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PMID:23356794
| Citation |
Comba, S, Menendez-Bravo, S, Arabolaza, A and Gramajo, H (2013) Identification and physiological characterization of phosphatidic acid phosphatase enzymes involved in triacylglycerol biosynthesis in Streptomyces coelicolor. Microb. Cell Fact. 12:9 |
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| Abstract |
Phosphatidic acid phosphatase (PAP, EC 3.1.3.4) catalyzes the dephosphorylation of phosphatidate yielding diacylglycerol (DAG), the lipid precursor for triacylglycerol (TAG) biosynthesis. Despite the importance of PAP activity in TAG producing bacteria, studies to establish its role in lipid metabolism have been so far restricted only to eukaryotes. Considering the increasing interest of bacterial TAG as a potential source of raw material for biofuel production, we have focused our studies on the identification and physiological characterization of the putative PAP present in the TAG producing bacterium Streptomyces coelicolor. |
| Links |
PubMed PMC3599759 Online version:10.1186/1475-2859-12-9 |
| Keywords |
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| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0008195: phosphatidate phosphatase activity |
ECO:0000314: |
F |
Figure 3 shows that heterologous expression of SCO1102 in E. coli resulted in increased amounts of fatty acid as well as diacylglycerol compared to the amounts of each produced by the control strain. |
complete | ||||
|
enables |
GO:0008195: phosphatidate phosphatase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
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