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Information on EC 2.7.8.20 - phosphatidylglycerol-membrane-oligosaccharide glycerophosphotransferase for references in articles please use BRENDA:EC2.7.8.20
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EC Tree
IUBMB Comments 1,2-beta- and 1,6-beta-linked glucose residues in membrane polysaccharides and in synthetic glucosides can act as acceptors.
The enzyme appears in viruses and cellular organisms
Synonyms
membrane-bound phosphoglycerol transferase I, oligosaccharide glycerophosphotransferase, OPG, phosphoglycerol transferase, phosphoglycerol transferase I,
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membrane-bound phosphoglycerol transferase I
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oligosaccharide glycerophosphotransferase
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phosphoglycerol transferase
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phosphoglycerol transferase I
phosphoglycerol transferase I
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phosphoglycerol transferase I
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phosphatidylglycerol + membrane-derived-oligosaccharide D-glucose = 1,2-diacyl-sn-glycerol + membrane-derived-oligosaccharide 6-(glycerophospho)-D-glucose
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substituted phospho group transfer
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phosphatidylglycerol:membrane-derived-oligosaccharide-D-glucose glycerophosphotransferase
1,2-beta- and 1,6-beta-linked glucose residues in membrane polysaccharides and in synthetic glucosides can act as acceptors.
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phosphatidylglycerol + (R)-alpha[(6-O-beta-D-glucopyranosyl-beta-D-glucopyranosyl)oxyl]benzeneacetonitrile
sn-1,2-diacylglycerol + (R)-alpha[(6-O-beta-D-glucopyranosyl-beta-D-glucopyranosyl)oxyl]benzeneacetonitrile-6-phosphoglycerol
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i.e. amygdalin
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phosphatidylglycerol + beta-gentiobiose
sn-1,2-diacylglycerol + beta-gentiobiose-6-phosphoglycerol
phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
phosphatidylglycerol + o-nitrophenyl-beta-D-glucoside
sn-1,2-diacylglycerol + o-nitrophenyl-beta-D-glucoside-6-phosphoglycerol
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phosphatidylglycerol + octyl-beta-D-glucoside
sn-1,2-diacylglycerol + octyl-beta-D-glucoside-6-phosphoglycerol
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phosphatidylglycerol + p-hydroxyphenyl-beta-D-glucoside
sn-1,2-diacylglycerol + p-hydroxyphenyl-beta-D-glucoside-6-phosphoglycerol
phosphatidylglycerol + p-nitrophenyl-beta-D-glucoside
sn-1,2-diacylglycerol + p-nitrophenyl-beta-D-glucoside-6-phosphoglycerol
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additional information
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phosphatidylglycerol + beta-gentiobiose
sn-1,2-diacylglycerol + beta-gentiobiose-6-phosphoglycerol
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phosphatidylglycerol + beta-gentiobiose
sn-1,2-diacylglycerol + beta-gentiobiose-6-phosphoglycerol
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much less active as substrate than arbutin
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phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
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phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
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phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
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phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
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1,2-beta- and 1,6-beta-linked glucose residues in membrane polysaccharides and in synthetic glucosides can act as acceptors
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phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
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the enzyme is specific for beta-glucosides
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phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
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the active site of the enzyme is on the periplasmic side of the cytoplasmic membrane
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phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
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the enzyme belongs to the alkaline phosphatase enzymes superfamily, with conserved metal-binding residues
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phosphatidylglycerol + p-hydroxyphenyl-beta-D-glucoside
sn-1,2-diacylglycerol + p-hydroxyphenyl-beta-D-glucoside-6-phosphoglycerol
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i.e. arbutin
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phosphatidylglycerol + p-hydroxyphenyl-beta-D-glucoside
sn-1,2-diacylglycerol + p-hydroxyphenyl-beta-D-glucoside-6-phosphoglycerol
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i.e. arbutin
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phosphatidylglycerol + p-hydroxyphenyl-beta-D-glucoside
sn-1,2-diacylglycerol + p-hydroxyphenyl-beta-D-glucoside-6-phosphoglycerol
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i.e. arbutin
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phosphatidylglycerol + p-hydroxyphenyl-beta-D-glucoside
sn-1,2-diacylglycerol + p-hydroxyphenyl-beta-D-glucoside-6-phosphoglycerol
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the enzyme activity is not affected by the osmolarity of the medium
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additional information
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the membrane-bound phosphoglycerol transferase I transfers residues from membrane phosphatidylglycerol to nascent osmoregulated periplasmic glucan molecules. Phosphoglycerol transferase II is a soluble periplasmic form of phosphoglycerol transferase I, both activities, phosphoglycerol transferase I and II, are necessary to complete osmoregulated periplasmic glucan substitution
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additional information
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the membrane-bound phosphoglycerol transferase I transfers residues from membrane phosphatidylglycerol to nascent osmoregulated periplasmic glucan molecules
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additional information
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cyclic beta-glucans are also substrates. The synthesis of glycerophosphorylated cyclic beta-glucans is osmotically regulated. The enzyme activity is regulated at both the transcriptional and posttranslational levels
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phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
additional information
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the membrane-bound phosphoglycerol transferase I transfers residues from membrane phosphatidylglycerol to nascent osmoregulated periplasmic glucan molecules. Phosphoglycerol transferase II is a soluble periplasmic form of phosphoglycerol transferase I, both activities, phosphoglycerol transferase I and II, are necessary to complete osmoregulated periplasmic glucan substitution
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phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
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phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
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phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
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the enzyme belongs to the alkaline phosphatase enzymes superfamily, with conserved metal-binding residues
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Ca2+
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divalent cation required, Ca2+ is less effective than Mn2+
Mg2+
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divalent cation required, less effective than Mn2+. At the optimal concentration, 0.5 mM, the activity is 67% of that observed with the same concentration of MnCl2
Mn2+
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divalent cation required, Mn2+ is the most effective
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arbutin
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at 5 mM, competitive to membrane-derived oligosaccharides
beta-gentiobiose
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at 1-5 mM, competitive to membrane-derived oligosaccharides
EDTA
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at 0.1 mM, for 1 h at 0ºC, activity is reduced to 40% of the control value. The activity is fully restored by addition of 0.5 mM MnCl2
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2 - 3
arbutin
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pH 4.5, 37ºC
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7.8 - 9.7
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50% of optimal activity at pH 7.8 and pH 9.7
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Rhizobium meliloti
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DF214, LIN205 and AB1133 strains
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gene opgB
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K12 strain CA198
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the active site is localized on the periplasmic face of the inner membrane
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membrane-bound
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expression in an enzyme defective Escherichia coli mutant strain
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expression in an enzyme defective Sinorhizobium meliloti mutant strain
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Jackson, B.J.; Kennedy, E.P.
The biosynthesis of membrane-derived oligosaccharides. A membrane-bound phosphoglycerol transferase
J. Biol. Chem.
258
2394-2398
1983
Escherichia coli
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Lanfroy, E.; Bohin, J.P.
Physical map location of the Escherichia coli gene encoding phosphoglycerol transferase I
J. Bacteriol.
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5736-5737
1993
Escherichia coli
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Bohin, J.P.; Kennedy, E.P.
Regulation of the synthesis of membrane-derived oligosaccharides in Escherichia coli. Assay of phosphoglycerol transferase I in vivo
J. Biol. Chem.
259
8388-8393
1984
Escherichia coli
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Galperin, M.Y.; Jedrzejas, M.J.
Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes
Proteins
45
318-324
2001
Escherichia coli
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Wang, P.; Ingram-Smith, C.; Hadley, J.A.; Miller, K.J.
Cloning, sequencing, and characterization of the cgmB gene of Sinorhizobium meliloti involved in cyclic beta-glucan biosynthesis
J. Bacteriol.
181
4576-4583
1999
Sinorhizobium meliloti
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Lequette, Y.; Lanfroy, E.; Cogez, V.; Bohin, J.P.; Lacroix, J.M.
Biosynthesis of osmoregulated periplasmic glucans in Escherichia coli: the membrane-bound and the soluble periplasmic phosphoglycerol transferases are encoded by the same gene
Microbiology
154
476-483
2008
Escherichia coli
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