Acetate kinase
| Acetate_kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 structure of butyrate kinase 2 reveals both open- and citrate-induced closed conformations: implications for substrate-induced fit conformational changes |
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| Identifiers | |||||||||
| Symbol | Acetate_kinase | ||||||||
| Pfam | PF00871 | ||||||||
| Pfam clan | CL0108 | ||||||||
| InterPro | IPR000890 | ||||||||
| PROSITE | PDOC00826 | ||||||||
| SCOP | 1g99 | ||||||||
| SUPERFAMILY | 1g99 | ||||||||
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In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation.[1][2] The enzyme is important in the process of glycolysis, enzyme levels being increased in the presence of excess glucose. The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme is involved in excretion of excess carbohydrate.[1] A related enzyme, butyrate kinase, facilitates the formation of butyryl-CoA by phosphorylating butyrate in the presence of ATP to form butyryl phosphate.[2]
References
- ^ a b Grundy FJ, Waters DA, Allen SH, Henkin TM (November 1993). "Regulation of the Bacillus subtilis acetate kinase gene by CcpA". J. Bacteriol. 175 (22): 7348–55. PMC 206879. PMID 8226682.
- ^ a b Oultram JD, Burr ID, Elmore MJ, Minton NP (September 1993). "Cloning and sequence analysis of the genes encoding phosphotransbutyrylase and butyrate kinase from Clostridium acetobutylicum NCIMB 8052". Gene 131 (1): 107–12. doi:10.1016/0378-1119(93)90677-U. PMID 8396545.
This article incorporates text from the public domain Pfam and InterPro IPR000890
