Biology:Adenylyl-sulfate kinase
| adenylylsulfate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Adenylylsulfate kinase homohexamer, Thiobacillus denitrificans | |||||||||
| Identifiers | |||||||||
| EC number | 2.7.1.25 | ||||||||
| CAS number | 9012-38-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| APS_kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of p. chrysogenum atp sulfurylase in the t-state | |||||||||
| Identifiers | |||||||||
| Symbol | APS_kinase | ||||||||
| Pfam | PF01583 | ||||||||
| Pfam clan | CL0023 | ||||||||
| InterPro | IPR002891 | ||||||||
| SCOP2 | 1d6j / SCOPe / SUPFAM | ||||||||
| CDD | cd02027 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
- ↑ "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. October 1998. doi:10.1074/jbc.273.44.28583. PMID 9786849.
Further reading
- "The mechanism of "active sulfate" formation". J. Am. Chem. Soc. 78 (24): 6408–6409. 1956. doi:10.1021/ja01605a028.
- "Isolation and identification of active sulfate". J. Biol. Chem. 229 (2): 837–51. 1957. PMID 13502346.
- "Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains". J. Biol. Chem. 273 (30): 19311–20. 1998. doi:10.1074/jbc.273.30.19311. PMID 9668121.
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