Adenylyl-sulfate kinase
| adenylylsulfate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Adenylylsulfate kinase homohexamer, Thiobacillus denitrificans | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.1.25 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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.
This enzyme contains an ATP binding P-loop motif.[1]
Structural studies
[edit]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
[edit]- ^ 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
[edit]- 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. doi:10.1016/S0021-9258(19)63689-6. 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.
