Information on EC 2.7.1.25 - adenylyl-sulfate kinase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
2.7.1.25
-
RECOMMENDED NAME
GeneOntology No.
adenylyl-sulfate kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
show the reaction diagram
mechanism
-
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
show the reaction diagram
mechanism
-
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
show the reaction diagram
kinetic scheme for APS kinase
-
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
show the reaction diagram
enzyme follows a compulsory ordered mechanism in which MgATP2- binds before APS, and PAPS leaves before MgADP-
-
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Purine metabolism
-
sulfate activation for sulfonation
-
Sulfur metabolism
-
SYSTEMATIC NAME
IUBMB Comments
ATP:adenylyl-sulfate 3'-phosphotransferase
The human phosphoadenosine-phosphosulfate synthase (PAPSS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3'-phosphoadenosine 5'-phosphosulfate synthetase1
-
-
3'-phosphoadenosine-5'-phosphosulfate synthetase
-
-
-
-
5'-phosphoadenosine sulfate kinase
-
-
-
-
adenosine 5'-phosphosulfate kinase
-
-
-
-
adenosine 5'-phosphosulfate kinase
-
-
adenosine 5-phosphosulfate kinase
O43252
adenosine 5-phosphosulfate kinase is a domain of human 3-phosphoadenosine 5-phosphosulfate synthetase 1
adenosine 5-phosphosulfate kinase
Q43295
-
adenosine phosphosulfate kinase
-
-
-
-
adenosine phosphosulfokinase
-
-
-
-
adenosine-5'-phosphosulfate 3'-phosphotransferase
-
-
-
-
adenosine-5'-phosphosulfate kinase
-
-
adenosine-5'-phosphosulfate kinase
Q43295
-
adenosine-5'-phosphosulfate-3'-phosphokinase
-
-
-
-
adenosine-5'phosphosulfate kinase
-
-
-
-
adenosine-5-phosphosulfate kinase
-
-
adenosine-5-phosphosulfate kinase
-
-
adenylyl-sulfate kinase
Q43295
-
adenylylsulfate 3'-phosphotransferase
-
-
-
-
adenylylsulfate kinase
-
-
-
-
APK1
-
isoform
APK2
-
isoform
APK3
-
isoform
APK4
-
isoform
APS kinase
-
-
-
-
APS kinase
Q43295
-
APS-kinase
B0FWC4
part of a triple fusion protein of APS-kinase, ATP-sulfurylase, and pyrophosphatase
ATP adenosine-5'-phosphosulfate 3'-phosphotransferase
-
-
-
-
ATP sulfurylase-APS kinase
O67174
bifunctional enzyme
kinase, adenylylsulfate (phosphorylating)
-
-
-
-
PAPS 2
-
-
PAPS synthase
-
-
-
PAPS synthetase
-
-
-
PAPS synthetase
-
two isoforms, type 1 and 2
PAPSS
O43252
PAPS synthetase, two isoforms: PAPSS1 and PAPSS2
PAPSS 1
O43252
-
MgATP:APS 3'-phosphotransferase
-
-
additional information
-
bifunctional enzyme with ATP sulfurylase activity and adenosine phosphosulfate kinase activity, catalyzes the formation of 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate
additional information
O43252
bifunctional enzyme with ATP sulfurylase activity and adenosine phosphosulfate kinase activity, catalyzes the formation of 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate
additional information
-
bifunctional enzyme with ATP sulfurylase activity and adenosine phosphosulfate kinase activity, catalyzes the formation of 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate
CAS REGISTRY NUMBER
COMMENTARY
9012-38-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
APS kinase gene Atakn1; APS kinase gene Atakn2
SwissProt
Manually annotated by BRENDA team
ecotype Columbia
-
-
Manually annotated by BRENDA team
guinea pig
SwissProt
Manually annotated by BRENDA team
guinea pig, isoenzyme PAPSS 1
SwissProt
Manually annotated by BRENDA team
CW15, cell wall mutant
-
-
Manually annotated by BRENDA team
zebra fish
GenBank
Manually annotated by BRENDA team
-
P23846
GenBank
Manually annotated by BRENDA team
overproducing K12 strain, JM83/pTL3/pGP1-2
-
-
Manually annotated by BRENDA team
strain AN1460
-
-
Manually annotated by BRENDA team
Escherichia coli AN1460
strain AN1460
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase
SwissProt
Manually annotated by BRENDA team
isoenzyme PAPSS 2; isoenzyme PAPSS 2b, splice variant of PAPSS2, several SNPs and polymorphisms are identified with reference to PAPSS 1 and 2
SwissProt
Manually annotated by BRENDA team
isoform 1
SwissProt
Manually annotated by BRENDA team
isoforms PAPSS 1 and PAPSS 2
-
-
Manually annotated by BRENDA team
isoforms PAPSS 1, PAPSS 2a and 2b
-
-
Manually annotated by BRENDA team
PAPSS 1
SwissProt
Manually annotated by BRENDA team
PAPSS1; Caucasian-American and African-American subjects
SwissProt
Manually annotated by BRENDA team
bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase
-
-
Manually annotated by BRENDA team
isoenzymes PAPS 1 and 2
-
-
Manually annotated by BRENDA team
Penicillium duponti
-
-
-
Manually annotated by BRENDA team
Ueda, marine alga
-
-
Manually annotated by BRENDA team
hydrothermal vent tube worm
-
-
Manually annotated by BRENDA team
puffer fish
UniProt
Manually annotated by BRENDA team
marine worm, bifunctional PAPS senthetase
SwissProt
Manually annotated by BRENDA team
pv. oryzae, Philippine race 6, raxQ gene
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
the apk1 apk3 apk4 triple mutant combination is pollen lethal
metabolism
B0FWC4
sulfate activation pathway
physiological function
-
the enzyme is essential for plant reproduction and viability
physiological function
-
in Arabidopsis thaliana, the enzyme is essential for reproductive viability
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenosine 5'-O-(3-thiotriphosphate) + adenosine 5-phosphosulfate
ADP + 3'-thiophosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
535fold lower Vmax than with ATP
-
?
adenosine 5'-phosphosulfate + ATP
3'-phosphoadenosine 5'-phosphosulfate + ADP
show the reaction diagram
B0FWC4
-
-
-
?
ATP + adenosine 5'-O-(2-fluorodiphosphate)
ADP + 3'-phosphoadenosine 5'-O-(2-fluorodiphosphate)
show the reaction diagram
-
15fold lower Vmax than with adenosine 5-phosphosulfate
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
O43252
-
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
O43252
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
show the reaction diagram
-
synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
O43252
synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q27128, -
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
show the reaction diagram
O43252
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
O54820
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-, O43252, O95340
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q27128, -
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
show the reaction diagram
Q27128
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
show the reaction diagram
-, Q43295
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
show the reaction diagram
Q12657
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
show the reaction diagram
-
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
show the reaction diagram
Q12657
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
show the reaction diagram
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
show the reaction diagram
O43252
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
show the reaction diagram
O43252
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
show the reaction diagram
-, O49196
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
show the reaction diagram
O54820
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
show the reaction diagram
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
show the reaction diagram
Q9VW48
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
show the reaction diagram
Q802U9
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
show the reaction diagram
Q90XY2
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
show the reaction diagram
-
ultimate step in biosynthesis of 3'-phosphoadenosine 5'-phosphosulfate, the primary biological sulfuryl donor
-
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
second step in pathway of assimilation of inorganic sulfate
-
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
enzyme is involved in sulfation of cartilaginous chondroitin sulfate, reduced enzyme activity causes brachymorphism
-
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-, O43252, O95340
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
show the reaction diagram
-
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
show the reaction diagram
Escherichia coli AN1460
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
-
ATP + adenylyl sulfate
ADP + 3'-phosphoadenylyl sulfate
show the reaction diagram
-
-
-
-
?
CTP + adenosine 5-phosphosulfate
CDP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
-
-
?
CTP + adenosine 5-phosphosulfate
CDP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
-
-
?
dATP + adenosine 5-phosphosulfate
dADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
-
-
?
MgATP2- + adenosine 5'-phosphosulfate
MgADP- + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
Q3SM86, -
-
-
-
?
MgATP2- + adenylyl sulfate
MgADP- + 3'-phosphoadenylyl sulfate
show the reaction diagram
O95340
-
-
-
r
MgATP2- + adenylyl sulfate
MgADP- + 3'-phosphoadenylyl sulfate
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
O43252
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
show the reaction diagram
-
synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
O43252
synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate
-
-
?
ATP + adenosine 5'-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
ultimate step in biosynthesis of 3'-phosphoadenosine 5'-phosphosulfate, the primary biological sulfuryl donor
-
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
second step in pathway of assimilation of inorganic sulfate
-
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-
enzyme is involved in sulfation of cartilaginous chondroitin sulfate, reduced enzyme activity causes brachymorphism
-
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram
-, O43252, O95340
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
show the reaction diagram
-
enzyme is involved in cysteine synthesis and sulfate assimilation, enzyme is required for activity of the avirulence rice resistant protein AvrXa21
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cd2+
-
0.42 and 1.1 mM, maximal activation of forward reaction in the presence of 0.42 and 1.1 mM ATP respectively
Co2+
-
5 mM, 58% of activation with Mg2+ or Mn2+
Co2+
-
0.42 and 1.1 mM, maximal activation of forward reaction in the presence of 0.42 and 1.1 mM ATP respectively, inhibitory in excess
Co2+
-
164% of activation with Mg2+
EDTA
-
assay with 0.25 mM EDTA
K+
-
10 mM, 60% stimulation compared to Mg2+
K+
-
assay with 100 mM KCl
Mg2+
-
activation
Mg2+
-
activation
Mg2+
Penicillium duponti
-
activation
Mg2+
-
0.42 and 1.1 mM, maximal activation of forward reaction in the presence of 0.42 and 1.1 mM ATP respectively, maximal activation of reverse reaction at concentrations that equals the ADP concentration at 0.03 and 0.07 mM
Mg2+
-
activation
Mg2+
-
affinity for adenosine 5'-phosphosulfate decreases by 15fold in the absence of Mg2+
Mg2+
O43252
in complex with ATP
Mg2+
-
assay with 2.5 mM MgCl2
Mn2+
-
5 mM yield the same reaction velocity as 5 mM Mg2+, excess inhibits slightly
Mn2+
-
0.42 and 1.1 mM, maximal activation of forward reaction in the presence of 0.42 and 1.1 mM ATP respectively, inhibitory in excess
Mn2+
-
274% of activation with Mg2+
NaCl
O43252
increased activity at high salt conditions, 100 mM
Zn2+
-
309% of activation with Mg2+
Mn2+
-
1 Mn2+ ion per subunit in the absence of substrate, 2 Mn2+ bind per subunit when APS or the ATP analog 5'-adenylylimidodiphosphate are present, afffinity for Mn2+ increases 23fold when the enzyme is phosphorylated
additional information
-
a divalent cation is required for activity
additional information
-
not activated by Cu2+ or Na+
additional information
-
no monovalent cations required, stereochemistry of divalent metal ion coordination
additional information
-
a divalent cation is required for activity
additional information
-
enzyme uses multiple metal ions to catalyze phosphoryl group transfer
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2'-Phosphoadenosine 5'-phosphosulfate
-
-
2,4,6-Trinitrobenzene sulfonate
-
in the presence or absence of ATP-sulfurylase
2,4,6-Trinitrobenzene sulfonate
-
0.05 mM, complete inhibition
2,4,6-Trinitrobenzene sulfonate
-
0.05 mM, 28% inhibition
2,6-dichlorophenol indophenol
-
0.05 mM, complete inhibition
3'-phosphoadenosine 5'-phosphosulfate
-
product inhibition
4-Aminophenylacetate
-
0.008 mM, 50% inhibition
adenosine 5'-phosphosulfate
-
potent substrate inhibition, ATP reverses
adenosine 5'-phosphosulfate
-
kinetics
adenosine 5'-phosphosulfate
-
-
adenosine 5'-phosphosulfate
-
substrate inhibition above 0.03-0.04 mM
adenosine 5'-phosphosulfate
-
-
adenosine 5'-phosphosulfate
-
substrate inhibition above 0.01 mM
adenosine 5'-phosphosulfate
-
-
adenosine 5'-phosphosulfate
O49196
uncompetitive inhibition above 0.001 mM
adenosine 5'-phosphosulfate
-
adenosine 5'-phosphosulfate can bind to E-MgADP forming a catalytically inactive E-MgADP-APS ternary complex
adenosine 5'-phosphosulfate
O43252
substrate inhibition
adenosine 5'-phosphosulfate
O95340
acts as a strong uncompetitive inhibitor of the APS kinase reaction
adenosine 5'-phosphosulfate
-
-
adenosine 5'-phosphosulfate
-
-
adenylyl sulfate
O95340
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
ATP
-
inhibition by free ATP, i.e. in excess of total Mg2+
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
Bromosuccinimide
-
strong inhibition
Bromosuccinimide
-
0.05 mM, complete inhibition
Cd2+
-
in excess
Co2+
-
2 mM, 63% inhibition
Co2+
-
in excess, activating below
Cu2+
-
2 mM, 90% inhibition
diethyldicarbonate
-
in the presence or absence of ATP-sulfurylase
EDTA
O49196
complete inhibition
ferricyanide
-
0.05 mM, complete inhibition
iodoacetamide
-
strong inhibition, dithiothreitol partially protects
Mercuriphenylacetate
-
0.05 mM, complete inhibition
N-ethylmaleimide
-
0.02 mM, 50% inhibition
NaClO3
-
6.57 mM, 50% inhibition of brain PAPSS activity, 3.26 mM, 50% inhibition of liver PAPSS
oxidized glutathione
-
thioredoxin reverses inactivation
p-chloromercuribenzoate
-
0.005 mM, 50% inhibition
Mn2+
-
in excess, activating below
additional information
-
not inhibited by Mg2+
-
additional information
-
-
-
additional information
-
not inhibited by ferricyanide
-
additional information
-
not inhibited by adenosine 5'-phosphosulfate
-
additional information
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ammonium sulfate
-
high salt activates at high adenosine 5'-phosphosulfate concentrations but inhibits at low adenosine 5'-phosphosulfate concentrations
ascorbate
-
activation
dithioerythritol
-
2 mM, 200% activation
dithiothreitol
-
activation
dithiothreitol
-
2 mM, 200% activation; activation
dithiothreitol
O49196
activity declines rapidly in the absence of dithiothreitol
dithiothreitol
O43252
-
glutathione
-
reduced glutathione increases the activity significantly
High ionic strength
O49196
maximal activity at a high concentration of buffer-salts either alone or plus dithiothreitol and thioredoxin 1 from Escherichia coli
-
Na2SO3
-
5 mM, 200% activation
thioredoxin
-
activation in the presence of dithiothreitol
thioredoxin
O49196
essential for activity
Thioredoxin f
-
from spinach, 0.002 mg, 3fold activation in the presence of saturating concentrations of thiols
-
L-cysteine
-
activation
additional information
-
not activated by 2-mercaptoethanol
-
additional information
-
not activated by 2-mercaptoethanol
-
additional information
-
not activated by 2-mercaptoethanol; not activated by L-cysteine and ascorbate
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.003
-
3'-phosphoadenosine 5'-phosphosulfate
-
pH 8.1, 30C, wild-type enzyme
0.008
-
3'-phosphoadenosine 5'-phosphosulfate
-
pH 8.0, 30C
0.039
-
3'-phosphoadenosine 5'-phosphosulfate
-
pH 8.1, 30C, S107A mutant enzyme
0.37
-
3'-phosphoadenosine 5'-phosphosulfate
-
pH 8.0, 25C
0.37
-
3'-phosphoadenosine 5'-phosphosulfate
-
-
0.06
-
adenosine 5'-O-(3-thiotriphosphate)
-
pH 8.0
0.00014
-
adenosine 5'-phosphosulfate
O49196
pH 7.4, 25C
0.00025
-
adenosine 5'-phosphosulfate
-
pH 8.0, 25C
0.0004
-
adenosine 5'-phosphosulfate
O43252
pH 8.0, 37C, COS-1 cell-expressed full length PAPS synthase
0.00043
-
adenosine 5'-phosphosulfate
-
oxidized wild type enzyme, at pH 7.5 and 17C
0.00043
-
adenosine 5'-phosphosulfate
-
oxidized wild type enzyme, at pH 7.5 and 25C
0.00045
-
adenosine 5'-phosphosulfate
-
-
0.00048
-
adenosine 5'-phosphosulfate
-
wild type enzyme, at pH 7.5 and 17C
0.00048
-
adenosine 5'-phosphosulfate
-
reduced wild type enzyme, at pH 7.5 and 17C
0.00048
-
adenosine 5'-phosphosulfate
-
reduced wild type enzyme, at pH 7.5 and 25C
0.0005
-
adenosine 5'-phosphosulfate
-
pH 8.0
0.0006
-
adenosine 5'-phosphosulfate
O43252
pH 8.0, 37C, COS-1 cell-expressed N-terminal fragment
0.0007
-
adenosine 5'-phosphosulfate
-
mutant enzyme D136N, at pH 7.5 and 17C
0.0008
-
adenosine 5'-phosphosulfate
-
pH 8.1, 30C
0.00087
-
adenosine 5'-phosphosulfate
-
oxidized mutant enzyme C86A/C119A, at pH 7.5 and 25C
0.00092
-
adenosine 5'-phosphosulfate
-
mutant enzyme D136A, at pH 7.5 and 17C
0.001
-
adenosine 5'-phosphosulfate
-
pH 8.1, 30C, wild-type enzyme at 100 mM ammonium sulfate
0.0014
-
adenosine 5'-phosphosulfate
-
pH 8.0, 30C
0.0014
-
adenosine 5'-phosphosulfate
-
-
0.00172
-
adenosine 5'-phosphosulfate
-
mutant enzyme R93A, at pH 7.5 and 17C
0.0019
-
adenosine 5'-phosphosulfate
-
reduced mutant enzyme C86A/C119A, at pH 7.5 and 25C
0.002
-
adenosine 5'-phosphosulfate
-
pH 6.8, 30C
0.0023
-
adenosine 5'-phosphosulfate
O43252
pH 8.0, 37C, Escherichia coli-expressed N-terminal fragment
0.0026
-
adenosine 5'-phosphosulfate
O43252
pH 8.0, 37C, Escherichia coli-expressed full length PAPS synthase
0.00263
-
adenosine 5'-phosphosulfate
-
N-terminal truncation variant APSKDELTA96, at pH 7.5 and 17C
0.0036
-
adenosine 5'-phosphosulfate
-
25C
0.0042
-
adenosine 5'-phosphosulfate
O43252
pH 8.0, 30C
0.006
-
adenosine 5'-phosphosulfate
-
pH 8.0
0.012
-
adenosine 5'-phosphosulfate
-
pH 8.1, 30C, S107A mutant enzyme at 100 mM ammonium sulfate
0.042
-
adenosine 5'-phosphosulfate
-
pH 8.0, 30C
0.002
-
adenylyl sulfate
O95340
value is below 0.002 for a deletion mutant lacking the first 34 amino acids of the N-terminus, delta34N; value is below 0.002 for wildtype adenylyl sulfate
0.0032
-
adenylyl sulfate
O95340
mutant R37A
0.0037
-
adenylyl sulfate
O95340
mutant R40A
0.0046
-
adenylyl sulfate
O95340
deletion mutant lacking the first 50 amino acids of the N-terminus, delta50N
0.007
-
ATP
-
pH 6.8, 30C
0.01
-
ATP
-
pH 8.0, 25C
0.05
0.06
ATP
-
pH 8.0
0.08
-
ATP
-
pH 8.0, 37C, PAPSS 1
0.147
-
ATP
O49196
pH 7.4, 25C
0.23
-
ATP
O43252
pH 8.0, 37C, COS-1 cell-expressed N-terminal fragment
0.26
-
ATP
O43252
pH 8.0, 37C, E. coli expressed N-terminal fragment
0.36
-
ATP
-
pH 8.0, 37C, PAPSS 2b
0.38
-
ATP
-
pH 8.0, 37C, PAPSS 2a
0.45
-
ATP
O43252
pH 8.0, 37C, E. coli-expressed full length PAPS synthase
1.5
-
ATP
-
pH 8.0, 30C
0.13
-
MgADP-
-
pH 8.0, 25C
0.13
-
MgADP-
-
-
0.14
-
MgATP2-
O43252
pH 8.0, 30C
0.8
-
MgATP2-
-
pH 8.1, 30C, wild-type enzyme at 100 mM ammonium sulfate
0.8
-
MgATP2-
-
pH 8.1, 30C
2.4
-
MgATP2-
-
pH 8.1, 30C, S107A mutant enzyme
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
kinetic study
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.09
-
adenosine 5'-O-(3-thiotriphosphate)
-
pH 8.0
14.1
-
adenosine 5'-phosphosulfate
-
oxidized wild type enzyme, at pH 7.5 and 17C
14.1
-
adenosine 5'-phosphosulfate
-
oxidized wild type enzyme, at pH 7.5 and 25C
29
-
adenosine 5'-phosphosulfate
-
mutant enzyme D136A, at pH 7.5 and 17C
45
-
adenosine 5'-phosphosulfate
-
mutant enzyme D136N, at pH 7.5 and 17C
82.3
-
adenosine 5'-phosphosulfate
-
N-terminal truncation variant APSKDELTA96, at pH 7.5 and 17C
136
-
adenosine 5'-phosphosulfate
-
mutant enzyme R93A, at pH 7.5 and 17C
203
-
adenosine 5'-phosphosulfate
-
oxidized mutant enzyme C86A/C119A, at pH 7.5 and 25C
239
-
adenosine 5'-phosphosulfate
-
reduced mutant enzyme C86A/C119A, at pH 7.5 and 25C
272
-
adenosine 5'-phosphosulfate
-
wild type enzyme, at pH 7.5 and 17C
272
-
adenosine 5'-phosphosulfate
-
reduced wild type enzyme, at pH 7.5 and 17C
272
-
adenosine 5'-phosphosulfate
-
reduced wild type enzyme, at pH 7.5 and 25C
50
-
adenosine 5-phosphosulfate
-
pH 8.0, 30C
0.17
-
adenylyl sulfate
O95340
mutant R40A
0.2
-
adenylyl sulfate
O95340
deletion mutant lacking the first 50 amino acids of the N-terminus, delta50N
0.207
-
adenylyl sulfate
O95340
mutant R37A
0.315
-
adenylyl sulfate
O95340
deletion mutant lacking the first 34 amino acids of the N-terminus, delta34N
0.364
-
adenylyl sulfate
O95340
wildtype adenylyl sulfate
1.7
-
ATP
-
pH 8.0, 37C, PAPSS 1
2.3
-
ATP
-
pH 8.0, 37C, PAPSS 2a
4.4
-
ATP
-
pH 8.0, 37C, PAPSS 2b
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
31000
-
adenosine 5'-phosphosulfate
-
mutant enzyme D136A, at pH 7.5 and 17C
6431
31300
-
adenosine 5'-phosphosulfate
-
N-terminal truncation variant APSKDELTA96, at pH 7.5 and 17C
6431
32700
-
adenosine 5'-phosphosulfate
-
oxidized wild type enzyme, at pH 7.5 and 17C
6431
32800
-
adenosine 5'-phosphosulfate
-
oxidized wild type enzyme, at pH 7.5 and 25C
6431
64000
-
adenosine 5'-phosphosulfate
-
mutant enzyme D136N, at pH 7.5 and 17C
6431
125000
-
adenosine 5'-phosphosulfate
-
reduced mutant enzyme C86A/C119A, at pH 7.5 and 25C
6431
189000
-
adenosine 5'-phosphosulfate
-
mutant enzyme R93A, at pH 7.5 and 17C
6431
233000
-
adenosine 5'-phosphosulfate
-
oxidized mutant enzyme C86A/C119A, at pH 7.5 and 25C
6431
567000
-
adenosine 5'-phosphosulfate
-
wild type enzyme, at pH 7.5 and 17C
6431
567000
-
adenosine 5'-phosphosulfate
-
reduced wild type enzyme, at pH 7.5 and 17C
6431
567000
-
adenosine 5'-phosphosulfate
-
reduced wild type enzyme, at pH 7.5 and 25C
6431
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0004
-
adenosine 5'-phosphosulfate
-
pH 8.0, 25C
0.00251
-
adenosine 5'-phosphosulfate
-
oxidized wild type enzyme, at pH 7.5 and 17C
0.00251
-
adenosine 5'-phosphosulfate
-
oxidized wild type enzyme, at pH 7.5 and 25C
0.0045
-
adenosine 5'-phosphosulfate
O49196
pH 7.4, 25C
0.013
-
adenosine 5'-phosphosulfate
-
pH 8.1, 30C
0.0328
-
adenosine 5'-phosphosulfate
-
mutant enzyme D136N, at pH 7.5 and 17C
0.0348
-
adenosine 5'-phosphosulfate
-
reduced mutant enzyme C86A/C119A, at pH 7.5 and 25C
0.0375
-
adenosine 5'-phosphosulfate
-
wild type enzyme, at pH 7.5 and 17C
0.0375
-
adenosine 5'-phosphosulfate
-
reduced wild type enzyme, at pH 7.5 and 17C
0.0375
-
adenosine 5'-phosphosulfate
-
reduced wild type enzyme, at pH 7.5 and 25C
0.0416
-
adenosine 5'-phosphosulfate
-
oxidized mutant enzyme C86A/C119A, at pH 7.5 and 25C
0.017
-
adenylyl sulfate
O95340
wild type adenylyl sulfate
0.029
-
adenylyl sulfate
O95340
deletion mutant lacking the first 34 amino acids of the N-terminus, delta34N
0.048
-
adenosine 5'-phosphosulfate
O43252
pH 8.0, 30C
additional information
-
adenylyl sulfate
O95340
no inhibition of a deletion mutant lacking the first 50 amino acids of the N-terminus, delta50N; no inhibition of mutant R37A; no inhibition of mutant R40A
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00016
-
-
recombinant enzyme
0.000298
-
-
wild type activity, specific activities given for all mutant enzymes
0.12
-
O43252
pH 8.0. 30C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7.5
-
in MES-Tricine-HEPES buffer
6.8
-
-
in imidazole buffer
7.5
-
O95340
assay at
7.5
-
-
assay at
8
-
-
90% of maximal activity at pH 7.5 and pH 8.5
additional information
-
-
pI: 6.2
additional information
-
-
-
additional information
-
-
pI: 5.5; pI: 7.4
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8.5
-
approx. 80% of maximal activity at pH 5.5, approx. half-maximal activity at pH 8.5
6
8
-
approx. 80% of maximal activity at pH 6.0, approx. 65% of maximal activity at pH 8.0, imidazole buffer
6
8
-
continuous increase of activity from pH 6.0 to 8.0
6
8.5
-
approx. 70% of maximal activity at pH 6.0, approx. 75% of maximal activity at pH 8.5, MES-Tricine-HEPES buffer
6.8
8
-
maximal activity at pH 6.8, approx. half-maximal activity at pH 8.0
7.5
9
-
approx. half-maximal activity at pH 7.5, approx. 80% of maximal activity at pH 9.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
30
-
-
assay at
37
-
O95340
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
Q27128, -
PAPS synthetase mRNA
Manually annotated by BRENDA team
-
major isoform PAPSS 2
Manually annotated by BRENDA team
O43252, O95340
; high expression of PAPSS 1
Manually annotated by BRENDA team
O54820
PAPSS 1 is the predominant isoform in adults
Manually annotated by BRENDA team
-
PAPSS 1 is the predominant isoform in adults
Manually annotated by BRENDA team
O43252, O95340
; high expression of PAPSS 2
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
Q27128, -
PAPS synthetase mRNA
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
-
APS kinase mRNA
Manually annotated by BRENDA team
-
major isoform PAPSS1
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
O43252, O95340
; high expression of PAPSS 2; predominantly PAPS2
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
Penicillium duponti
-
-
Manually annotated by BRENDA team
Q27128, -
PAPS synthetase mRNA
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
-
APS kinase mRNA
Manually annotated by BRENDA team
O43252, O95340
PAPSS 1
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
-
PAPSS 1, 2a and 2b
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
localization is suggested by an in vitro chloroplast import assay
Manually annotated by BRENDA team
Escherichia coli AN1460
-
-
-
Manually annotated by BRENDA team
-
isoforms APK4, AK1, and APK2
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
29500
-
-
in the presence of dithiothreitol, gel filtration
40000
45000
-
gel filtration
40000
-
-
phosphorylated enzyme, gel filtration
49500
52000
-
gel filtration
50000
-
-
gel filtration
57000
-
-
gel filtration at 22C
57000
-
Penicillium duponti
-
gel filtration at 22C or 46C
57000
-
-
gel filtration at 22C
58000
-
-
gel filtration
59000
60000
-
gel filtration
61000
-
-
gel filtration
80000
-
-
dephosphorylated enzyme, gel filtration
85000
90000
-
gel filtration
150000
-
O43252
gel filtration
162000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 44000, SDS-PAGE
?
-
x * 22321, deduced from DNA sequence of cysC coding region
?
Q27128, -
x * 57000, in vitro translation product, SDS-PAGE; x * 68000, deduced from nucleotide sequence
?
-
x * 29786, deduced from nucleotide sequence
?
O49196
x * 31977, deduced from nucleotide sequence
dimer
-
2 * 30000, SDS-PAGE
dimer
-
2 * 33000, gel filtration at 46C, the enzyme dissociates into two inactive monomers by heating above 42C
dimer
-
2 * 31000, dissociation
dimer
-
2 * 21000, phosphorylated enzyme, SDS-PAGE; native protein undergoes dimer-tetramer interconversions depending on experimental conditions and phosphorylation state
dimer
-
2 * 40000-45000, dithiothreitol-treated enzyme, SDS-PAGE
dimer
-
2 * 28000-29500, dithiothreitol-treated enzyme, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 23670
dimer
-
2 * 716000, MALDI-TOF mass spectrometry, native mass by gel filtration
dimer
O43252
2 * 71000
dimer
-
2 * 71000, asymmetric complex, only one monomer is occupied by a bound ATP or ADP, crystal structure analysis
dimer
Escherichia coli AN1460
-
2 * 40000-45000, dithiothreitol-treated enzyme, SDS-PAGE
-
homodimer
-
2 * 22000, SDS-PAGE
homohexamer
Q3SM86, -
6 * 60500, calculated, crystall structure analysis
tetramer
-
4 * 14500, SDS-PAGE
tetramer
-
4 * 21000, dephosphorylated enzyme, SDS-PAGE; native protein undergoes dimer-tetramer interconversions depending on experimental conditions and phosphorylation state
tetramer
-
monomers and dimers are catalytically active
tetramer
Escherichia coli AN1460
-
monomers and dimers are catalytically active
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
side-chain modification
-
enzyme is phosphorylated upon incubation with ATP, phosphorylation site is identified as Ser109, phosphorylated enzyme is kinetically competent
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystals are grown by hanging drop vapor diffusion at 25C in 40% (v/v) ethanol, 1.0% (w/v) PEG 6000, 50 mM sodium acetate and 5 mM MgATP
-, O67174
APSK isoform 1 in complex with beta,gamma-imidoadenosine-5'-triphosphate, Mg2+, and adenosine 5'-phosphosulfate, hanging drop vapor diffusion method, using 100 mM HEPES, pH 7.5, 200 mM MgCl2, and 15-17.5% (w/v) PEG 2000
-
in complex with adenosine 5'-phosphosulfate, hanging drop vapor diffusion method, using 100 mM HEPES, pH 7.25, 200 mM MgCl2, and 1517.5% (w/v) PEG 2000
-
; crystals are grown at room temperature using hanging drops containing equal volumes of protein and reservoir solution
O95340
crystal structures of the PAPSS1 APS-kinase domain in complex with APS and in complex with the products PAPS and ADP are solved, both structures of isolated domain, obtained in different crystal forms, reveal symmetrical dimers
-
hanging drop vapor diffusion method
-
crystals are grown in 1.7 M NaH2PO4, 300 mM K2HPO4 and 100 mM Na-succinate, pH 4.0 by hanging drop vapor diffusion at room temperature, crystal structure of E-ADP-APS ternary complex at 1.43 A, crystal structure of E-ADP binary complex at 2.0 A
-
hanging-drop vapor diffusion method
Q3SM86, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
below, reversible inactivation at 30C, reactivation rate increases with increasing pH
7
-
-
reversible inactivation at 42C
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
no loss of activity after 7 d at room temperatures
25
-
-
70% loss of activity after 7 d at room temperature
35
-
-
inactivation above, reversible by cooling to 0-30C
36
-
-
equilibrium between active and inactive enzyme form
37
-
-
no loss of activity after 2 h, recombinant enzyme
40
-
-
reversible inactivation above by subunit dissociation, kinetics, MgATP2- or MgADP- stimulate reactivation
43
-
-
reversible inactivation, t1/2: 1 min
50
-
-
rapid loss of activity, approx. 80% of activity is recovered upon cooling at 0C, presence of MgATP2- accelerates the recovery process
50
-
-
1 min, 80% reversible inactivation
60
100
-
1 min, 85% reversible inactivation
60
-
-
complete inactivation after 15 min
70
-
-
no significant loss of activity after 15 min
80
-
-
irreversible inactivation, t1/2: 47 min, pH 8, 0.023 mg protein/ml
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme is rapidly inactivated by dialysis, dilution or freezing even in the presence of glycerol
O49196
more stable in ampholyte polybuffer 74 than in Tris or imidazole buffers
-
slow freezing can cause loss of activity
-
rapid loss of activity in dilute solutions
-
slow inactivation in dilute solutions, even at low temperatures
-
stable to ammonium sulfate precipitation
-
rapid loss of activity in dilute solutions
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
generation of atomic oxygen during the photodeoxygenation of 2,8-dihydroxymethyldibenzothiophene S-oxide is capable of oxidizing the enzyme at the regulatory thiol residues
-
722457
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, recombinant APS kinase fusion protein, 1 year, no loss of activity
-
-20C, stable to prolonged storage
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ni-NTA column chromatography and Superdex-200 gel filtration
-
nickel affinity column chromatography and Superdex-200 gel filtration
-
ammonium sulfate, Sephacryl S-200, partially purified
-
ammonium sulfate, Sephacryl S-300, chromatofocusing, 2'5'-ADP-agarose
-
ammonium sulfate, Giogel P2, Blue Sepharose, Sephacryl S-300, PBE 94
-
ammonium sulfate, phenyl-Sepharose, Q-Sepharose, Sephacryl S-300, hydroxylapatite, pentyl- agarose, aminohexyl agarose, ATP-agarose
-
DEAE-Sepharose, Matrex gel blue A, phenyl Cellofine
-
; protein solutions are applied on Blue-Sepharose columns and further purified by ion-exchange chromatography
O95340
Ni2+-column, recombinant enzyme
-
protein solution is loaded on a Glutathione-Sepharose Fast Flow column and further purified by gel-filtration chromatography using Superdex 200
-
recombinant enzyme using His-tag
O43252
recombinant protein using His-tag
-
recombinant protein using His-tag
-
ammonium sulfate, Affi-gel blue, Matrix-gel green, Agarose A
-
partial
Penicillium duponti
-
ammonium sulfate, affinity chromatography, gel filtration, ion-exchange chromatography
-
alumina C-gamma gel, ammonium sulfate, hydroxyapatite, Cellex CM, unstable upon column chromatography
-
ammonium sulfate, Blue Sepharose, Sephacryl S-200, PBE 94, Red Sepharose, phenyl-sepharose
-
Ni-NTA column chromatography and Superdex-200 gel filtration
-
immobilized metal ion affinity chromatography (Ni2+)
Q3SM86, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
O49196
expression in Escherichia coli as fusion protein with glutathione-S-transferase or maltose binding protein
-
structural gene cysC
-
APS kinase domain (amino acids 25-227) of the PAPSS1 coding region are expressed as a GST-fusion protein in Escherichia coli
O95340
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)
-
expressed in COS-1 and HEK293 cells
O43252
expression of full-length PAPS synthase and 1-268 N-terminal fragment in COS-1 cells and Escherichia coli
O43252
the APS-kinase domain (25-227 amino acid resiudes) of the PAPSS1 coding region are expressed as a GST-fusion protein in Escherichia coli BL-21
-
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)
-
expresssion in Escherichia coli
-
expression of wild-type and S107A mutant enzyme in Escherichia coli
-
expressed in Escherichia coli BL21-DE3
B0FWC4
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3)
Q3SM86, -
in vitro transcription/translation
Q27128, -
expression in Escherichia coli cysD-mutant
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
O49196
similar catalytic activity as wild-type
S182F
O49196
similar catalytic activity as wild-type
delta34N
O95340
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
O95340
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
O43252
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
-
slightly lower APS kinase activity than wild-type
G427A
O43252, O95340
-
G427A/H428A
-
no APS kinase activity
H425A
-
no APS kinase activity
H425A
O43252, O95340
-
H428A
-
no APS kinase activity
N426K
-
2fold higher APS kinase activity than wild-type
N426K
O43252, O95340
-
R333C
O43252
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
O95340
mutant clone shows no substrate inhibition by adenylyl sulfate, mutant is kinetically indistinguishable from deletion mutant delta50N lacking the first N-terminal residues
R40A
O95340
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
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
D136N
-
the mutant displays drastically reduced affinity for adenosine 5'-phosphosulfate compared to the wild type enzyme
additional information
-
the N-terminal truncation variant (APSKDELTA96) is completely insensitive to substrate inhibition by adenosine 5-phosphosulfate
H428A
O43252, O95340
-
additional information
O95340
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; 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