Information on EC 2.7.1.25 - adenylyl-sulfate kinase:
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

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EC NUMBERCOMMENTARY
2.7.1.25-

RECOMMENDED NAMEGeneOntology No.
adenylyl-sulfate kinaseGO:0004020

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
show the reaction diagram		mechanismPenicillium chrysogenum-641210
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
show the reaction diagram		mechanismEscherichia coli-641215, 641216
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
show the reaction diagram		kinetic scheme for APS kinaseEscherichia coli-641228
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-Penicillium chrysogenum-641233
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
phospho group transfer----

PATHWAYKEGG LinkMetaCyc Link
Metabolic pathways01100 -
Microbial metabolism in diverse environments01120 -
Purine metabolism00230 -
sulfate activation for sulfonation-PWY-5340
Sulfur metabolism00920 -

SYSTEMATIC NAMEIUBMB Comments
ATP:adenylyl-sulfate 3'-phosphotransferaseThe 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).

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
3'-phosphoadenosine 5'-phosphosulfate synthetase1Homo sapiens--674838, 675437
3'-phosphoadenosine-5'-phosphosulfate synthetase----
5'-phosphoadenosine sulfate kinase----
adenosine 5'-phosphosulfate kinase----
adenosine 5-phosphosulfate kinaseHomo sapiensO95340adenosine 5-phosphosulfate kinase is a domain of human 3-phosphoadenosine 5-phosphosulfate synthetase 1674838
adenosine phosphosulfate kinase----
adenosine phosphosulfokinase----
adenosine-5'-phosphosulfate 3'-phosphotransferase----
adenosine-5'-phosphosulfate-3'-phosphokinase----
adenosine-5'phosphosulfate kinase----
adenylylsulfate 3'-phosphotransferase----
adenylylsulfate kinase----
APS kinase----
APS-kinasePhytophthora infestans T30-4B0FWC4part of a triple fusion protein of APS-kinase, ATP-sulfurylase, and pyrophosphatase705207
ATP adenosine-5'-phosphosulfate 3'-phosphotransferase----
ATP sulfurylase-APS kinaseAquifex aeolicusO67174bifunctional enzyme675422
kinase, adenylylsulfate (phosphorylating)----
PAPS 2Homo sapiens--641229
PAPS synthase---641224
PAPS synthetase---641220
PAPS synthetaseHomo sapiens-two isoforms, type 1 and 2660598
PAPSSHomo sapiensO43252PAPS synthetase, two isoforms: PAPSS1 and PAPSS2661026
PAPSS 1Homo sapiens--641229
PAPSS 1Homo sapiensO43252, O95340; 641234
PAPSS1Homo sapiens--674838, 675437
MgATP:APS 3'-phosphotransferaseThiobacillus denitrificansQ3SM86-701464
additional informationMus musculus-bifunctional enzyme with ATP sulfurylase activity and adenosine phosphosulfate kinase activity, catalyzes the formation of 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate662177
additional informationHomo sapiens-bifunctional enzyme with ATP sulfurylase activity and adenosine phosphosulfate kinase activity, catalyzes the formation of 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate660598, 661125, 662642

CAS REGISTRY NUMBERCOMMENTARY
9012-38-8-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Aquifex aeolicus-675422O67174SwissProtManually annotated by BRENDA team
Arabidopsis thaliana-641222Q43295SwissProtManually annotated by BRENDA team
Arabidopsis thalianaAPS kinase gene Atakn1; APS kinase gene Atakn2641230O49196SwissProtManually annotated by BRENDA team
Caenorhabditis elegans-641234--Manually annotated by BRENDA team
Cavia porcellusguinea pig641231O54820SwissProtManually annotated by BRENDA team
Cavia porcellusguinea pig, isoenzyme PAPSS 1641234O54820SwissProtManually annotated by BRENDA team
Chlamydomonas reinhardtiiCW15, cell wall mutant641212, 641213, 641214--Manually annotated by BRENDA team
Danio reriozebra fish641234Q802U9GenBankManually annotated by BRENDA team
Drosophila melanogaster-641234Q9VW48SwissProtManually annotated by BRENDA team
Escherichia coli-641216, 641228--Manually annotated by BRENDA team
Escherichia coli-641223P23846GenBankManually annotated by BRENDA team
Escherichia colioverproducing K12 strain, JM83/pTL3/pGP1-2641215--Manually annotated by BRENDA team
Escherichia colistrain AN1460641217--Manually annotated by BRENDA team
Escherichia coli AN1460strain AN1460641217--Manually annotated by BRENDA team
Geobacillus stearothermophilus-641221--Manually annotated by BRENDA team
Homo sapiens-641227, 662642, 674838O43252SwissProtManually annotated by BRENDA team
Homo sapiens-641234, 660598, 675437--Manually annotated by BRENDA team
Homo sapiens-674838O95340SwissProtManually annotated by BRENDA team
Homo sapiensbifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase641224O43252SwissProtManually annotated by BRENDA team
Homo sapiensisoenzyme PAPSS 2; isoenzyme PAPSS 2b, splice variant of PAPSS2, several SNPs and polymorphisms are identified with reference to PAPSS 1 and 2641234O95340SwissProtManually annotated by BRENDA team
Homo sapiensisoform 1661125O43252SwissProtManually annotated by BRENDA team
Homo sapiensisoforms PAPSS 1 and PAPSS 2641229--Manually annotated by BRENDA team
Homo sapiensisoforms PAPSS 1, PAPSS 2a and 2b641231--Manually annotated by BRENDA team
Homo sapiensPAPSS 1641234O43252SwissProtManually annotated by BRENDA team
Homo sapiensPAPSS1; Caucasian-American and African-American subjects661026O43252SwissProtManually annotated by BRENDA team
Mus musculus-662177--Manually annotated by BRENDA team
Mus musculusbifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase641225--Manually annotated by BRENDA team
Mus musculusisoenzymes PAPS 1 and 2641234--Manually annotated by BRENDA team
Penicillium chrysogenum-641207, 641208, 641209, 641210, 641226--Manually annotated by BRENDA team
Penicillium chrysogenum-641223, 641233Q12657SwissProtManually annotated by BRENDA team
Penicillium duponti-641208--Manually annotated by BRENDA team
Phytophthora infestans T30-4-705207B0FWC4SwissProtManually annotated by BRENDA team
Pyropia yezoensisUeda, marine alga641211--Manually annotated by BRENDA team
Rattus norvegicus-641204, 641205, 641220--Manually annotated by BRENDA team
Riftia pachyptilahydrothermal vent tube worm641206--Manually annotated by BRENDA team
Saccharomyces cerevisiae-641217, 641218, 641219, 641221--Manually annotated by BRENDA team
Sinorhizobium melilotiNodQ gene641232--Manually annotated by BRENDA team
Takifugu rubripespuffer fish641234Q90XY2UniProtManually annotated by BRENDA team
Thiobacillus denitrificans-701464Q3SM86UniprotManually annotated by BRENDA team
Urechis caupo-641234Q27128SwissProtManually annotated by BRENDA team
Urechis caupomarine worm, bifunctional PAPS senthetase641220Q27128SwissProtManually annotated by BRENDA team
Xanthomonas oryzaepv. oryzae, Philippine race 6, raxQ gene641232--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
metabolismPhytophthora infestans T30-4B0FWC4sulfate activation pathway705207

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM 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-phosphosulfateADP + 3'-thiophosphoadenosine 5'-phosphosulfate
show the reaction diagram		Escherichia coli-535fold lower Vmax than with ATP641228-641228?
adenosine 5'-phosphosulfate + ATP3'-phosphoadenosine 5'-phosphosulfate + ADP
show the reaction diagram		Phytophthora infestans T30-4B0FWC4-705207--?
ATP + adenosine 5'-O-(2-fluorodiphosphate)ADP + 3'-phosphoadenosine 5'-O-(2-fluorodiphosphate)
show the reaction diagram		Escherichia coli-15fold lower Vmax than with adenosine 5-phosphosulfate641228-641228?
ATP + adenosine 5'-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Mus musculus--662177--?
ATP + adenosine 5'-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiens--660598, 662642--?
ATP + adenosine 5'-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiensO43252-661026, 661125--?
ATP + adenosine 5'-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiensO43252involved in the synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate, inactivating mutations of PAPSS2 causes skeletal disorders661026--?
ATP + adenosine 5'-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiens-synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate660598--?
ATP + adenosine 5'-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiensO43252synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate661125--?
ATP + adenosine 5'-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiens-synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate, decreased activity leads to defects in skeleton662642--?
ATP + adenosine 5'-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Mus musculus-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 processes662177--?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Chlamydomonas reinhardtii-ATP can be replaced by GTP, ITP or UTP641213i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641213r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Pyropia yezoensis-ATP can be replaced by GTP, ITP or UTP641211i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641211?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Escherichia coli-no substrates are AMP, forward reaction, and 2'-phosphoadenosine 5'-phosphosulfate, reverse reaction641215i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641215r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Pyropia yezoensis-optimal concentration of APS at 0.003 mM641211i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641211?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Urechis caupoQ27128enzyme has both ATP sulfurylase and APS kinase activity641220i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641220-
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiensO43252enzyme has both ATP sulfurylase and APS kinase activity641224i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641224?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Penicillium chrysogenum-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 kinase641210i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641210r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Escherichia coli-in the absence of adenosine 5'-phosphosulfate ATP phosphorylates the enzyme at a rate equivalent to the overall kinase reaction, phosphorylation site: Ser-109641216i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641216-
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Chlamydomonas reinhardtii-GTP, ITP or UTP are poor substrates641213i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641213r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Cavia porcellusO54820i.e. adenylylsulfate or APS641231i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641231?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Sinorhizobium meliloti-i.e. adenylylsulfate or APS641232i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641232?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Chlamydomonas reinhardtii-i.e. adenylylsulfate or APS641214i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641214-
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Chlamydomonas reinhardtii-i.e. adenylylsulfate or APS641212i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641212r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Chlamydomonas reinhardtii-i.e. adenylylsulfate or APS641213i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641213r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Mus musculus-i.e. adenylylsulfate or APS641225i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641225?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Mus musculus-i.e. adenylylsulfate or APS641234i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641234?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Escherichia coli-i.e. adenylylsulfate or APS641216i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641216-
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Escherichia coli-i.e. adenylylsulfate or APS641217i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641217-
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Escherichia coli-i.e. adenylylsulfate or APS641228i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641228-
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Escherichia coli-i.e. adenylylsulfate or APS641215i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641215r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiens-i.e. adenylylsulfate or APS641229i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641229?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiens-i.e. adenylylsulfate or APS641231i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641231?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiensO43252, O95340i.e. adenylylsulfate or APS641234i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641234?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Rattus norvegicus-i.e. adenylylsulfate or APS641220i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641220-
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Rattus norvegicus-i.e. adenylylsulfate or APS641204i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641204r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Rattus norvegicus-i.e. adenylylsulfate or APS641205i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641205r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Saccharomyces cerevisiae-i.e. adenylylsulfate or APS641217i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641217-
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Saccharomyces cerevisiae-i.e. adenylylsulfate or APS641218i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641218-
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Saccharomyces cerevisiae-i.e. adenylylsulfate or APS641219i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641219?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Saccharomyces cerevisiae, Geobacillus stearothermophilus-i.e. adenylylsulfate or APS641221i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641221?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Penicillium chrysogenum-i.e. adenylylsulfate or APS641226i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641226-
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Penicillium chrysogenum-i.e. adenylylsulfate or APS641207i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641207r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Penicillium chrysogenum-i.e. adenylylsulfate or APS641208i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641208r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Penicillium chrysogenum-i.e. adenylylsulfate or APS641209i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641209r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Penicillium chrysogenum-i.e. adenylylsulfate or APS641210i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641210r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Penicillium duponti-i.e. adenylylsulfate or APS641208i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641208r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Xanthomonas oryzae-i.e. adenylylsulfate or APS641232i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641232?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Pyropia yezoensis-i.e. adenylylsulfate or APS641211i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641211?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Riftia pachyptila-i.e. adenylylsulfate or APS641206i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641206?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Urechis caupoQ27128i.e. adenylylsulfate or APS641220i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641220-
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Urechis caupoQ27128i.e. adenylylsulfate or APS641234i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641234-
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Arabidopsis thalianaQ43295i.e. adenylylsulfate or APS641222i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641222?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Penicillium chrysogenumQ12657i.e. adenylylsulfate or APS641223i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641223?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Penicillium chrysogenum-i.e. adenylylsulfate or APS641233i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641233?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Penicillium chrysogenumQ12657i.e. adenylylsulfate or APS641223i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641223r
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Escherichia coliP23846i.e. adenylylsulfate or APS641223i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641223?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiensO43252i.e. adenylylsulfate or APS641224i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641224?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiensO43252i.e. adenylylsulfate or APS641227i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641227?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Arabidopsis thalianaO49196i.e. adenylylsulfate or APS641230i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641230?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Cavia porcellusO54820i.e. adenylylsulfate or APS641234i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641234?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Candida elegans-i.e. adenylylsulfate or APS641234i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641234?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Drosophila melanogasterQ9VW48i.e. adenylylsulfate or APS641234i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641234?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Danio rerioQ802U9i.e. adenylylsulfate or APS641234i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641234?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Takifugu rubripesQ90XY2i.e. adenylylsulfate or APS641234i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate641234?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Escherichia coli-ultimate step in biosynthesis of 3'-phosphoadenosine 5'-phosphosulfate, the primary biological sulfuryl donor641216-641216?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Penicillium chrysogenum-second step in pathway of assimilation of inorganic sulfate641207-641207?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Mus musculus-enzyme is involved in sulfation of cartilaginous chondroitin sulfate, reduced enzyme activity causes brachymorphism641234-641234?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiensO43252, O95340PAPSS 1 is essential for the sulfonation of mucin like glycoproteins such as GlyCAM-1, CD34 and MAdCAM-1 in high endothelial venules641234--?
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Xanthomonas oryzae-enzyme is involved in cysteine synthesis and sulfate assimilation, enzyme is required for activity of the avirulence rice resistant protein AvrXa21641232-641232?
CTP + adenosine 5-phosphosulfateCDP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Chlamydomonas reinhardtii--641213-641213?
CTP + adenosine 5-phosphosulfateCDP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Pyropia yezoensis--641211-641211?
dATP + adenosine 5-phosphosulfatedADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Chlamydomonas reinhardtii--641213-641213?
MgATP2- + adenosine 5'-phosphosulfateMgADP- + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Thiobacillus denitrificansQ3SM86-701464--?
MgATP2- + adenylyl sulfateMgADP- + 3'-phosphoadenylyl sulfate
show the reaction diagram		Homo sapiensO95340-674838--r
MgATP2- + adenylyl sulfateMgADP- + 3'-phosphoadenylyl sulfate
show the reaction diagram		Homo sapiens--675437--r

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
ATP + adenosine 5'-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiensO43252involved in the synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate, inactivating mutations of PAPSS2 causes skeletal disorders661026--
ATP + adenosine 5'-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiens-synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate660598--
ATP + adenosine 5'-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiensO43252synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate661125--
ATP + adenosine 5'-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiens-synthesis of the important sulfate donor 3'-phosphoadenosine 5'-phosphosulfate from ATP and sulfate, decreased activity leads to defects in skeleton662642--
ATP + adenosine 5'-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Mus musculus-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 processes662177--
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Escherichia coli-ultimate step in biosynthesis of 3'-phosphoadenosine 5'-phosphosulfate, the primary biological sulfuryl donor641216-641216
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Penicillium chrysogenum-second step in pathway of assimilation of inorganic sulfate641207-641207
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Mus musculus-enzyme is involved in sulfation of cartilaginous chondroitin sulfate, reduced enzyme activity causes brachymorphism641234-641234
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Homo sapiensO43252, O95340PAPSS 1 is essential for the sulfonation of mucin like glycoproteins such as GlyCAM-1, CD34 and MAdCAM-1 in high endothelial venules641234--
ATP + adenosine 5-phosphosulfateADP + 3'-phosphoadenosine 5'-phosphosulfate
show the reaction diagram		Xanthomonas oryzae-enzyme is involved in cysteine synthesis and sulfate assimilation, enzyme is required for activity of the avirulence rice resistant protein AvrXa21641232-641232

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Cd2+Escherichia coli-0.42 and 1.1 mM, maximal activation of forward reaction in the presence of 0.42 and 1.1 mM ATP respectively641215
Co2+Penicillium chrysogenum-5 mM, 58% of activation with Mg2+ or Mn2+641207
Co2+Escherichia coli-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 excess641215
Co2+Geobacillus stearothermophilus-164% of activation with Mg2+641221
EDTAHomo sapiens-assay with 0.25 mM EDTA674838, 675437
K+Chlamydomonas reinhardtii-10 mM, 60% stimulation compared to Mg2+641213
K+Homo sapiens-assay with 100 mM KCl674838, 675437
Mg2+Rattus norvegicus-activation641204
Mg2+Riftia pachyptila-activation641206
Mg2+Penicillium duponti, Penicillium duponti K 1014, Penicillium duponti K1014-activation641208
Mg2+Penicillium chrysogenum-activation641207, 641208, 641209, 641210
Mg2+Chlamydomonas reinhardtii-activation641212, 641213
Mg2+Escherichia coli-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 mM641215
Mg2+Saccharomyces cerevisiae-activation641219
Mg2+Geobacillus stearothermophilus--641221
Mg2+Escherichia coli-affinity for adenosine 5'-phosphosulfate decreases by 15fold in the absence of Mg2+641228
Mg2+Homo sapiensO43252in complex with ATP661125
Mg2+Homo sapiens-assay with 2.5 mM MgCl2674838, 675437
Mn2+Penicillium chrysogenum-5 mM yield the same reaction velocity as 5 mM Mg2+, excess inhibits slightly641207
Mn2+Chlamydomonas reinhardtii--641213
Mn2+Escherichia coli-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 excess641215
Mn2+Geobacillus stearothermophilus-274% of activation with Mg2+641221
NaClHomo sapiensO43252increased activity at high salt conditions, 100 mM661125
Zn2+Geobacillus stearothermophilus-309% of activation with Mg2+641221
Mn2+Escherichia coli-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 phosphorylated641228
additional informationPyropia yezoensis, Pyropia yezoensis Ueda-a divalent cation is required for activity641211
additional informationChlamydomonas reinhardtii-not activated by Cu2+ or Na+641213
additional informationEscherichia coli-no monovalent cations required, stereochemistry of divalent metal ion coordination641215
additional informationSaccharomyces cerevisiae-a divalent cation is required for activity641219
additional informationEscherichia coli-enzyme uses multiple metal ions to catalyze phosphoryl group transfer641228

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2'-Phosphoadenosine 5'-phosphosulfatePenicillium chrysogenum--641207 2D-image
2,4,6-Trinitrobenzene sulfonatePenicillium chrysogenum-in the presence or absence of ATP-sulfurylase641209 2D-image
2,4,6-Trinitrobenzene sulfonateEscherichia coli-0.05 mM, complete inhibition641217 2D-image
2,4,6-Trinitrobenzene sulfonateSaccharomyces cerevisiae-0.05 mM, 28% inhibition641217 2D-image
2,6-dichlorophenol indophenolEscherichia coli, Saccharomyces cerevisiae-0.05 mM, complete inhibition641217 2D-image
3'-phosphoadenosine 5'-phosphosulfatePenicillium chrysogenum-product inhibition641207 2D-image
4-AminophenylacetateChlamydomonas reinhardtii-0.008 mM, 50% inhibition641213 2D-image
adenosine 5'-phosphosulfateRattus norvegicus-potent substrate inhibition, ATP reverses641205 2D-image
adenosine 5'-phosphosulfatePenicillium chrysogenum-kinetics641207 2D-image
adenosine 5'-phosphosulfatePyropia yezoensis--641211 2D-image
adenosine 5'-phosphosulfateChlamydomonas reinhardtii-substrate inhibition above 0.03-0.04 mM641212 2D-image
adenosine 5'-phosphosulfateEscherichia coli--641215 2D-image
adenosine 5'-phosphosulfateArabidopsis thalianaQ43295substrate inhibition above 0.01 mM641222 2D-image
adenosine 5'-phosphosulfatePenicillium chrysogenum--641226 2D-image
adenosine 5'-phosphosulfateArabidopsis thalianaO49196uncompetitive inhibition above 0.001 mM641230 2D-image
adenosine 5'-phosphosulfatePenicillium chrysogenum-adenosine 5'-phosphosulfate can bind to E-MgADP forming a catalytically inactive E-MgADP-APS ternary complex641233 2D-image
adenosine 5'-phosphosulfateHomo sapiensO43252substrate inhibition661125 2D-image
adenosine 5'-phosphosulfateHomo sapiensO95340acts as a strong uncompetitive inhibitor of the APS kinase reaction674838 2D-image
adenylyl sulfateHomo sapiensO95340adenylyl sulfate acts as a strong uncompetitive inhibitor of the APS kinase reaction674838 2D-image
ADPEscherichia coli-free form, reverse reaction, weak641215 2D-image
Ammonium sulfatePenicillium chrysogenum-high salt inhibits at low adenosine 5'-phosphosulfate concentrations, but activates at high adenosine 5'-phosphosulfate concentrations641223 2D-image
AMPChlamydomonas reinhardtii--641213 2D-image
ATPPenicillium chrysogenum-inhibition by free ATP, i.e. in excess of total Mg2+641207 2D-image
ATPChlamydomonas reinhardtii-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 mM641212 2D-image
ATPEscherichia coli-free form, weak inhibition; MgATP2-: product inhibition, reverse reaction641215 2D-image
BromosuccinimideChlamydomonas reinhardtii-strong inhibition641213 2D-image
BromosuccinimideEscherichia coli, Saccharomyces cerevisiae-0.05 mM, complete inhibition641217 2D-image
Cd2+Escherichia coli-in excess641215 2D-image
CMPChlamydomonas reinhardtii--641213 2D-image
Co2+Chlamydomonas reinhardtii-2 mM, 63% inhibition641213 2D-image
Co2+Escherichia coli-in excess, activating below641215 2D-image
Cu2+Chlamydomonas reinhardtii-2 mM, 90% inhibition641213 2D-image
dehydroascorbateEscherichia coli, Saccharomyces cerevisiae--641217 2D-image
DiethyldicarbonatePenicillium chrysogenum-in the presence or absence of ATP-sulfurylase641209 2D-image
EDTAEscherichia coli--641215 2D-image
EDTAArabidopsis thalianaO49196complete inhibition641230 2D-image
FADEscherichia coli, Saccharomyces cerevisiae--641217 2D-image
ferricyanideEscherichia coli-0.05 mM, complete inhibition641217 2D-image
GMPChlamydomonas reinhardtii--641213 2D-image
iodoacetamideRattus norvegicus-strong inhibition, dithiothreitol partially protects641205 2D-image
MercuriphenylacetateEscherichia coli, Saccharomyces cerevisiae-0.05 mM, complete inhibition641217 2D-image
N-ethylmaleimideChlamydomonas reinhardtii-0.02 mM, 50% inhibition641213 2D-image
NaClO3Homo sapiens-6.57 mM, 50% inhibition of brain PAPSS activity, 3.26 mM, 50% inhibition of liver PAPSS641229 2D-image
oxidized glutathioneEscherichia coli-thioredoxin reverses inactivation641217 2D-image
p-chloromercuribenzoateChlamydomonas reinhardtii-0.005 mM, 50% inhibition641213 2D-image
reduced glutathionEscherichia coli, Saccharomyces cerevisiae--641217-
UMPChlamydomonas reinhardtii--641213 2D-image
Mn2+Escherichia coli-in excess, activating below641215 2D-image
additional informationEscherichia coli-not inhibited by Mg2+641215-
additional informationEscherichia coli--641217-
additional informationSaccharomyces cerevisiae-not inhibited by ferricyanide641217-
additional informationGeobacillus stearothermophilus-not inhibited by adenosine 5'-phosphosulfate641221-
additional informationSaccharomyces cerevisiae--641221-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
Ammonium sulfatePenicillium chrysogenum-high salt activates at high adenosine 5'-phosphosulfate concentrations but inhibits at low adenosine 5'-phosphosulfate concentrations641223 2D-image
ascorbateEscherichia coli-activation641217 2D-image
dithioerythritolChlamydomonas reinhardtii-2 mM, 200% activation641213 2D-image
dithiothreitolRattus norvegicus-activation641205 2D-image
dithiothreitolChlamydomonas reinhardtii-2 mM, 200% activation; activation641213 2D-image
dithiothreitolEscherichia coli, Saccharomyces cerevisiae-activation641217 2D-image
dithiothreitolArabidopsis thalianaO49196activity declines rapidly in the absence of dithiothreitol641230 2D-image
dithiothreitolHomo sapiensO43252-661125 2D-image
glutathioneEscherichia coli, Saccharomyces cerevisiae-reduced glutathione increases the activity significantly641217 2D-image
High ionic strengthArabidopsis thalianaO49196maximal activity at a high concentration of buffer-salts either alone or plus dithiothreitol and thioredoxin 1 from Escherichia coli641230-
Na2SO3Chlamydomonas reinhardtii-5 mM, 200% activation641213 2D-image
thioredoxinEscherichia coli, Saccharomyces cerevisiae-activation in the presence of dithiothreitol641217 2D-image
thioredoxinArabidopsis thalianaO49196essential for activity641230 2D-image
Thioredoxin fChlamydomonas reinhardtii-from spinach, 0.002 mg, 3fold activation in the presence of saturating concentrations of thiols641214-
L-cysteineEscherichia coli-activation641217 2D-image
additional informationChlamydomonas reinhardtii-not activated by 2-mercaptoethanol641213-
additional informationEscherichia coli-not activated by 2-mercaptoethanol641217-
additional informationSaccharomyces cerevisiae-not activated by 2-mercaptoethanol; not activated by L-cysteine and ascorbate641217-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.003-3'-phosphoadenosine 5'-phosphosulfatePenicillium chrysogenum-pH 8.1, 30°C, wild-type enzyme641223 2D-image
0.008-3'-phosphoadenosine 5'-phosphosulfatePenicillium chrysogenum-pH 8.0, 30°C641207 2D-image
0.039-3'-phosphoadenosine 5'-phosphosulfatePenicillium chrysogenum-pH 8.1, 30°C, S107A mutant enzyme641223 2D-image
0.37-3'-phosphoadenosine 5'-phosphosulfateEscherichia coli-pH 8.0, 25°C641215 2D-image
0.37-3'-phosphoadenosine 5'-phosphosulfateEscherichia coli--641228 2D-image
0.06-adenosine 5'-O-(3-thiotriphosphate)Escherichia coli-pH 8.0641228 2D-image
0.00014-adenosine 5'-phosphosulfateArabidopsis thalianaO49196pH 7.4, 25°C641230 2D-image
0.00025-adenosine 5'-phosphosulfateEscherichia coli-pH 8.0, 25°C641215 2D-image
0.0004-adenosine 5'-phosphosulfateHomo sapiensO43252pH 8.0, 37°C, COS-1 cell-expressed full length PAPS synthase641224 2D-image
0.00045-adenosine 5'-phosphosulfatePyropia yezoensis--641211 2D-image
0.0005-adenosine 5'-phosphosulfateEscherichia coli-pH 8.0641228 2D-image
0.0006-adenosine 5'-phosphosulfateHomo sapiensO43252pH 8.0, 37°C, COS-1 cell-expressed N-terminal fragment641224 2D-image
0.0008-adenosine 5'-phosphosulfatePenicillium chrysogenum-pH 8.1, 30°C641226 2D-image
0.001-adenosine 5'-phosphosulfatePenicillium chrysogenum-pH 8.1, 30°C, wild-type enzyme at 100 mM ammonium sulfate641223 2D-image
0.0014-adenosine 5'-phosphosulfatePenicillium chrysogenum-pH 8.0, 30°C641207 2D-image
0.0014-adenosine 5'-phosphosulfatePenicillium chrysogenum--641210 2D-image
0.002-adenosine 5'-phosphosulfateChlamydomonas reinhardtii-pH 6.8, 30°C641213 2D-image
0.0023-adenosine 5'-phosphosulfateHomo sapiensO43252pH 8.0, 37°C, Escherichia coli-expressed N-terminal fragment641224 2D-image
0.0026-adenosine 5'-phosphosulfateHomo sapiensO43252pH 8.0, 37°C, Escherichia coli-expressed full length PAPS synthase641224 2D-image
0.0036-adenosine 5'-phosphosulfateArabidopsis thalianaQ4329525°C641222 2D-image
0.0042-adenosine 5'-phosphosulfateHomo sapiensO43252pH 8.0, 30°C661125 2D-image
0.006-adenosine 5'-phosphosulfateChlamydomonas reinhardtii-pH 8.0641212 2D-image
0.012-adenosine 5'-phosphosulfatePenicillium chrysogenum-pH 8.1, 30°C, S107A mutant enzyme at 100 mM ammonium sulfate641223 2D-image
0.042-adenosine 5'-phosphosulfateGeobacillus stearothermophilus-pH 8.0, 30°C641221 2D-image
0.002-adenylyl sulfateHomo sapiensO95340value 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 sulfate674838 2D-image
0.0032-adenylyl sulfateHomo sapiensO95340mutant R37A674838 2D-image
0.0037-adenylyl sulfateHomo sapiensO95340mutant R40A674838 2D-image
0.0046-adenylyl sulfateHomo sapiensO95340deletion mutant lacking the first 50 amino acids of the N-terminus, delta50N674838 2D-image
0.007-ATPChlamydomonas reinhardtii-pH 6.8, 30°C641213 2D-image
0.01-ATPEscherichia coli-pH 8.0, 25°C641215 2D-image
0.050.06ATPChlamydomonas reinhardtii-pH 8.0641212 2D-image
0.08-ATPHomo sapiens-pH 8.0, 37°C, PAPSS 1641231 2D-image
0.147-ATPArabidopsis thalianaO49196pH 7.4, 25°C641230 2D-image
0.22-ATPGeobacillus stearothermophilus-pH 8.0, 30°C641221 2D-image
0.23-ATPHomo sapiensO43252pH 8.0, 37°C, COS-1 cell-expressed N-terminal fragment641224 2D-image
0.26-ATPHomo sapiensO43252pH 8.0, 37°C, E. coli expressed N-terminal fragment641224 2D-image
0.36-ATPHomo sapiens-pH 8.0, 37°C, PAPSS 2b641231 2D-image
0.38-ATPHomo sapiens-pH 8.0, 37°C, PAPSS 2a641231 2D-image
0.45-ATPHomo sapiensO43252pH 8.0, 37°C, E. coli-expressed full length PAPS synthase641224 2D-image
1.5-ATPPenicillium chrysogenum-pH 8.0, 30°C641207 2D-image
1.9-ATPArabidopsis thalianaQ4329525°C641222 2D-image
0.13-MgADP-Escherichia coli-pH 8.0, 25°C641215 2D-image
0.13-MgADP-Escherichia coli--641228 2D-image
0.14-MgATP2-Homo sapiensO43252pH 8.0, 30°C661125 2D-image
0.8-MgATP2-Penicillium chrysogenum-pH 8.1, 30°C, wild-type enzyme at 100 mM ammonium sulfate641223 2D-image
0.8-MgATP2-Penicillium chrysogenum-pH 8.1, 30°C641226 2D-image
2.4-MgATP2-Penicillium chrysogenum-pH 8.1, 30°C, S107A mutant enzyme641223 2D-image
additional information-additional informationRattus norvegicus-kinetic study641205-
additional information-additional informationPenicillium chrysogenum-kinetic study641207-
additional information-additional informationEscherichia coli-kinetic study641215-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.09-adenosine 5'-O-(3-thiotriphosphate)Escherichia coli-pH 8.0641228 2D-image
50-adenosine 5-phosphosulfateEscherichia coli-pH 8.0, 30°C641215 2D-image
0.17-adenylyl sulfateHomo sapiensO95340mutant R40A674838 2D-image
0.2-adenylyl sulfateHomo sapiensO95340deletion mutant lacking the first 50 amino acids of the N-terminus, delta50N674838 2D-image
0.207-adenylyl sulfateHomo sapiensO95340mutant R37A674838 2D-image
0.315-adenylyl sulfateHomo sapiensO95340deletion mutant lacking the first 34 amino acids of the N-terminus, delta34N674838 2D-image
0.364-adenylyl sulfateHomo sapiensO95340wildtype adenylyl sulfate674838 2D-image
1.7-ATPHomo sapiens-pH 8.0, 37°C, PAPSS 1641231 2D-image
2.3-ATPHomo sapiens-pH 8.0, 37°C, PAPSS 2a641231 2D-image
4.4-ATPHomo sapiens-pH 8.0, 37°C, PAPSS 2b641231 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0004-adenosine 5'-phosphosulfateEscherichia coli-pH 8.0, 25°C641215 2D-image
0.0045-adenosine 5'-phosphosulfateArabidopsis thalianaO49196pH 7.4, 25°C641230 2D-image
0.013-adenosine 5'-phosphosulfatePenicillium chrysogenum, Penicillium chrysogenum 31B, Penicillium chrysogenum AS-P-78, Penicillium chrysogenum CCF1269, Penicillium chrysogenum DS12975, Penicillium chrysogenum DS17690, Penicillium chrysogenum LN33, Penicillium chrysogenum NCAIM 00237, Penicillium chrysogenum NCIM-722, Penicillium chrysogenum NRRL1951, Penicillium chrysogenum Q-176, Penicillium chrysogenum Westling, Penicillium chrysogenum Wis. 54-1255, Penicillium chrysogenum WIS 54-1255, Penicillium chrysogenum yielding-pH 8.1, 30°C641226 2D-image
0.017-adenylyl sulfateHomo sapiensO95340wild type adenylyl sulfate674838 2D-image
0.029-adenylyl sulfateHomo sapiensO95340deletion mutant lacking the first 34 amino acids of the N-terminus, delta34N674838 2D-image
0.048-adenosine 5'-phosphosulfateHomo sapiensO43252pH 8.0, 30°C661125 2D-image
additional information-adenylyl sulfateHomo sapiensO95340no 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 R40A674838 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.00016-Mus musculus-recombinant enzyme641225
0.000298-Mus musculus-wild type activity, specific activities given for all mutant enzymes662177
0.0020.006Chlamydomonas reinhardtii--641212
0.12-Homo sapiensO43252pH 8.0. 30°C661125
0.136-Chlamydomonas reinhardtii--641213
0.208-Saccharomyces cerevisiae--641219
0.614-Escherichia coli, Saccharomyces cerevisiae--641217
0.843-Escherichia coli, Saccharomyces cerevisiae--641217
1.7-Geobacillus stearothermophilus--641221
24.4-Penicillium chrysogenum--641209
24.7-Penicillium chrysogenum--641207
52.5-Rattus norvegicus--641205
153-Escherichia coli--641215

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
6-Chlamydomonas reinhardtii--641213
6.57.5Chlamydomonas reinhardtii-in MES-Tricine-HEPES buffer641213
6.87Escherichia coli, Saccharomyces cerevisiae--641217
6.87Saccharomyces cerevisiae--641221
6.8-Chlamydomonas reinhardtii-in imidazole buffer641213
78Geobacillus stearothermophilus--641221
7-Pyropia yezoensis--641211
7.5-Homo sapiensO95340assay at674838
7.5-Homo sapiens-assay at675437
8-Penicillium chrysogenum-90% of maximal activity at pH 7.5 and pH 8.5641207
8-Escherichia coli, Saccharomyces cerevisiae--641217
8.5-Rattus norvegicus--641205
additional information-Chlamydomonas reinhardtii-pI: 6.2641213
additional information-Escherichia coli--641215
additional information-Escherichia coli, Saccharomyces cerevisiae-pI: 5.5; pI: 7.4641217

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.58.5Chlamydomonas reinhardtii-approx. 80% of maximal activity at pH 5.5, approx. half-maximal activity at pH 8.5641213
68Chlamydomonas reinhardtii-approx. 80% of maximal activity at pH 6.0, approx. 65% of maximal activity at pH 8.0, imidazole buffer641213
68Escherichia coli, Saccharomyces cerevisiae-continuous increase of activity from pH 6.0 to 8.0641217
68.5Chlamydomonas reinhardtii-approx. 70% of maximal activity at pH 6.0, approx. 75% of maximal activity at pH 8.5, MES-Tricine-HEPES buffer641213
6.88Escherichia coli, Saccharomyces cerevisiae-maximal activity at pH 6.8, approx. half-maximal activity at pH 8.0641217
7.59Rattus norvegicus-approx. half-maximal activity at pH 7.5, approx. 80% of maximal activity at pH 9.0641205

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
25-Escherichia coli-assay at641215
30-Riftia pachyptila-assay at641206
30-Penicillium chrysogenum-assay at641207, 641209
30-Chlamydomonas reinhardtii-assay at641213, 641214
37-Homo sapiensO95340assay at674838
37-Homo sapiens-assay at675437

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
adrenal glandHomo sapiens-PAPSS 1, 2a and 2b641231Manually annotated by BRENDA team
adultUrechis caupoQ27128PAPS synthetase mRNA641220Manually annotated by BRENDA team
bone marrowHomo sapiens-PAPSS 1641231Manually annotated by BRENDA team
brainHomo sapiens-major isoform PAPSS 2641229Manually annotated by BRENDA team
brainHomo sapiens-PAPSS 1641231Manually annotated by BRENDA team
brainHomo sapiensO43252, O95340; high expression of PAPSS 1641234Manually annotated by BRENDA team
brainHomo sapiens--661026, 661125Manually annotated by BRENDA team
cartilageCavia porcellusO54820PAPSS 1 is the predominant isoform in adults641231Manually annotated by BRENDA team
cartilageHomo sapiens-PAPSS 1 is the predominant isoform in adults641231Manually annotated by BRENDA team
cartilageHomo sapiensO43252, O95340; high expression of PAPSS 2641234Manually annotated by BRENDA team
colonHomo sapiens-PAPSS 1, 2a and 2b641231Manually annotated by BRENDA team
embryoUrechis caupoQ27128PAPS synthetase mRNA641220Manually annotated by BRENDA team
kidneyHomo sapiens-PAPSS 1, 2a and 2b641231Manually annotated by BRENDA team
leafArabidopsis thalianaQ43295APS kinase mRNA641222Manually annotated by BRENDA team
liverRattus norvegicus--641204, 641205Manually annotated by BRENDA team
liverHomo sapiens-major isoform PAPSS1641229Manually annotated by BRENDA team
liverHomo sapiens-PAPSS 1, 2a and 2b641231Manually annotated by BRENDA team
liverHomo sapiensO43252, O95340; high expression of PAPSS 2; predominantly PAPS2641234Manually annotated by BRENDA team
lungHomo sapiens-PAPSS 1, 2a and 2b641231Manually annotated by BRENDA team
myceliumPenicillium duponti, Penicillium duponti K 1014, Penicillium duponti K1014--641208Manually annotated by BRENDA team
myceliumPenicillium chrysogenum--641207, 641208, 641209, 641210Manually annotated by BRENDA team
oocyteUrechis caupoQ27128PAPS synthetase mRNA641220Manually annotated by BRENDA team
ovaryHomo sapiens-PAPSS 1, 2a and 2b641231Manually annotated by BRENDA team
placentaHomo sapiens-PAPSS 1, 2a and 2b641231Manually annotated by BRENDA team
prostateHomo sapiens-PAPSS 1641231Manually annotated by BRENDA team
rootArabidopsis thalianaQ43295APS kinase mRNA641222Manually annotated by BRENDA team
skinHomo sapiensO43252, O95340PAPSS 1641234Manually annotated by BRENDA team
small intestineHomo sapiens-PAPSS 1, 2a and 2b641231Manually annotated by BRENDA team
spleenHomo sapiens-PAPSS 1, 2a and 2b641231Manually annotated by BRENDA team
stomachHomo sapiens-PAPSS 1641231Manually annotated by BRENDA team
thallusPyropia yezoensis--641211Manually annotated by BRENDA team
thymusHomo sapiens-PAPSS 1641231Manually annotated by BRENDA team
thyroid glandHomo sapiens-PAPSS 1, 2a and 2b641231Manually annotated by BRENDA team
trophosome tissueRiftia pachyptila--641206Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
chloroplastArabidopsis thalianaQ43295localization is suggested by an in vitro chloroplast import assay9507641222Manually annotated by BRENDA team
chloroplastArabidopsis thalianaO49196-9507641230Manually annotated by BRENDA team
cytosolRattus norvegicus--5829641205Manually annotated by BRENDA team
cytosolEscherichia coli, Saccharomyces cerevisiae--5829641217Manually annotated by BRENDA team
cytosolHomo sapiens--5829641229Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
2yvu, downloadSCOP (2yvu)CATH (2yvu)Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
2gks, downloadSCOP (2gks)CATH (2gks)Aquifex aeolicus (strain VF5)
3uie, downloadSCOP (3uie)CATH (3uie)Arabidopsis thaliana
4fxp, downloadSCOP (4fxp)CATH (4fxp)Arabidopsis thaliana
1x6v, downloadSCOP (1x6v)CATH (1x6v)Homo sapiens
1xjq, downloadSCOP (1xjq)CATH (1xjq)Homo sapiens
1xnj, downloadSCOP (1xnj)CATH (1xnj)Homo sapiens
2ax4, downloadSCOP (2ax4)CATH (2ax4)Homo sapiens
2ofw, downloadSCOP (2ofw)CATH (2ofw)Homo sapiens
2ofx, downloadSCOP (2ofx)CATH (2ofx)Homo sapiens
2pey, downloadSCOP (2pey)CATH (2pey)Homo sapiens
1d6j, downloadSCOP (1d6j)CATH (1d6j)Penicillium chrysogenum
1m7g, downloadSCOP (1m7g)CATH (1m7g)Penicillium chrysogenum
1m7h, downloadSCOP (1m7h)CATH (1m7h)Penicillium chrysogenum
3cr7, downloadSCOP (3cr7)CATH (3cr7)Penicillium chrysogenum
3cr8, downloadSCOP (3cr8)CATH (3cr8)Thiobacillus denitrificans (strain ATCC 25259)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
29500-Saccharomyces cerevisiae-in the presence of dithiothreitol, gel filtration641217
4000045000Saccharomyces cerevisiae-gel filtration641217
40000-Escherichia coli-phosphorylated enzyme, gel filtration641215
4950052000Saccharomyces cerevisiae-gel filtration641217
50000-Geobacillus stearothermophilus-gel filtration641221
57000-Penicillium chrysogenum-gel filtration at 22°C641208
57000-Penicillium duponti, Penicillium duponti K 1014, Penicillium duponti K1014-gel filtration at 22°C or 46°C641208
57000-Penicillium chrysogenum-gel filtration at 22°C641209
58000-Rattus norvegicus-gel filtration641205
5900060000Penicillium chrysogenum-gel filtration641207
61000-Pyropia yezoensis-gel filtration641211
80000-Escherichia coli-dephosphorylated enzyme, gel filtration641215
8500090000Escherichia coli-gel filtration641217
150000-Homo sapiensO43252gel filtration661125
162000-Homo sapiens-gel filtration660598

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Chlamydomonas reinhardtii-x * 44000, SDS-PAGE641213
?Escherichia coli-x * 22321, deduced from DNA sequence of cysC coding region641216
?Urechis caupoQ27128x * 57000, in vitro translation product, SDS-PAGE; x * 68000, deduced from nucleotide sequence641220
?Arabidopsis thalianaQ43295x * 29786, deduced from nucleotide sequence641222
?Arabidopsis thalianaO49196x * 31977, deduced from nucleotide sequence641230
dimerPenicillium chrysogenum-2 * 30000, SDS-PAGE641207
dimerPenicillium chrysogenum-2 * 33000, gel filtration at 46°C, the enzyme dissociates into two inactive monomers by heating above 42°C641208, 641209
dimerPyropia yezoensis, Pyropia yezoensis Ueda-2 * 31000, dissociation641211
dimerEscherichia coli-2 * 21000, phosphorylated enzyme, SDS-PAGE; native protein undergoes dimer-tetramer interconversions depending on experimental conditions and phosphorylation state641215
dimerEscherichia coli-2 * 40000-45000, dithiothreitol-treated enzyme, SDS-PAGE641217
dimerSaccharomyces cerevisiae-2 * 28000-29500, dithiothreitol-treated enzyme, SDS-PAGE641217
dimerGeobacillus stearothermophilus-2 * 26000, SDS-PAGE641221
dimerSaccharomyces cerevisiae--641221
dimerPenicillium chrysogenum-2 * 23670641233
dimerHomo sapiens-2 * 716000, MALDI-TOF mass spectrometry, native mass by gel filtration660598
dimerHomo sapiensO432522 * 71000661125
dimerHomo sapiens-2 * 71000, asymmetric complex, only one monomer is occupied by a bound ATP or ADP, crystal structure analysis662642
homohexamerThiobacillus denitrificansQ3SM866 * 60500, calculated, crystall structure analysis701464
tetramerRattus norvegicus-4 * 14500, SDS-PAGE641205
tetramerEscherichia coli-4 * 21000, dephosphorylated enzyme, SDS-PAGE; native protein undergoes dimer-tetramer interconversions depending on experimental conditions and phosphorylation state641215
tetramerEscherichia coli-monomers and dimers are catalytically active641217

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
side-chain modificationEscherichia coli-enzyme is phosphorylated upon incubation with ATP, phosphorylation site is identified as Ser109, phosphorylated enzyme is kinetically competent641216

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
crystals are grown by hanging drop vapor diffusion at 25°C in 40% (v/v) ethanol, 1.0% (w/v) PEG 6000, 50 mM sodium acetate and 5 mM MgATPAquifex aeolicusO67174675422
; crystals are grown at room temperature using hanging drops containing equal volumes of protein and reservoir solutionHomo sapiensO95340674838
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 dimersHomo sapiens-675437
hanging drop vapor diffusion methodHomo sapiens-660598, 662642
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 APenicillium chrysogenum-641233
hanging-drop vapor diffusion methodThiobacillus denitrificansQ3SM86701464

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
6-Penicillium chrysogenum-below, reversible inactivation at 30°C, reactivation rate increases with increasing pH641209
7-Penicillium chrysogenum-reversible inactivation at 42°C641209

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
25-Geobacillus stearothermophilus-no loss of activity after 7 d at room temperatures641221
25-Saccharomyces cerevisiae-70% loss of activity after 7 d at room temperature641221
35-Penicillium chrysogenum-inactivation above, reversible by cooling to 0-30°C641208
36-Penicillium chrysogenum-equilibrium between active and inactive enzyme form641209
37-Mus musculus-no loss of activity after 2 h, recombinant enzyme641225
40-Penicillium chrysogenum-reversible inactivation above by subunit dissociation, kinetics, MgATP2- or MgADP- stimulate reactivation641209
43-Penicillium chrysogenum-reversible inactivation, t1/2: 1 min641209
50-Penicillium chrysogenum-rapid loss of activity, approx. 80% of activity is recovered upon cooling at 0°C, presence of MgATP2- accelerates the recovery process641207
50-Penicillium chrysogenum-1 min, 80% reversible inactivation641209
60100Penicillium chrysogenum-1 min, 85% reversible inactivation641209
60-Saccharomyces cerevisiae-complete inactivation after 15 min641221
70-Geobacillus stearothermophilus-no significant loss of activity after 15 min641221
80-Penicillium chrysogenum-irreversible inactivation, t1/2: 47 min, pH 8, 0.023 mg protein/ml641209

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
recombinant enzyme is rapidly inactivated by dialysis, dilution or freezing even in the presence of glycerolArabidopsis thalianaO49196641230
more stable in ampholyte polybuffer 74 than in Tris or imidazole buffersChlamydomonas reinhardtii-641213
slow freezing can cause loss of activityChlamydomonas reinhardtii-641213
rapid loss of activity in dilute solutionsEscherichia coli-641217
slow inactivation in dilute solutions, even at low temperaturesPenicillium chrysogenum-641209
stable to ammonium sulfate precipitationRattus norvegicus-641205
rapid loss of activity in dilute solutionsSaccharomyces cerevisiae-641217

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-70°C, recombinant APS kinase fusion protein, 1 year, no loss of activityArabidopsis thalianaQ43295641222
-20°C, stable to prolonged storageChlamydomonas reinhardtii-641213

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Aquifex aeolicusO67174675422
ammonium sulfate, Sephacryl S-200, partially purifiedChlamydomonas reinhardtii-641212
ammonium sulfate, Sephacryl S-300, chromatofocusing, 2'5'-ADP-agaroseChlamydomonas reinhardtii-641213
-Escherichia coli-641216, 641228
ammonium sulfate, Giogel P2, Blue Sepharose, Sephacryl S-300, PBE 94Escherichia coli-641217
ammonium sulfate, phenyl-Sepharose, Q-Sepharose, Sephacryl S-300, hydroxylapatite, pentyl- agarose, aminohexyl agarose, ATP-agaroseEscherichia coli-641215
DEAE-Sepharose, Matrex gel blue A, phenyl CellofineGeobacillus stearothermophilus-641221
-Homo sapiens-662642
; protein solutions are applied on Blue-Sepharose columns and further purified by ion-exchange chromatographyHomo sapiensO95340674838
Ni2+-column, recombinant enzymeHomo sapiens-641227
protein solution is loaded on a Glutathione-Sepharose Fast Flow column and further purified by gel-filtration chromatography using Superdex 200Homo sapiens-675437
recombinant enzyme using His-tagHomo sapiensO43252661125
recombinant protein using His-tagHomo sapiens-660598
recombinant protein using His-tagMus musculus-662177
-Penicillium chrysogenum-641208
ammonium sulfate, Affi-gel blue, Matrix-gel green, Agarose APenicillium chrysogenum-641207
partialPenicillium duponti-641208
ammonium sulfate, affinity chromatography, gel filtration, ion-exchange chromatographyPyropia yezoensis, Pyropia yezoensis Ueda-641211
alumina C-gamma gel, ammonium sulfate, hydroxyapatite, Cellex CM, unstable upon column chromatographyRattus norvegicus-641205
ammonium sulfate, Blue Sepharose, Sephacryl S-200, PBE 94, Red Sepharose, phenyl-sepharoseSaccharomyces cerevisiae-641217
partialSaccharomyces cerevisiae-641219
immobilized metal ion affinity chromatography (Ni2+)Thiobacillus denitrificansQ3SM86701464

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression in Escherichia coliArabidopsis thalianaO49196641230
expression in Escherichia coli as fusion protein with glutathione-S-transferase or maltose binding proteinArabidopsis thalianaQ43295641222
structural gene cysCEscherichia coli-641216
-Homo sapiens-641227, 662642
APS kinase domain (amino acids 25-227) of the PAPSS1 coding region are expressed as a GST-fusion protein in Escherichia coliHomo sapiensO95340674838
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)Homo sapiens-660598, 661125
expressed in COS-1 and HEK293 cellsHomo sapiensO43252661026
expression of full-length PAPS synthase and 1-268 N-terminal fragment in COS-1 cells and Escherichia coliHomo sapiensO43252641224
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-21Homo sapiens-675437
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)Mus musculus-662177
expresssion in Escherichia coliMus musculus-641225
expression of wild-type and S107A mutant enzyme in Escherichia coliPenicillium chrysogenum-641223
expressed in Escherichia coli BL21-DE3Phytophthora infestans T30-4B0FWC4705207
expressed in Escherichia coli BL21(DE3)Thiobacillus denitrificansQ3SM86701464
in vitro transcription/translationUrechis caupoQ27128641220
expression in Escherichia coli cysD-mutantXanthomonas oryzae, Xanthomonas oryzae IAM 1657, Xanthomonas oryzae No.5-641232

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
S182CArabidopsis thalianaO49196similar catalytic activity as wild-type641230
S182FArabidopsis thalianaO49196similar catalytic activity as wild-type641230
delta34NHomo sapiensO95340deletion mutant lacking the first 34 N-terminal residues from APS kinase domain results in an enzyme with similar kinetic behaviour to the full-length domain674838
delta50NHomo sapiensO95340deletion 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 dimer674838
E531QHomo sapiensO43252identified as naturally occurring mutation, E531Q found in a single sample of an African-American’s subject, almost no effect of mutations when expressed in COS-1 or HEK293 cells661026
G427AHomo sapiens-slightly lower APS kinase activity than wild-type641227
G427AHomo sapiensO43252, O95340-641234
G427A/H428AHomo sapiens-no APS kinase activity641227
H425AHomo sapiens-no APS kinase activity641227
H425AHomo sapiensO43252, O95340-641234
H428AHomo sapiens-no APS kinase activity641227
N426KHomo sapiens-2fold higher APS kinase activity than wild-type641227
N426KHomo sapiensO43252, O95340-641234
R333CHomo sapiensO43252identified as naturally occurring mutation, R333C found exclusively in Caucasian-American’s DNA, almost no effect of mutations when expressed in COS-1 or HEK293 cells661026
R37AHomo sapiensO95340mutant clone shows no substrate inhibition by adenylyl sulfate, mutant is kinetically indistinguishable from deletion mutant delta50N lacking the first N-terminal residues674838
R40AHomo sapiensO95340mutant clone shows no substrate inhibition by adenylyl sulfate, mutant is kinetically indistinguishable from deletion mutant delta50N lacking the first N-terminal residues674838
D87AMus musculus-almost complete loss of activity662177
D87EMus musculus-80% loss of activity662177
D87RMus musculus-almost complete loss of activity662177
D89AMus musculus-almost complete loss of activity662177
D89EMus musculus-75% loss of activity662177
D89RMus musculus-almost complete loss of activity662177
DN89NDMus musculus-switch mutant, almost complete loss of activity662177
G79RMus musculus-reduced APS kinase activity641234
G88AMus musculus-less than 30% loss of kinase activity662177
G88DMus musculus-almost complete loss of activity662177
G88RMus musculus-almost complete loss of activity662177
K97AMus musculus-no effect on activity662177
LD86DLMus musculus-switch mutant, almost complete loss of activity662177
N90AMus musculus-30% loss of kinase activity662177
N90QMus musculus-30% loss of kinase activity662177
R92AMus musculus-complete loss of kinase activity662177
S104APenicillium chrysogenum-similar properties as wild-type641223
S107APenicillium chrysogenum-similar properties as wild-type enzyme641223
S107CPenicillium chrysogenum-similar properties as wild-type, suggesting that S107 is not essential for activity but may be located in the substrate binding pocket641223
S97APenicillium chrysogenum-similar properties as wild-type641223
S99APenicillium chrysogenum-similar properties as wild-type641223
T103APenicillium chrysogenum-similar properties as wild-type641223
Y109FPenicillium chrysogenum-similar properties as wild-type, velocity curve is shifted to the far right641223
H428AHomo sapiensO43252, O95340-641234
additional informationHomo sapiensO95340generation 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 PAPSS1674838

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
Anovulation- PubMed
Carcinoma- PubMed,  PubMed
Carcinoma, Hepatocellular- PubMed
Chondrosarcoma- PubMed,  PubMed,  PubMed,  PubMed,  PubMed
Dwarfism- PubMed
Hepatitis B- PubMed
Neoplasms- PubMed,  PubMed
Tuberculosis- PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
641204Yu, 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 oxyanionsArch. Biochem. Biophys.269156-1741989Rattus norvegicus PubMed
641205Hommes, F.A.; Moss, L.; Touchton, J.Purification and some properties of liver adenylylsulfate kinaseBiochim. Biophys. Acta924270-2751987Rattus norvegicus PubMed
641206Renosto, 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.29066-781991Riftia pachyptila PubMed
641207Renosto, F.; Seubert, P.A.; Segel, I.H.Adenosine 5-phosphosulfate kinase from Penicillium chrysogenum. Purification and kinetic characterizationJ. Biol. Chem.2592113-21231984Penicillium chrysogenum PubMed
641208Renosto, 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)J. Bacteriol.164674-6831985Penicillium chrysogenum, Penicillium duponti PubMed
641209Renosto, F.; Seubert, P.A.; Knudson, P.; Segel, I.H.APS kinase from Penicillium chrysogenum. Dissociation and reassociation of subunits as the basis of the reversible heat inactivationJ. Biol. Chem.2601535-15441985Penicillium chrysogenum PubMed
641210Renosto, F.; Martin, R.L.; Segel, I.H.Sulfate-activating enzymes of Penicillium chrysogenum. The ATP sulfurylase.adenosine 5-phosphosulfate complex does not serve as a substrate for adenosine 5-phosphosulfate kinaseJ. Biol. Chem.2649433-94371989Penicillium chrysogenum PubMed
641211Kanno, N.; Sato, M.; Sato, Y.Purification and properties of adenosine-5'-phosphosulfate kinase from the marine red macroalga Porphyra yezoensis UedaBot. Mar.33369-3741990Pyropia yezoensis-
641212Schwenn, J.D.; Jender, H.G.A kinetic investigation of the APS-kinase from chlamydomonas reinhardii CW 15Phytochemistry20601-6041981Chlamydomonas reinhardtii-
641213Schwenn, J.D.; Jender, H.G.Purification and properties of the ATP:adenylylsulfate 3'-phosphotransferase from chlamydomonas reinhardiiArch. Microbiol.1389-141984Chlamydomonas reinhardtii-
641214Schwenn, 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 15FEBS Lett.17076-801984Chlamydomonas reinhardtii-
641215Satishchandran, C.; Markham, G.D.Adenosine-5-phosphosulfate kinase from Escherichia coli K12. Purification, characterization, and identification of a phosphorylated enzyme intermediateJ. Biol. Chem.26415012-150211989Escherichia coli PubMed
641216Satishchandran, C.; Hickman, Y.N.; Markham, G.D.Characterization of the phosphorylated enzyme intermediate formed in the adenosine 5-phosphosulfate kinase reactionBiochemistry3111684-116881992Escherichia coli PubMed
641217Schriek, U.; Schwenn, J.D.Properties of the purified APS-kinase from Escherichia coli and Saccharomyces cerevisiaeArch. Microbiol.14532-381986Escherichia coli, Escherichia coli AN1460, Saccharomyces cerevisiae PubMed
641218Bandurski, R.S.; Wilson, L.G.; Squires, C.L.J. Am. Chem. Soc.786408-64091956Saccharomyces cerevisiae-
641219Robbins, P.W.; Lipmann, F.J. Am. Chem. Soc.786409-64101956Saccharomyces cerevisiae-
641220Rosenthal, E.; Leustak, T.A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activitiesGene165243-2481995Rattus norvegicus, Urechis caupo (Q27128), Urechis caupo PubMed
641221Onda, M.; Hayashi, M.; Suiko, M.; Liu, M.C.; Nakajima, H.Purification and characterization of adenosine 5'-phosphosulfate kinase from the thermophilic bacterium Bacillus stearothermophilusBiosci. Biotechnol. Biochem.60134-1361996Geobacillus stearothermophilus, Saccharomyces cerevisiae-
641222Lee, S.; Leustek, T.APS kinase from Arabidopsis thaliana: genomic organization, expression, and kinetic analysis of the recombinant enzymeBiochem. Biophys. Res. Commun.247171-1751998Arabidopsis thaliana, Arabidopsis thaliana (Q43295) PubMed
641223MacRae, 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 residuesJ. Biol. Chem.27328583-285891998Escherichia coli (P23846), Penicillium chrysogenum, Penicillium chrysogenum (Q12657) PubMed
641224Venkatachalam, K.V.; Akita, H.; Strott, C.A.Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domainsJ. Biol. Chem.27319311-193201998Homo sapiens, Homo sapiens (O43252) PubMed
641225Deyrup, 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 kinaseJ. Biol. Chem.27410751-107571999Mus musculus PubMed
641226MacRae, I.J.; Segel, I.H.Adenosine 5'-phosphosulfate (APS) kinase: diagnosing the mechanism of substrate inhibitionArch. Biochem. Biophys.361277-2821999Penicillium chrysogenum PubMed
641227Venkatachalam, 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 synthaseJ. Biol. Chem.2742601-26041999Homo sapiens, Homo sapiens (O43252) PubMed
641228Satishchandran, C.; Markham, G.D.Mechanistic studies of Escherichia coli adenosine-5'-phosphosulfate kinaseArch. Biochem. Biophys.378210-2152000Escherichia coli PubMed
641229Xu, 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 localizationBiochem. Biophys. Res. Commun.268437-4442000Homo sapiens PubMed
641230Lillig, C.H.; Schiffmann, S.; Berndt, C.; Berken, A.; Tischka, R.; Schwenn, J.D.Molecular and catalytic properties of Arabidopsis thaliana adenylyl sulfate (APS)-kinaseArch. Biochem. Biophys.392303-3102001Arabidopsis thaliana, Arabidopsis thaliana (O49196) PubMed
641231Fuda, H.; Shimizu, C.; Lee, Y.C.; Akita, H.; Strott, C.A.Characterization and expression of human bifunctional 3'-phosphoadenosine 5'-phosphosulphate synthase isoformsBiochem. J.365497-5042002Cavia porcellus (O54820), Homo sapiens PubMed
641232Shen, 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 activityMol. Microbiol.4437-482002Sinorhizobium meliloti, Xanthomonas oryzae PubMed
641233Lansdon, E.B.; Segel, I.H.; Fisher, A.J.Ligand-induced structural changes in adenosine 5'-phosphosulfate kinase from Penicillium chrysogenumBiochemistry4113672-136802002Penicillium chrysogenum, Penicillium chrysogenum (Q12657) PubMed
641234Venkatachalam, K.V.Human 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase: biochemistry, molecular biology and genetic deficiencyIUBMB Life551-112003Caenorhabditis elegans, Cavia porcellus (O54820), Danio rerio (Q802U9), Drosophila melanogaster (Q9VW48), Homo sapiens, Homo sapiens (O43252), Homo sapiens (O95340), Mus musculus, Takifugu rubripes (Q90XY2), Urechis caupo (Q27128) PubMed
660598Harjes, S.; Scheidig, A.; Bayer, P.Expression, purification and crystallization of human 3'-phosphoadenosine-5'-phosphosulfate synthetase 1Acta Crystallogr. Sect. D60350-3522004Homo sapiens PubMed
661026Xu, 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 genomicsBiochem. Pharmacol.651787-17962003Homo sapiens, Homo sapiens (O43252) PubMed
661125Lansdon, 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 domainsBiochemistry434356-43652004Homo sapiens, Homo sapiens (O43252) PubMed
662177Singh, B.; Schwartz, N.B.Identification and functional characterization of the novel BM-motif in the murine phosphoadenosine phosphosulfate (PAPS) synthetaseJ. Biol. Chem.27871-752003Mus musculus PubMed
662642Harjes, S.; Bayer, P.; Scheidig, A.J.The crystal structure of human PAPS synthetase 1 reveals asymmetry in substrate bindingJ. Mol. Biol.347623-6352005Homo sapiens, Homo sapiens (O43252) PubMed
674838Sekulic, N.; Konrad, M.; Lavie, A.Structural mechanism for substrate inhibition of the adenosine 5-phosphosulfate kinase domain of human 3-phosphoadenosine 5-phosphosulfate synthetase 1 and its ramifications for enzyme regulationJ. Biol. Chem.28222112-221212007Homo sapiens, Homo sapiens (O43252), Homo sapiens (O95340) PubMed
675422Yu, Z.; Lansdon, E.B.; Segel, I.H.; Fisher, A.J.Crystal structure of the bifunctional ATP sulfurylase-APS kinase from the chemolithotrophic thermophile Aquifex aeolicusJ. Mol. Biol.365732-7432007Aquifex aeolicus, Aquifex aeolicus (O67174) PubMed
675437Sekulic, N.; Dietrich, K.; Paarmann, I.; Ort, S.; Konrad, M.; Lavie, A.Elucidation of the active conformation of the APS-kinase domain of human PAPS synthetase 1J. Mol. Biol.367488-5002007Homo sapiens PubMed
701464Gay, S.C.; Segel, I.H.; Fisher, A.J.Structure of the two-domain hexameric APS kinase from Thiobacillus denitrificans: structural basis for the absence of ATP sulfurylase activityActa Crystallogr. Sect. D651021-10312009Thiobacillus denitrificans (Q3SM86), Thiobacillus denitrificans PubMed
705207Bradley, M.E.; Rest, J.S.; Li, W.H.; Schwartz, N.B.Sulfate activation enzymes: phylogeny and association with pyrophosphataseJ. Mol. Evol.681-132009Phytophthora infestans T30-4 (B0FWC4) PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.7.1.25)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)