Summary
In enzymology, a glycerol-3-phosphate O-acyltransferase (EC 2.3.1.15) is an enzyme that catalyzes the chemical reaction
| glycerol-3-phosphate O-acyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.15 | ||||||||
| CAS no. | 9029-96-3 | ||||||||
| 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 | ||||||||
| |||||||||
- acyl-CoA + sn-glycerol 3-phosphate CoA + 1-acyl-sn-glycerol 3-phosphate
Thus, the two substrates of this enzyme are acyl-CoA and sn-glycerol 3-phosphate, whereas its two products are CoA and 1-acyl-sn-glycerol 3-phosphate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:sn-glycerol-3-phosphate 1-O-acyltransferase. Other names in common use include alpha-glycerophosphate acyltransferase, 3-glycerophosphate acyltransferase, ACP:sn-glycerol-3-phosphate acyltransferase, glycerol 3-phosphate acyltransferase, glycerol phosphate acyltransferase, glycerol phosphate transacylase, glycerophosphate acyltransferase, glycerophosphate transacylase, sn-glycerol 3-phosphate acyltransferase, and sn-glycerol-3-phosphate acyltransferase. This enzyme participates in glycerolipid metabolism and glycerophospholipid metabolism. The later pathways in human is part of the WikiPathways[1] machine readable pathway collection.
Structural studies edit
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1IUQ and 1K30. Currently 4 different proteins are assigned to this reaction, GPAT1, GPAT2, GPAT3 and GPAT4. GPAT1 and 2 are considered mitochondrial proteins.[2][3]
References edit
- Bertrams M; Heinz E (1981). "Positional Specificity and Fatty Acid Selectivity of Purified sn-Glycerol 3-Phosphate Acyltransferases from Chloroplasts". Plant Physiol. 68 (3): 653–657. doi:10.1104/pp.68.3.653. PMC 425956. PMID 16661974.
- Frentzen M, Heinz E, McKeon TA, Stumpf PK (1983). "Specificities and selectivities of glycerol-3-phosphate acyltransferase and monoacylglycerol-3-phosphate acyltransferase from pea and spinach chloroplasts". Eur. J. Biochem. 129 (3): 629–36. doi:10.1111/j.1432-1033.1983.tb07096.x. PMID 6825679.
- Green PR, Vanaman TC, Modrich P, Bell RM (1983). "Partial NH2- and COOH-terminal sequence and cyanogen bromide peptide analysis of Escherichia coli sn-glycerol-3-phosphate acyltransferase". J. Biol. Chem. 258 (18): 10862–6. PMID 6350296.
- Yamashita S, Numa S (1972). "Partial purification and properties of glycerophosphate acyltransferase from rat liver. Formation of 1-acylglycerol 3-phosphate from sn-glycerol 3-phosphate and palmityl coenzyme A". Eur. J. Biochem. 31 (3): 565–73. doi:10.1111/j.1432-1033.1972.tb02566.x. PMID 4650158.
