 5'-phosphosulfate + ADP
-
-
-
?
ADP + 3'-phosphoadenylyl sulfate
ATP + adenylyl sulfate
-
-
-
-
r
ATP + adenosine 5'-O-(2-fluorodiphosphate)
ADP + 3'-phosphoadenosine 5'-O-(2-fluorodiphosphate)
-
15fold lower Vmax than with adenosine 5-phosphosulfate
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
ATP + adenosine-5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
ATP + adenylyl sulfate
ADP + 3'-phosphoadenylyl sulfate
CTP + adenosine 5-phosphosulfate
CDP + 3'-phosphoadenosine 5'-phosphosulfate
dATP + adenosine 5-phosphosulfate
dADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
?
MgATP2- + adenosine 5'-phosphosulfate
MgADP- + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
?
MgATP2- + adenylyl sulfate
MgADP- + 3'-phosphoadenylyl sulfate
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
involved in the synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate, inactivating mutations of PAPSS2 causes skeletal disorders
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate, decreased activity leads to defects in skeleton
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate, enzyme defect causes brachymorphism, a severe growth disorder affecting skeletal elements as well as other physiological processes
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
-
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
Candida elegans
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
ATP can be replaced by GTP, ITP or UTP
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
GTP, ITP or UTP are poor substrates
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
no substrates are AMP, forward reaction, and 2'-phosphoadenosine 5'-phosphosulfate, reverse reaction
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
in the absence of adenosine 5'-phosphosulfate ATP phosphorylates the enzyme at a rate equivalent to the overall kinase reaction, phosphorylation site: Ser-109
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
P23846
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
ultimate step in biosynthesis of 3'-phosphoadenosine 5'-phosphosulfate, the primary biological sulfuryl donor
-
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
enzyme has both ATP sulfurylase and APS kinase activity
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
PAPSS 1 is essential for the sulfonation of mucin like glycoproteins such as GlyCAM-1, CD34 and MAdCAM-1 in high endothelial venules
-
-
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
enzyme is involved in sulfation of cartilaginous chondroitin sulfate, reduced enzyme activity causes brachymorphism
-
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
ATP can be replaced by GTP, ITP or UTP
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
optimal concentration of APS at 0.003 mM
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
no substrate-chanelling of adenosine 5'-phosphosulfate between ATP-sulfurylase, EC 2.7.7.4, and APS-kinase, i.e. ATP-sulfurylase-APS-complex is no substrate for the kinase
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
second step in pathway of assimilation of inorganic sulfate
-
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
Penicillium duponti
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
enzyme has both ATP sulfurylase and APS kinase activity
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
enzyme is involved in cysteine synthesis and sulfate assimilation, enzyme is required for activity of the avirulence rice resistant protein AvrXa21
-
?
ATP + adenosine-5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
?
ATP + adenosine-5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
-
?
ATP + adenosine-5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
?
ATP + adenosine-5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
-
?
ATP + adenylyl sulfate
ADP + 3'-phosphoadenylyl sulfate
-
-
-
-
?
ATP + adenylyl sulfate
ADP + 3'-phosphoadenylyl sulfate
-
-
-
?
ATP + adenylyl sulfate
ADP + 3'-phosphoadenylyl sulfate
-
-
-
r
ATP + adenylyl sulfate
ADP + 3'-phosphoadenylyl sulfate
-
-
-
-
r
ATP + adenylyl sulfate
ADP + 3'-phosphoadenylyl sulfate
-
-
-
r
CTP + adenosine 5-phosphosulfate
CDP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
?
CTP + adenosine 5-phosphosulfate
CDP + 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
?
MgATP2- + adenylyl sulfate
MgADP- + 3'-phosphoadenylyl sulfate
-
-
-
r
MgATP2- + adenylyl sulfate
MgADP- + 3'-phosphoadenylyl sulfate
-
-
-
-
r
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1-phenyl-N-[4-(pyridin-2-yl)-1,3-thiazol-2-yl]-1H-imidazole-5-carboxamide
-
2'-Phosphoadenosine 5'-phosphosulfate
-
-
2,4,6-Trinitrobenzene sulfonate
2,6-dichlorophenol indophenol
2-(3-fluorophenoxy)-N-[4-(2-pyridyl)thiazol-2-yl]acetamide
shows good docking results. The inhibitor halts not only Entamoeba trophozoite proliferation but also cyst formation
2-(3-fluorophenoxy)-N-[4-(pyridin-2-yl)-1,3-thiazol-2-yl]acetamide
-
2-cycloheptyl-4-(4-methoxy-3-[4-[4-(2H-tetrazol-5-yl)phenoxy]butoxy]phenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
2-cycloheptyl-5-(4-methoxy-3-[4-[4-(2H-tetrazol-5-yl)phenoxy]butoxy]phenyl)-4,4-dimethyl-2,4-dihydro-3H-pyrazol-3-one
-
3'-phosphoadenosine 5'-phosphosulfate
-
product inhibition
3-(methanesulfonyl)-5,7-dimethyl[1,2]thiazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
3-phenyl-N-[4-(2-pyridyl)thiazol-2-yl]imidazole-4-carboxamide
shows good docking results. The inhibitor halts not only Entamoeba trophozoite proliferation but also cyst formation
3-[5-(3,5-dichloro-4-fluorophenyl)-5-(trifluoromethyl)-4,5-dihydro-1,2-oxazol-3-yl]-N-[(1-hydroxy-3,3-dimethyl-1,3-dihydro-2,1-benzoxaborol-5-yl)methyl]-5-methylbenzamide
-
3-[7-(benzyloxy)-4,8-dimethyl-2-oxo-2H-1-benzopyran-3-yl]propanoic acid
-
4-(3-methoxyphenyl)-5-(phenylmethanesulfonyl)-1H-tetrazol-4-ium
-
4-Aminophenylacetate
-
0.008 mM, 50% inhibition
5-bromo-2-chloro-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)benzamide
-
8-(4-methyl-3-[3-[([2-methyl-5-[(4,6,8-trisulfonaphthalen-1-yl)carbamoyl]phenyl]carbamoyl)amino]benzamido]benzamido)naphthalene-1,3,5-trisulfonic acid
-
adenosine 5'-phosphosulfate
adenosine-5'-phosphosulfate
adenylyl sulfate
adenylyl sulfate acts as a strong uncompetitive inhibitor of the APS kinase reaction
ADP
-
free form, reverse reaction, weak
ammonium sulfate
high salt inhibits at low adenosine 5'-phosphosulfate concentrations, but activates at high adenosine 5'-phosphosulfate concentrations
auranofin
shows good docking results. The inhibitor halts not only Entamoeba trophozoite proliferation but also cyst formation
Cu2+
-
2 mM, 90% inhibition
diethyldicarbonate
-
in the presence or absence of ATP-sulfurylase
ferricyanide
-
0.05 mM, complete inhibition
iodoacetamide
-
strong inhibition, dithiothreitol partially protects
Mn2+
-
in excess, activating below
N,N'-[furan-2,5-diylbis(2-chloro-4,1-phenylene)]diguanidine
-
N,N'-[furan-2,5-diylbis(3-chloro-4,1-phenylene)]diguanidine
-
N-ethylmaleimide
-
0.02 mM, 50% inhibition
N-[2-(5-chloro-2-methoxyanilino)-2-oxoethyl]-N-methyl-2-phenyl-2H-1,2,3-triazole-4-carboxamide
-
NaClO3
-
6.57 mM, 50% inhibition of brain PAPSS activity, 3.26 mM, 50% inhibition of liver PAPSS
p-chloromercuribenzoate
-
0.005 mM, 50% inhibition
2,4,6-Trinitrobenzene sulfonate
-
0.05 mM, complete inhibition
2,4,6-Trinitrobenzene sulfonate
-
in the presence or absence of ATP-sulfurylase
2,4,6-Trinitrobenzene sulfonate
-
0.05 mM, 28% inhibition
2,6-dichlorophenol indophenol
-
0.05 mM, complete inhibition
2,6-dichlorophenol indophenol
-
0.05 mM, complete inhibition
adenosine 5'-phosphosulfate
substrate inhibition above 0.01 mM
adenosine 5'-phosphosulfate
uncompetitive inhibition above 0.001 mM
adenosine 5'-phosphosulfate
-
adenosine 5'-phosphosulfate
-
-
adenosine 5'-phosphosulfate
-
adenosine 5'-phosphosulfate
-
substrate inhibition above 0.03-0.04 mM
adenosine 5'-phosphosulfate
-
-
adenosine 5'-phosphosulfate
substrate inhibition
adenosine 5'-phosphosulfate
acts as a strong uncompetitive inhibitor of the APS kinase reaction
adenosine 5'-phosphosulfate
-
-
adenosine 5'-phosphosulfate
-
kinetics
adenosine 5'-phosphosulfate
-
-
adenosine 5'-phosphosulfate
adenosine 5'-phosphosulfate can bind to E-MgADP forming a catalytically inactive E-MgADP-APS ternary complex
adenosine 5'-phosphosulfate
-
potent substrate inhibition, ATP reverses
adenosine 5'-phosphosulfate
-
-
adenosine-5'-phosphosulfate
-
-
adenosine-5'-phosphosulfate
substrate inhibition
adenosine-5'-phosphosulfate
-
substrate inhibition
ATP
-
in the absence of ATP regenerating system, substrate inhibition above 0.6 mM, in the presence of ATP regenerating system, substrate inhibition above 0.2 mM
ATP
-
free form, weak inhibition; MgATP2-: product inhibition, reverse reaction
ATP
-
inhibition by free ATP, i.e. in excess of total Mg2+
Bromosuccinimide
-
strong inhibition
Bromosuccinimide
-
0.05 mM, complete inhibition
Bromosuccinimide
-
0.05 mM, complete inhibition
Co2+
-
2 mM, 63% inhibition
Co2+
-
in excess, activating below
dehydroascorbate
-
-
EDTA
complete inhibition
FAD
-
-
GSSG
-
-
Mercuriphenylacetate
-
0.05 mM, complete inhibition
Mercuriphenylacetate
-
0.05 mM, complete inhibition
oxidized glutathione
-
thioredoxin reverses inactivation
additional information
validation of in silico molecular docking analysis and an in vitro enzyme activity assay for large scale screening. Inhibitor screening, In silico molecular docking analysis and simulation ranks the binding free energy between a homology modeling structure of EhAPSK and 400 compounds, overview. Analysis of the cytotoxicity
-
additional information
-
validation of in silico molecular docking analysis and an in vitro enzyme activity assay for large scale screening. Inhibitor screening, In silico molecular docking analysis and simulation ranks the binding free energy between a homology modeling structure of EhAPSK and 400 compounds, overview. Analysis of the cytotoxicity
-
additional information
-
not inhibited by Mg2+
-
additional information
-
-
-
additional information
-
not inhibited by adenosine 5'-phosphosulfate
-
additional information
-
not inhibited by ferricyanide
-
additional information
-
-
-
additional information
-
not inhibited by ATP
-
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0.003 - 0.37
3'-phosphoadenosine 5'-phosphosulfate
0.06
adenosine 5'-O-(3-thiotriphosphate)
-
pH 8.0
0.00014 - 0.042
adenosine 5'-phosphosulfate
0.00044 - 0.00072
adenosine-5'-phosphosulfate
0.002 - 0.0046
adenylyl sulfate
additional information
additional information
-
0.003
3'-phosphoadenosine 5'-phosphosulfate
pH 8.1, 30°C, wild-type enzyme
0.008
3'-phosphoadenosine 5'-phosphosulfate
-
pH 8.0, 30°C
0.039
3'-phosphoadenosine 5'-phosphosulfate
pH 8.1, 30°C, S107A mutant enzyme
0.37
3'-phosphoadenosine 5'-phosphosulfate
-
-
0.37
3'-phosphoadenosine 5'-phosphosulfate
-
pH 8.0, 25°C
0.00014
adenosine 5'-phosphosulfate
pH 7.4, 25°C
0.00025
adenosine 5'-phosphosulfate
-
pH 8.0, 25°C
0.0004
adenosine 5'-phosphosulfate
pH 8.0, 37°C, COS-1 cell-expressed full length PAPS synthase
0.00043
adenosine 5'-phosphosulfate
-
oxidized wild type enzyme, at pH 7.5 and 17°C
0.00043
adenosine 5'-phosphosulfate
oxidized wild type enzyme, at pH 7.5 and 25°C
0.00045
adenosine 5'-phosphosulfate
-
-
0.00048
adenosine 5'-phosphosulfate
-
reduced wild type enzyme, at pH 7.5 and 17°C
0.00048
adenosine 5'-phosphosulfate
reduced wild type enzyme, at pH 7.5 and 25°C
0.00048
adenosine 5'-phosphosulfate
wild type enzyme, at pH 7.5 and 17°C
0.0005
adenosine 5'-phosphosulfate
-
pH 8.0
0.0006
adenosine 5'-phosphosulfate
pH 8.0, 37°C, COS-1 cell-expressed N-terminal fragment
0.0007
adenosine 5'-phosphosulfate
mutant enzyme D136N, at pH 7.5 and 17°C
0.0008
adenosine 5'-phosphosulfate
-
pH 8.1, 30°C
0.00087
adenosine 5'-phosphosulfate
oxidized mutant enzyme C86A/C119A, at pH 7.5 and 25°C
0.00092
adenosine 5'-phosphosulfate
mutant enzyme D136A, at pH 7.5 and 17°C
0.001
adenosine 5'-phosphosulfate
pH 8.1, 30°C, wild-type enzyme at 100 mM ammonium sulfate
0.0014
adenosine 5'-phosphosulfate
-
-
0.0014
adenosine 5'-phosphosulfate
-
pH 8.0, 30°C
0.00172
adenosine 5'-phosphosulfate
-
mutant enzyme R93A, at pH 7.5 and 17°C
0.0019
adenosine 5'-phosphosulfate
reduced mutant enzyme C86A/C119A, at pH 7.5 and 25°C
0.002
adenosine 5'-phosphosulfate
-
pH 6.8, 30°C
0.0023
adenosine 5'-phosphosulfate
pH 8.0, 37°C, Escherichia coli-expressed N-terminal fragment
0.0026
adenosine 5'-phosphosulfate
pH 8.0, 37°C, Escherichia coli-expressed full length PAPS synthase
0.00263
adenosine 5'-phosphosulfate
-
N-terminal truncation variant APSKDELTA96, at pH 7.5 and 17°C
0.0036
adenosine 5'-phosphosulfate
25°C
0.0042
adenosine 5'-phosphosulfate
pH 8.0, 30°C
0.006
adenosine 5'-phosphosulfate
-
pH 8.0
0.012
adenosine 5'-phosphosulfate
pH 8.1, 30°C, S107A mutant enzyme at 100 mM ammonium sulfate
0.042
adenosine 5'-phosphosulfate
-
pH 8.0, 30°C
0.00044
adenosine-5'-phosphosulfate
-
mutant enzyme C36A/C69A, at pH 8.0 and 25°C
0.00072
adenosine-5'-phosphosulfate
-
wild type enzyme, at pH 8.0 and 25°C
0.002
adenylyl sulfate
value is below 0.002 for a deletion mutant lacking the first 34 amino acids of the N-terminus, delta34N
0.002
adenylyl sulfate
value is below 0.002 for wildtype adenylyl sulfate
0.0032
adenylyl sulfate
mutant R37A
0.0037
adenylyl sulfate
mutant R40A
0.0046
adenylyl sulfate
deletion mutant lacking the first 50 amino acids of the N-terminus, delta50N
0.13
ADP
-
pH 8.0, 25°C
0.13
ADP
-
ADP in form of MgADP-
0.007
ATP
-
pH 6.8, 30°C
0.08
ATP
-
pH 8.0, 37°C, PAPSS 1
0.14
ATP
-
mutant enzyme C36A/C69A, at pH 8.0 and 25°C
0.14
ATP
ATP in form of MgATP2-
0.23
ATP
pH 8.0, 37°C, COS-1 cell-expressed N-terminal fragment
0.26
ATP
pH 8.0, 37°C, E. coli expressed N-terminal fragment
0.36
ATP
-
pH 8.0, 37°C, PAPSS 2b
0.38
ATP
-
pH 8.0, 37°C, PAPSS 2a
0.45
ATP
pH 8.0, 37°C, E. coli-expressed full length PAPS synthase
0.46
ATP
-
at pH 8.0 and 25°C
0.75
ATP
-
wild type enzyme, at pH 8.0 and 25°C
0.8
ATP
pH 8.1, 30°C, wild-type enzyme at 100 mM ammonium sulfate
0.8
ATP
-
ATP in form of MgATP2-
0.8
ATP
ATP in form of MgATP2-
2.4
ATP
pH 8.1, 30°C, S107A mutant enzyme
2.4
ATP
ATP in form of MgATP2-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
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C86A/C119A
the mutant is kinetically similar to the reduced wild type enzyme
D136A
the mutant displays drastically reduced affinity for adenosine 5'-phosphosulfate compared to the wild type enzyme
D136N
the mutant displays drastically reduced affinity for adenosine 5'-phosphosulfate compared to the wild type enzyme
R93A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme. The mutation modestly reduces kcat by 2fold and increases the Km for adenosine 5-phosphosulfate by 3fold
S182C
similar catalytic activity as wild-type
S182F
similar catalytic activity as wild-type
delta34N
deletion mutant lacking the first 34 N-terminal residues from APS kinase domain results in an enzyme with similar kinetic behaviour to the full-length domain
delta50N
deletion mutant lacking the first 50 N-terminal residues from APS kinase domain show no substrate inhibition by adenylyl sulfate and approximately half of the full-length's turnover number, crystal structure reveals an asymmetrical dimer
E531Q
identified as naturally occurring mutation, E531Q found in a single sample of an African-Americans subject, almost no effect of mutations when expressed in COS-1 or HEK293 cells
G427A/H428A
no APS kinase activity
R333C
identified as naturally occurring mutation, R333C found exclusively in Caucasian-Americans DNA, almost no effect of mutations when expressed in COS-1 or HEK293 cells
R37A
mutant clone shows no substrate inhibition by adenylyl sulfate, mutant is kinetically indistinguishable from deletion mutant delta50N lacking the first N-terminal residues
R40A
mutant clone shows no substrate inhibition by adenylyl sulfate, mutant is kinetically indistinguishable from deletion mutant delta50N lacking the first N-terminal residues
D87A
-
almost complete loss of activity
D87E
-
80% loss of activity
D87R
-
almost complete loss of activity
D89A
-
almost complete loss of activity
D89E
-
75% loss of activity
D89R
-
almost complete loss of activity
DN89ND
-
switch mutant, almost complete loss of activity
G79R
-
reduced APS kinase activity
G88A
-
less than 30% loss of kinase activity
G88D
-
almost complete loss of activity
G88R
-
almost complete loss of activity
K97A
-
no effect on activity
LD86DL
-
switch mutant, almost complete loss of activity
N90A
-
30% loss of kinase activity
N90Q
-
30% loss of kinase activity
R92A
-
complete loss of kinase activity
C541A
the mutant shows reduced activity compared to the wild type enzyme
C549A
the mutant shows increased activity compared to the wild type enzyme
C36A/C69A
-
the mutant is not inhibited by oxidized glutathione and shows activity reduced to 71%
S104A
similar properties as wild-type
S107A
similar properties as wild-type enzyme
S107C
similar properties as wild-type, suggesting that S107 is not essential for activity but may be located in the substrate binding pocket
S97A
similar properties as wild-type
S99A
similar properties as wild-type
T103A
similar properties as wild-type
Y109F
similar properties as wild-type, velocity curve is shifted to the far right
H23C
the mutation does not significantly alter the steady-state kinetic parameters of the enzyme
T61E
the mutation does not significantly alter the steady-state kinetic parameters of the enzyme
G427A
-
G427A
slightly lower APS kinase activity than wild-type
H425A
-
H425A
no APS kinase activity
H428A
-
H428A
no APS kinase activity
N426K
-
N426K
2fold higher APS kinase activity than wild-type
K19R
site-directed mutagenesis, the P-loop Lys is substituted by Arg. K19R is a kinase-dead point mutation, because the Lys residue in the P-loop is required for productive ATP binding and kinase activity
K19R
-
site-directed mutagenesis, the P-loop Lys is substituted by Arg. K19R is a kinase-dead point mutation, because the Lys residue in the P-loop is required for productive ATP binding and kinase activity
-
additional information
-
the N-terminal truncation variant (APSKDELTA96) is completely insensitive to substrate inhibition by adenosine 5-phosphosulfate
additional information
the results show that the alpha1 Helix constructed by N-terminal residue 35-50 of the APS kinase domain are critical in stabilizing a symmetrical dimer, interactions established by the highly conserved arginines 37 and 40 are indispensable for maintaining substrate inhibition of the APS kinase domain in human PAPSS1
additional information
the results show that the alpha1 Helix constructed by N-terminal residue 35-50 of the APS kinase domain are critical in stabilizing a symmetrical dimer, interactions established by the highly conserved arginines 37 and 40 are indispensable for maintaining substrate inhibition of the APS kinase domain in human PAPSS1
additional information
-
the results show that the alpha1 Helix constructed by N-terminal residue 35-50 of the APS kinase domain are critical in stabilizing a symmetrical dimer, interactions established by the highly conserved arginines 37 and 40 are indispensable for maintaining substrate inhibition of the APS kinase domain in human PAPSS1
additional information
generation of truncated and point mutants of the APS kinase domain that are active but devoid of substrate inhibition. Structural analysis of these mutant enzymes reveals the intrasubunit rearrangements that occur upon substrate binding
additional information
generation of truncated and point mutants of the APS kinase domain that are active but devoid of substrate inhibition. Structural analysis of these mutant enzymes reveals the intrasubunit rearrangements that occur upon substrate binding
additional information
-
generation of truncated and point mutants of the APS kinase domain that are active but devoid of substrate inhibition. Structural analysis of these mutant enzymes reveals the intrasubunit rearrangements that occur upon substrate binding
additional information
construction of MXAN3487-lacZ fusion protein. Genome-wide transposon mutagenesis is used to identify MXAN3487 (MXAN_RS16905) as a gene encoding a putative adenosine 5'-phosphosulfate (APS) kinase (i.e. adenylylsulfate kinase), as a regulator for the timing of cell aggregation. In-frame deletion resulting in plasmid pBJ113-DELTAMXAN3487, a pBJ113 derivative. Expression of the Escherichia coli cysC gene in mutant strain DELTAMXAN3487 partially complements the phenotype
additional information
-
construction of MXAN3487-lacZ fusion protein. Genome-wide transposon mutagenesis is used to identify MXAN3487 (MXAN_RS16905) as a gene encoding a putative adenosine 5'-phosphosulfate (APS) kinase (i.e. adenylylsulfate kinase), as a regulator for the timing of cell aggregation. In-frame deletion resulting in plasmid pBJ113-DELTAMXAN3487, a pBJ113 derivative. Expression of the Escherichia coli cysC gene in mutant strain DELTAMXAN3487 partially complements the phenotype
additional information
-
construction of MXAN3487-lacZ fusion protein. Genome-wide transposon mutagenesis is used to identify MXAN3487 (MXAN_RS16905) as a gene encoding a putative adenosine 5'-phosphosulfate (APS) kinase (i.e. adenylylsulfate kinase), as a regulator for the timing of cell aggregation. In-frame deletion resulting in plasmid pBJ113-DELTAMXAN3487, a pBJ113 derivative. Expression of the Escherichia coli cysC gene in mutant strain DELTAMXAN3487 partially complements the phenotype
-
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Yu, M.; Martin, R.L.; Jain, S.; Chen, L.J.; Segel, I.H.
Rat liver ATP-sulfurylase: purification, kinetic characterization, and interaction with arsenate, selenate, phosphate, and other inorganic oxyanions
Arch. Biochem. Biophys.
269
156-174
1989
Rattus norvegicus
brenda
Hommes, F.A.; Moss, L.; Touchton, J.
Purification and some properties of liver adenylylsulfate kinase
Biochim. Biophys. Acta
924
270-275
1987
Rattus norvegicus
brenda
Renosto, F.; Martin, R.L.; Borrell, J.L.; Nelson, D.C.; Segel, I.H.
ATP sulfurylase from trophosome tissue of Riftia pachyptila (hydrothermal vent tube worm)
Arch. Biochem. Biophys.
290
66-78
1991
Riftia pachyptila
brenda
Renosto, F.; Seubert, P.A.; Segel, I.H.
Adenosine 5-phosphosulfate kinase from Penicillium chrysogenum. Purification and kinetic characterization
J. Biol. Chem.
259
2113-2123
1984
Penicillium chrysogenum
brenda
Renosto, F.; Schultz, T.; Re, E.; Mazer, J.; Chandler, C.J.; Barron, A.; Segel, I.H.
Comparative stability and catalytic and chemical properties of the sulfate-activating enzymes from Penicillium chrysogenum (mesophile) and Penicillium duponti (thermophile)
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164
674-683
1985
Penicillium chrysogenum, Penicillium duponti
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APS kinase from Penicillium chrysogenum. Dissociation and reassociation of subunits as the basis of the reversible heat inactivation
J. Biol. Chem.
260
1535-1544
1985
Penicillium chrysogenum
brenda
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Sulfate-activating enzymes of Penicillium chrysogenum. The ATP sulfurylase.adenosine 5-phosphosulfate complex does not serve as a substrate for adenosine 5-phosphosulfate kinase
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264
9433-9437
1989
Penicillium chrysogenum
brenda
Kanno, N.; Sato, M.; Sato, Y.
Purification and properties of adenosine-5'-phosphosulfate kinase from the marine red macroalga Porphyra yezoensis Ueda
Bot. Mar.
33
369-374
1990
Neopyropia yezoensis
-
brenda
Schwenn, J.D.; Jender, H.G.
A kinetic investigation of the APS-kinase from chlamydomonas reinhardii CW 15
Phytochemistry
20
601-604
1981
Chlamydomonas reinhardtii
-
brenda
Schwenn, J.D.; Jender, H.G.
Purification and properties of the ATP:adenylylsulfate 3'-phosphotransferase from chlamydomonas reinhardii
Arch. Microbiol.
138
9-14
1984
Chlamydomonas reinhardtii
-
brenda
Schwenn, J.D.; Schriek, U.
A new role for thioredoxin in assimilatory silphate reduction. Activation of the adenylylsulphate kinase from the green alga chlamydomonas reinhardii CW 15
FEBS Lett.
170
76-80
1984
Chlamydomonas reinhardtii
-
brenda
Satishchandran, C.; Markham, G.D.
Adenosine-5-phosphosulfate kinase from Escherichia coli K12. Purification, characterization, and identification of a phosphorylated enzyme intermediate
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264
15012-15021
1989
Escherichia coli
brenda
Satishchandran, C.; Hickman, Y.N.; Markham, G.D.
Characterization of the phosphorylated enzyme intermediate formed in the adenosine 5-phosphosulfate kinase reaction
Biochemistry
31
11684-11688
1992
Escherichia coli
brenda
Schriek, U.; Schwenn, J.D.
Properties of the purified APS-kinase from Escherichia coli and Saccharomyces cerevisiae
Arch. Microbiol.
145
32-38
1986
Saccharomyces cerevisiae, Escherichia coli, Escherichia coli AN1460
brenda
Bandurski, R.S.; Wilson, L.G.; Squires, C.L.
The mechanism of active sulfate formation
J. Am. Chem. Soc.
78
6408-6409
1956
Saccharomyces cerevisiae
-
brenda
Robbins, P.W.; Lipmann, F.
The enzymatic sequence in the biosynthesis of active sulfate
J. Am. Chem. Soc.
78
6409-6410
1956
Saccharomyces cerevisiae
-
brenda
Rosenthal, E.; Leustak, T.
A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities
Gene
165
243-248
1995
Rattus norvegicus, Urechis caupo (Q27128), Urechis caupo
brenda
Onda, M.; Hayashi, M.; Suiko, M.; Liu, M.C.; Nakajima, H.
Purification and characterization of adenosine 5'-phosphosulfate kinase from the thermophilic bacterium Bacillus stearothermophilus
Biosci. Biotechnol. Biochem.
60
134-136
1996
Geobacillus stearothermophilus, Saccharomyces cerevisiae
-
brenda
Lee, S.; Leustek, T.
APS kinase from Arabidopsis thaliana: genomic organization, expression, and kinetic analysis of the recombinant enzyme
Biochem. Biophys. Res. Commun.
247
171-175
1998
Arabidopsis thaliana (Q43295), Arabidopsis thaliana
brenda
MacRae, I.J.; Rose, A.B.; Segel, I.H.
Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. site-directed mutagenesis at putative phosphoryl-accepting and ATP P-loop residues
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273
28583-28589
1998
Escherichia coli (P23846), Escherichia coli, Penicillium chrysogenum (Q12657), Penicillium chrysogenum
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Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains
J. Biol. Chem.
273
19311-19320
1998
Homo sapiens (O43252), Homo sapiens
brenda
Deyrup, A.T.; Krishnan, S.; Singh, B.; Schwartz, N.B.
Activity and stability of recombinant bifunctional rearranged and monofunctional domains of ATP-sulfurylase and adenosine 5'-phosphosulfate kinase
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274
10751-10757
1999
Mus musculus
brenda
MacRae, I.J.; Segel, I.H.
Adenosine 5'-phosphosulfate (APS) kinase: diagnosing the mechanism of substrate inhibition
Arch. Biochem. Biophys.
361
277-282
1999
Penicillium chrysogenum
brenda
Venkatachalam, K.V.; Fuda, H.; Koonin, E.V.; Strott, C.A.
Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase
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274
2601-2604
1999
Homo sapiens (O43252), Homo sapiens
brenda
Satishchandran, C.; Markham, G.D.
Mechanistic studies of Escherichia coli adenosine-5'-phosphosulfate kinase
Arch. Biochem. Biophys.
378
210-215
2000
Escherichia coli
brenda
Xu, Z.H.; Otterness, D.M.; Freimuth, R.R.; Carlini, E.J.; Wood, T.C.; Mitchell, S.; Moon, E.; Kim, U.J.; Xu, J.P.; Siciliano, M.J.; Weinshilboum, R.M.
Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization
Biochem. Biophys. Res. Commun.
268
437-444
2000
Homo sapiens
brenda
Lillig, C.H.; Schiffmann, S.; Berndt, C.; Berken, A.; Tischka, R.; Schwenn, J.D.
Molecular and catalytic properties of Arabidopsis thaliana adenylyl sulfate (APS)-kinase
Arch. Biochem. Biophys.
392
303-310
2001
Arabidopsis thaliana (O49196), Arabidopsis thaliana
brenda
Fuda, H.; Shimizu, C.; Lee, Y.C.; Akita, H.; Strott, C.A.
Characterization and expression of human bifunctional 3'-phosphoadenosine 5'-phosphosulphate synthase isoforms
Biochem. J.
365
497-504
2002
Cavia porcellus (O54820), Homo sapiens
brenda
Shen, Y.; Sharma, P.; da Silva, F.G.; Ronald, P.
The Xanthomonas oryzae pv. oryzae raxP and raxQ genes encode an ATP sulphurylase and adenosine-5'-phosphosulphate kinase that are required for AvrXa21 avirulence activity
Mol. Microbiol.
44
37-48
2002
Sinorhizobium meliloti, Xanthomonas oryzae
brenda
Lansdon, E.B.; Segel, I.H.; Fisher, A.J.
Ligand-induced structural changes in adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum
Biochemistry
41
13672-13680
2002
Penicillium chrysogenum (Q12657), Penicillium chrysogenum
brenda
Venkatachalam, K.V.
Human 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase: biochemistry, molecular biology and genetic deficiency
IUBMB Life
55
1-11
2003
Caenorhabditis elegans, Homo sapiens, Homo sapiens (O43252), Homo sapiens (O95340), Mus musculus, Cavia porcellus (O54820), Urechis caupo (Q27128), Danio rerio (Q802U9), Takifugu rubripes (Q90XY2), Drosophila melanogaster (Q9VW48)
brenda
Harjes, S.; Scheidig, A.; Bayer, P.
Expression, purification and crystallization of human 3'-phosphoadenosine-5'-phosphosulfate synthetase 1
Acta Crystallogr. Sect. D
60
350-352
2004
Homo sapiens
brenda
Xu, Z.H.; Thomae, B.A.; Eckloff, B.W.; Wieben, E.D.; Weinshilboum, R.M.
Pharmacogenetics of human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1): gene resequencing, sequence variation, and functional genomics
Biochem. Pharmacol.
65
1787-1796
2003
Homo sapiens (O43252), Homo sapiens
brenda
Lansdon, E.B.; Fisher, A.J.; Segel, I.H.
Human 3'-phosphoadenosine 5'-phosphosulfate synthetase (isoform 1, brain): kinetic properties of the adenosine triphosphate sulfurylase and adenosine 5'-phosphosulfate kinase domains
Biochemistry
43
4356-4365
2004
Homo sapiens (O43252), Homo sapiens
brenda
Singh, B.; Schwartz, N.B.
Identification and functional characterization of the novel BM-motif in the murine phosphoadenosine phosphosulfate (PAPS) synthetase
J. Biol. Chem.
278
71-75
2003
Mus musculus
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Arabidopsis thaliana (Q43295), Arabidopsis thaliana
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Wang, D.; Xu, S.; Song, D.; Knight, S.; Mao, X.
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Myxococcus xanthus (Q1D6P1), Myxococcus xanthus, Myxococcus xanthus DK 1622 (Q1D6P1)
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Mi-Ichi, F.; Ishikawa, T.; Tam, V.K.; Deloer, S.; Hamano, S.; Hamada, T.; Yoshida, H.
Characterization of Entamoeba histolytica adenosine 5-phosphosulfate (APS) kinase, validation as a target and provision of leads for the development of new drugs against amoebiasis
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Entamoeba histolytica (C4LUW9), Entamoeba histolytica
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