Adenylyl-sulfate kinase () is an enzyme that catalyzes the chemical reaction
The enzyme characterised from liver converts the adenosine monophosphate derivative, 5'-adenylyl sulfate, to 3'-phosphoadenosine-5'-phosphosulfate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). The enzyme is also found in human brain.
This enzyme is a transferase, specifically one 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. It participates in 3 metabolic pathways: purine metabolism, selenoamino acid metabolism, and sulfur metabolism.
This enzyme contains an ATP binding P-loop motif.
Structural studies As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
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