Adenylyl-sulfate kinase

Protein family From Wikipedia, the free encyclopedia

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
Quick facts APS_kinase, Identifiers ...
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:
PDB  IPR002891 PF01583 (ECOD; PDBsum)  
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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

Further reading

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