Monogalactosyldiacylglycerol synthase

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
Search PMC articles PubMed articles NCBI proteins

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 ${\displaystyle \rightleftharpoons }$ 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.