Any feedback?
Information on EC 2.7.1.25 - adenylyl-sulfate kinase and Organism(s) Penicillium chrysogenum and UniProt Accession Q12657
for references in articles please use BRENDA:EC2.7.1.25Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.1.25 adenylyl-sulfate kinaseIUBMB Comments
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).
Specify your search results
Word Map
- 2.7.1.25
- chrysogenum
-
sulfate-activating
- 3'-phosphate
-
sulphurylase
-
2.7.7.4
-
brachymorphic
- cysd
-
molybdolysis
-
spondyloepimetaphyseal
-
atp-sulphurylase
The taxonomic range for the selected organisms is: Penicillium chrysogenum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
aps kinase, papss1, aps-kinase, paps synthetase, papss, paps synthase, adenosine-5'-phosphosulfate kinase, mxan3487, adenosine 5'-phosphosulfate kinase, adenylylsulfate kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-phosphoadenosine-5'-phosphosulfate synthetase
-
-
-
-
5'-phosphoadenosine sulfate kinase
-
-
-
-
adenosine 5'-phosphosulfate kinase
-
-
-
-
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
-
-
-
-
ATP adenosine-5'-phosphosulfate 3'-phosphotransferase
-
-
-
-
kinase, adenylylsulfate (phosphorylating)
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
enzyme follows a compulsory ordered mechanism in which MgATP2- binds before APS, and PAPS leaves before MgADP-
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
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).
CAS REGISTRY NUMBER
COMMENTARY
9012-38-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + adenylyl sulfate
ADP + 3'-phosphoadenylyl sulfate
-
-
-
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
no substrate-chanelling of adenosine 5'-phosphosulfate between ATP-sulfurylase, EC 2.7.7.4, and APS-kinase, i.e. ATP-sulfurylase-APS-complex is no substrate for the kinase
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
second step in pathway of assimilation of inorganic sulfate
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
-
second step in pathway of assimilation of inorganic sulfate
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
-
5 mM yield the same reaction velocity as 5 mM Mg2+, excess inhibits slightly
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 5'-phosphosulfate
adenosine 5'-phosphosulfate can bind to E-MgADP forming a catalytically inactive E-MgADP-APS ternary complex
ammonium sulfate
high salt inhibits at low adenosine 5'-phosphosulfate concentrations, but activates at high adenosine 5'-phosphosulfate concentrations
2,4,6-Trinitrobenzene sulfonate
-
in the presence or absence of ATP-sulfurylase
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ammonium sulfate
high salt activates at high adenosine 5'-phosphosulfate concentrations but inhibits at low adenosine 5'-phosphosulfate concentrations
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
3'-phosphoadenosine 5'-phosphosulfate
pH 8.1, 30°C, wild-type enzyme
0.039
3'-phosphoadenosine 5'-phosphosulfate
pH 8.1, 30°C, S107A mutant enzyme
0.001
adenosine 5'-phosphosulfate
pH 8.1, 30°C, wild-type enzyme at 100 mM ammonium sulfate
0.012
adenosine 5'-phosphosulfate
pH 8.1, 30°C, S107A mutant enzyme at 100 mM ammonium sulfate
0.8
ATP
pH 8.1, 30°C, wild-type enzyme at 100 mM ammonium sulfate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). KAPS_PENCH
211
0
23770
Swiss-Prot
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
-
2 * 33000, gel filtration at 46°C, the enzyme dissociates into two inactive monomers by heating above 42°C
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
2 * 33000, gel filtration at 46°C, the enzyme dissociates into two inactive monomers by heating above 42°C
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S107C
similar properties as wild-type, suggesting that S107 is not essential for activity but may be located in the substrate binding pocket
Y109F
similar properties as wild-type, velocity curve is shifted to the far right
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
below, reversible inactivation at 30°C, reactivation rate increases with increasing pH
641209
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
reversible inactivation above by subunit dissociation, kinetics, MgATP2- or MgADP- stimulate reactivation
50
80
-
irreversible inactivation, t1/2: 47 min, pH 8, 0.023 mg protein/ml
50
-
rapid loss of activity, approx. 80% of activity is recovered upon cooling at 0°C, presence of MgATP2- accelerates the recovery process
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and S107A mutant enzyme in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Renosto, F.; Seubert, P.A.; Segel, I.H.
Adenosine 5-phosphosulfate kinase from Penicillium chrysogenum. Purification and kinetic characterization
J. Biol. Chem.
259
2113-2123
1984
Penicillium chrysogenum
Renosto, F.; Schultz, T.; Re, E.; Mazer, J.; Chandler, C.J.; Barron, A.; Segel, I.H.
Comparative stability and catalytic and chemical properties of the sulfate-activating enzymes from Penicillium chrysogenum (mesophile) and Penicillium duponti (thermophile)
J. Bacteriol.
164
674-683
1985
Penicillium chrysogenum, Penicillium duponti
Renosto, 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 inactivation
J. Biol. Chem.
260
1535-1544
1985
Penicillium chrysogenum
Renosto, 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 kinase
J. Biol. Chem.
264
9433-9437
1989
Penicillium chrysogenum
MacRae, I.J.; Rose, A.B.; Segel, I.H.
Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. site-directed mutagenesis at putative phosphoryl-accepting and ATP P-loop residues
J. Biol. Chem.
273
28583-28589
1998
Escherichia coli (P23846), Escherichia coli, Penicillium chrysogenum (Q12657), Penicillium chrysogenum
MacRae, I.J.; Segel, I.H.
Adenosine 5'-phosphosulfate (APS) kinase: diagnosing the mechanism of substrate inhibition
Arch. Biochem. Biophys.
361
277-282
1999
Penicillium chrysogenum
EXTERNAL LINKS (specific for EC-Number 2.7.1.25)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
