Adenylyl-sulfate kinase

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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

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.

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

  • IUBMB entry for 2.7.1.25
  • BRENDA references for 2.7.1.25 (Recommended.)
  • PubMed references for 2.7.1.25
  • PubMed Central references for 2.7.1.25
  • Google Scholar references for 2.7.1.25
  • Bandurski RS, Wilson LG, Squires CL (1956). "The mechanism of "active sulfate" formation". J. Am. Chem. Soc. 78: 6408&ndash, 6409.
  • ROBBINS PW, LIPMANN F (1957). "Isolation and identification of active sulfate". J. Biol. Chem. 229: 837&ndash, 51. PMID 13502346.
  • Venkatachalam KV, Akita H, Strott CA (1998). "Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains". J. Biol. Chem. 273: 19311&ndash, 20. PMID 9668121.

External links

The CAS registry number for this enzyme class is 9012-38-8.

Gene Ontology (GO) codes


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