| EC |
3.1.1.71 |
| Accepted name: |
acetylalkylglycerol acetylhydrolase |
| Reaction: |
2-acetyl-1-alkyl-sn-glycerol + H2O = 1-alkyl-sn-glycerol + acetate |
| Other name(s): |
alkylacetylglycerol acetylhydrolase |
| Systematic name: |
2-acetyl-1-alkyl-sn-glycerol acetylhydrolase |
| Comments: |
Hydrolysis of the acetyl group from the 1-alkyl-2-acetyl and 1-alkyl-3-acetyl substrates occurs at apparently identical rates. The enzyme from Erlich ascites cells is membrane-bound. It differs from lipoprotein lipase (EC 3.1.1.34) since 1,2-diacetyl-sn-glycerols are not substrates. It also differs from EC 3.1.1.47, 1-acetyl-2-alkyl-glycerophosphocholine esterase. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
| References: |
| 1. |
Blank, M.L., Smith, Z.L., Cress, E.A., Snyder, F. Characterization of the enzymatic hydrolysis of acetate from alkylacetylglycerols in the de novo pathway of PAF biosynthesis. Biochim. Biophys. Acta 1042 (1990) 153–158. [DOI] [PMID: 2302414] |
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| [EC 3.1.1.71 created 1999] |
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