Glycerol-1-phosphatase
| Glycerol-1-phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.3.21 | ||||||||
| CAS no. | 37228-75-4 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme glycerol-1-phosphatase (EC 3.1.3.21) catalyzes the reaction
The enzyme characterised from Dunaliella salina hydrolyses racemic glycerol 3-phosphate to glycerol and orthophosphate.[1][2]
Among the organisms that have been shown to express this enzymatic activity are Arabidopsis thaliana (plant) via the AtSgpp and AtGpp gene products;[3] Dunaliella salina (alga);[1] Saccharomyces cerevisiae (fungus) via the GPP1/RHR2/YIL053W and GPP2/HOR2/YER062C gene products;[4][5] Candida albicans (fungus) via the GPP1 gene product;[6] Mycobacterium tuberculosis (bacteria) via the rv1692 gene product;[7] and C57BL/6N mice and Wistar rats (mammals) via the PGP gene product.[8]
Nomenclature
This enzyme is a hydrolase, specifically one acting on phosphoric monoester bonds. The systematic name is glycerol-1-phosphate phosphohydrolase. Other names in common use include α-glycerophosphatase, α-glycerol phosphatase, glycerol 3-phosphatase, glycerol-3-phosphate phosphatase, and glycerol 3-phosphate phosphohydrolase.[9]
References
- 1 2 Sussman I, Avron M (13 October 1981). "Characterization and partial purification of DL-glycerol-1-phosphatase from Dunaliella salina". Biochimica et Biophysica Acta (BBA) - Enzymology (Abstract). 661 (2): 199–204. doi:10.1016/0005-2744(81)90004-8. PMID 6252970.
- ↑ Schomburg, Dietmar; Salzmann, Margit (1991). "Glycerol-1-phosphatase". Enzyme Handbook 3. pp. 393–396. doi:10.1007/978-3-642-76463-9_82. ISBN 978-3-642-48962-4.
- ↑ 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. Bibcode:2014Plant.240..479C. doi:10.1007/s00425-014-2102-6. hdl:10251/87695. PMID 24915748. S2CID 8764480 – via SpringerLink.
- ↑ 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.
- ↑ Enzyme 3.1.3.21 at KEGG Pathway Database.