| 1,2-diacylglycerol 3-beta-galactosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.46 | ||||||||
| CAS no. | 37277-55-7 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a monogalactosyldiacylglycerol synthase (EC 2.4.1.46) is an enzyme that catalyzes the chemical reaction
- UDP-galactose + 1,2-diacyl-sn-glycerol UDP + 3-beta-D-galactosyl-1,2-diacyl-sn-glycerol
Thus, the two substrates of this enzyme are UDP-galactose and 1,2-diacyl-sn-glycerol, whereas its two products are UDP and 3-beta-D-galactosyl-1,2-diacyl-sn-glycerol.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:1,2-diacyl-sn-glycerol 3-beta-D-galactosyltransferase. Other names in common use include uridine diphosphogalactose-1,2-diacylglycerol galactosyltransferase, UDP-galactose:diacylglycerol galactosyltransferase, MGDG synthase, UDP galactose-1,2-diacylglycerol galactosyltransferase, UDP-galactose-diacylglyceride galactosyltransferase, UDP-galactose:1,2-diacylglycerol 3-beta-D-galactosyltransferase, 1beta-MGDG, and 1,2-diacylglycerol 3-beta-galactosyltransferase. This enzyme participates in glycerolipid metabolism.
References
- Veerkamp JH (1974). "Biochemical changes in Bifidobacterium bifidum var. pennsylvanicus after cell-wall inhibition. VI. Biosynthesis of the galactosyldiglycerides". Biochim. Biophys. Acta. 348 (1): 23–34. doi:10.1016/0005-2760(74)90089-7. PMID 4838219.
- Wenger DA, Petitpas JW, Pieringer RA (1968). "The metabolism of glyceride glycolipids. II. Biosynthesis of monogalactosyl diglyceride from uridine diphosphate galactose and diglyceride in brain". Biochemistry. 7 (10): 3700–7. doi:10.1021/bi00850a049. PMID 5681471.
- K, Douce R, Joyard J (1999). "Biochemical and topological properties of type A MGDG synthase, a spinach chloroplast envelope enzyme catalyzing the synthesis of both prokaryotic and eukaryotic MGDG". Eur. J. Biochem. 265 (3): 990–1001. doi:10.1046/j.1432-1327.1999.00801.x. PMID 10518794.
- Benning C, Ohta H (2005). "Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants". J. Biol. Chem. 280 (4): 2397–400. doi:10.1074/jbc.R400032200. PMID 15590685.