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Enzyme Nomenclature
Information on EC 2.7.8.20 - phosphatidylglycerol-membrane-oligosaccharide glycerophosphotransferase
for references in articles please use BRENDA:EC2.7.8.20
Word Map on EC 2.7.8.20
- 2.7.8.20
-
periplasmic
- phosphoethanolamine
- oligosaccharides
-
osmoregulated
- phospholipids
- lactobacillus
- arbutin
-
kennedy
-
succinyl
-
lipoteichoic
- beta-glucoside
- colitis
- glucans
- acidophilus
- cerebroside
- phosphoglycerate
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metal-binding
-
variously
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pyrophosphatase
-
schulman
-
sulfatases
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bacteriol
- diglyceride
- phosphopentomutase
-
jackson
-
mutase
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cofactor-independent
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.7.8.20
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RECOMMENDED NAME
GeneOntology No.
phosphatidylglycerol-membrane-oligosaccharide glycerophosphotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphatidylglycerol + membrane-derived-oligosaccharide D-glucose = 1,2-diacyl-sn-glycerol + membrane-derived-oligosaccharide 6-(glycerophospho)-D-glucose
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
substituted phospho group transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
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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CAS REGISTRY NUMBER
COMMENTARY
80146-86-7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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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-
-
-
?
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
-
-
-
?
phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
-
-
-
?
phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
-
1,2-beta- and 1,6-beta-linked glucose residues in membrane polysaccharides and in synthetic glucosides can act as acceptors
-
?
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
-
?
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
-
?
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
-
?
phosphatidylglycerol + p-hydroxyphenyl-beta-D-glucoside
sn-1,2-diacylglycerol + p-hydroxyphenyl-beta-D-glucoside-6-phosphoglycerol
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i.e. arbutin
-
?
phosphatidylglycerol + p-hydroxyphenyl-beta-D-glucoside
sn-1,2-diacylglycerol + p-hydroxyphenyl-beta-D-glucoside-6-phosphoglycerol
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i.e. arbutin
-
?
phosphatidylglycerol + p-hydroxyphenyl-beta-D-glucoside
sn-1,2-diacylglycerol + p-hydroxyphenyl-beta-D-glucoside-6-phosphoglycerol
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i.e. arbutin
-
?
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
-
?
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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-
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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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-
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additional information
?
-
-
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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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
additional information
?
-
-
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
-
-
-
phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
-
-
-
?
phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
-
-
-
?
phosphatidylglycerol + membrane-derived oligosaccharide D-glucose
sn-1,2-diacylglycerol + beta-D-glucoside-6-phosphoglycerol
-
the enzyme belongs to the alkaline phosphatase enzymes superfamily, with conserved metal-binding residues
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-gentiobiose
-
at 1-5 mM, competitive to membrane-derived oligosaccharides
EDTA
-
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the active site is localized on the periplasmic face of the inner membrane
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in an enzyme defective Sinorhizobium meliloti mutant strain
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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.8.20)
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