Information on EC 2.4.1.96 - sn-glycerol-3-phosphate 1-galactosyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.96
-
RECOMMENDED NAME
GeneOntology No.
sn-glycerol-3-phosphate 1-galactosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + sn-glycerol 3-phosphate = UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:sn-glycerol-3-phosphate 1-alpha-D-galactosyltransferase
The product is hydrolysed by a phosphatase to isofloridoside, which is involved in osmoregulation (cf. EC 2.4.1.137 sn-glycerol-3-phosphate 2-alpha-galactosyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
9076-70-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cf. EC 2.4.1.15; gene Gasu_26940
UniProt
Manually annotated by BRENDA team
cf. EC 2.4.1.15; gene Gasu_26940
UniProt
Manually annotated by BRENDA team
Ochromonas malhamensis
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-galactose + sn-glycerol 3-phosphate
UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
show the reaction diagram
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-galactose + sn-glycerol 3-phosphate
UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
show the reaction diagram
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
show the reaction diagram
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
sn-glycerol 3-phosphate
-
-
0.01
UDPgalactose
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
about 50% of activity maximum at pH 6 and pH 9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
68000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 70000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
Ochromonas malhamensis
-
30 min, enzyme in crude extract, 50% loss of activity
30
Ochromonas malhamensis
-
almost complete inactivation after some min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
a combination of dithioerythritol and bovine serum gamma-globulin stabilizes the enzyme during cell destruction
Ochromonas malhamensis
-
cetyltrimethylammonium bromide, optimal concentration for stabilization, 0.075% w/v at pH 8.5, 0.1% w/v at pH 7.2, 0.2 w/v at pH 6.2
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glycerol, 30% v/v, stabilizes the enzyme at pH 7.8 but not at lower or higher pH values
-
the presumable proenzyme is fully stable even over 20 h in cell extract at pH 7.8 containing bovine serum albumin at 0°C, activation of the proenzyme is followed by rapid inactivation
Ochromonas malhamensis
-
unstable to repeated freezing and thawing
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene Gasu_26940, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree