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 ${\displaystyle \rightleftharpoons }$ 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.

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

• Bandurski RS, Wilson LG, Squires CL (1956). "The mechanism of "active sulfate" formation". J. Am. Chem. Soc. 78 (24): 6408–6409. doi:10.1021/ja01605a028.
• ROBBINS PW, LIPMANN F (1957). "Isolation and identification of active sulfate". J. Biol. Chem. 229 (2): 837–51. 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 (30): 19311–20. doi:10.1074/jbc.273.30.19311. PMID 9668121.

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