Glycerol-1-phosphatase
In enzymology, a glycerol-1-phosphatase (EC 3.1.3.21) is an enzyme that catalyzes the chemical reaction
- glycerol 1-phosphate + H2O glycerol + phosphate
| glycerol-1-phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.3.21 | ||||||||
| CAS number | 37228-75-4 | ||||||||
| 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 | ||||||||
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Thus, the two substrates of this enzyme are glycerol 1-phosphate and H2O, whereas its two products are glycerol and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is glycerol-1-phosphate phosphohydrolase. Other names in common use include alpha-glycerophosphatase, alpha-glycerol phosphatase, glycerol 3-phosphatase, glycerol-3-phosphate phosphatase, and glycerol 3-phosphate phosphohydrolase. This enzyme participates in glycerolipid metabolism.
Among the organisms that have been shown to express this enzymatic activity are A. thaliana (plant) via the AtSgpp and AtGpp gene products;[1] D. salina (alga);[2] S. cerevisiae (fungus) via the GPP1/RHR2/YIL053W and GPP2/HOR2/YER062C gene products;[3][4] C. albicans (fungus) via the GPP1 gene product;[5] M. tuberculosis (bacteria) via the rv1692 gene product;[6] and C57BL/6N mice and Wistar rats (mammals) via the PGP gene product.[7]
References
- Caparrós-Martín JA, McCarthy-Suárez I, Culiáñez-Macià FA (September 2014). "The kinetic analysis of the substrate specificity of motif 5 in a HAD hydrolase-type phosphosugar phosphatase of Arabidopsis thaliana". Planta (Abstract). 240 (3): 479–87. doi:10.1007/s00425-014-2102-6. PMID 24915748 – via SpringerLink.
- Sussman I, Avron M (13 October 1981). "Characterization and partial purification of DL-glycerol-1-phosphatase from Dunaliella salina". Biochimica et Biophysica Acta (Abstract). 661 (2): 199–204. doi:10.1016/0005-2744(81)90004-8. PMID 6252970.
- Norbeck J, Påhlman AK, Akhtar N, et al. (7 June 1996). "Purification and Characterization of Two Isoenzymes of DL-Glycerol-3-phosphatase from Saccharomyces cerevisiae". Journal of Biological Chemistry. 271 (23): 13875–81. doi:10.1074/jbc.271.23.13875. PMID 8662716.
- Påhlman AK, Granath K, Ansell R, et al. (2 February 2001). "The Yeast Glycerol 3-Phosphatases Gpp1p and Gpp2p Are Required for Glycerol Biosynthesis and Differentially Involved in the Cellular Responses to Osmotic, Anaerobic, and Oxidative Stress". Journal of Biological Chemistry. 276 (5): 3555–63. doi:10.1074/jbc.M007164200. PMID 11058591.
- Fan J, Whiteway M, Shen SH (April 2005). "Disruption of a gene encoding glycerol 3-phosphatase from Candida albicans impairs intracellular glycerol accumulation-mediated salt-tolerance". FEMS Microbiology Letters. 245 (1): 107–16. doi:10.1016/j.femsle.2005.02.031. PMID 15796987 – via Oxford University Press.
- Larrouy-Maumus G, Biswas T, Hunt DM, et al. (25 June 2013). "Discovery of a glycerol 3-phosphate phosphatase reveals glycerophospholipid polar head recycling in Mycobacterium tuberculosis". Proceedings of the National Academy of Sciences of the United States of America. 110 (28): 11320–5. Bibcode:2013PNAS..11011320L. doi:10.1073/pnas.1221597110. PMC 3710836. PMID 23801751.
- Mugago Y, Zhao S, Seifried A, et al. (11 January 2016). "Identification of a mammalian glycerol-3-phosphate phosphatase". Proceedings of the National Academy of Sciences of the United States of America. 113 (4): E430–9. doi:10.1073/pnas.1514375113. PMC 4743820. PMID 26755581.