Adenylyl-sulfate kinase

In enzymology, an adenylyl-sulfate kinase (EC 2.7.1.25) is an enzyme that catalyzes the chemical reaction

ATP + adenylyl sulfate ADP + 3'-phosphoadenylyl sulfate
adenylylsulfate kinase
Adenylylsulfate kinase homohexamer, Thiobacillus denitrificans
Identifiers
EC no.2.7.1.25
CAS no.9012-38-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
APS_kinase
crystal structure of p. chrysogenum atp sulfurylase in the t-state
Identifiers
SymbolAPS_kinase
PfamPF01583
Pfam clanCL0023
InterProIPR002891
SCOP21d6j / SCOPe / SUPFAM
CDDcd02027
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Thus, the two substrates of this enzyme are ATP and adenylyl sulfate, whereas its two products are ADP and 3'-phosphoadenylyl sulfate.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:adenylyl-sulfate 3'-phosphotransferase. Other names in common use include adenylylsulfate kinase (phosphorylating), 5'-phosphoadenosine sulfate kinase, adenosine 5'-phosphosulfate kinase, adenosine phosphosulfate kinase, adenosine phosphosulfokinase, adenosine-5'-phosphosulfate-3'-phosphokinase, and APS kinase. This enzyme participates in 3 metabolic pathways: purine metabolism, selenoamino acid metabolism, and sulfur metabolism.

This enzyme contains an ATP binding P-loop motif.[1]

Structural studies

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1D6J, 1M7G, 1M7H, 1X6V, 1XJQ, 1XNJ, 2AX4, 2GKS, 2OFW, 2OFX, and 2PEY.

References

  1. MacRae IJ, Rose AB, Segel IH (October 1998). "Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. site-directed mutagenesis at putative phosphoryl-accepting and ATP P-loop residues". J. Biol. Chem. 273 (44): 28583–9. doi:10.1074/jbc.273.44.28583. PMID 9786849.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR002891


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