| EC |
3.1.3.106 |
| Accepted name: |
2-lysophosphatidate phosphatase |
| Reaction: |
a 1-acyl-sn-glycerol 3-phosphate + H2O = a 1-acyl-sn-glycerol + phosphate |
| Other name(s): |
1-acyl-sn-glycerol 3-phosphatase; CPC3 (gene name); PHM8 (gene name) |
| Systematic name: |
1-acyl-sn-glycerol 3-phosphate phosphohydrolase |
| Comments: |
The enzyme has been studied from the plants Arachis hypogaea (peanut) and Arabidopsis thaliana (thale cress) and from the yeast Saccharomyces cerevisiae. The enzyme from yeast, but not from the plants, requires Mg2+. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
| References: |
| 1. |
Shekar, S., Tumaney, A.W., Rao, T.J. and Rajasekharan, R. Isolation of lysophosphatidic acid phosphatase from developing peanut cotyledons. Plant Physiol. 128 (2002) 988–996. [PMID: 11891254] |
| 2. |
Reddy, V.S., Singh, A.K. and Rajasekharan, R. The Saccharomyces cerevisiae PHM8 gene encodes a soluble magnesium-dependent lysophosphatidic acid phosphatase. J. Biol. Chem. 283 (2008) 8846–8854. [PMID: 18234677] |
| 3. |
Reddy, V.S., Rao, D.K. and Rajasekharan, R. Functional characterization of lysophosphatidic acid phosphatase from Arabidopsis thaliana. Biochim. Biophys. Acta 1801 (2010) 455–461. [PMID: 20045079] |
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| [EC 3.1.3.106 created 2019] |
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