| 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 | ||||||
| |||||||
Adenylyl-sulfate kinase (EC 2.7.1.25) 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).[1][2] The enzyme is also found in human brain.[3]
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.[4]
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1D6J, PDB: 1M7G, PDB: 1M7H, PDB: 1X6V, PDB: 1XJQ, PDB: 1XNJ, PDB: 2AX4, PDB: 2GKS, PDB: 2OFW, PDB: 2OFX, and PDB: 2PEY.
References
- Bandurski RS, Wilson LG, Squires CL (1956). "The mechanism of "active sulfate" formation". J. Am. Chem. Soc. 78 (24): 6408–6409. Bibcode:1956JAChS..78.6408B. 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.
- Enzyme 2.7.1.25 at KEGG Pathway Database.
- 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.