Information on EC 2.4.1.137 - sn-glycerol-3-phosphate 2-alpha-galactosyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.137
-
RECOMMENDED NAME
GeneOntology No.
sn-glycerol-3-phosphate 2-alpha-galactosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + sn-glycerol 3-phosphate = UDP + 2-(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 2-alpha-D-galactosyltransferase
The product is hydrolysed by a phosphatase to floridoside (cf. EC 2.4.1.96 sn-glycerol-3-phosphate 1-galactosyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
80747-34-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Zan.
-
-
Manually annotated by BRENDA team
Zan.
-
-
Manually annotated by BRENDA team
Stackh.
-
-
Manually annotated by BRENDA team
Stackh.
-
-
Manually annotated by BRENDA team
Lightf., Batt.
-
-
Manually annotated by BRENDA team
O.F. Müller, Lamour.
-
-
Manually annotated by BRENDA team
gene Gasu_10960
-
-
Manually annotated by BRENDA team
gene Gasu_10960
-
-
Manually annotated by BRENDA team
Lomentaria umbellata
H. u. H., Gendo
-
-
Manually annotated by BRENDA team
-
-
-
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 + 2-(alpha-D-galactosyl)-sn-glycerol 3-phosphate
show the reaction diagram
UDP-galactose + sn-glycerol 3-phosphate
UDP + 2-(alpha-D-galactosyl)-sn-glycerol 3-phosphate
show the reaction diagram
-
the enzyme is involved in synthesis and degradation of floridoside. Decrease in enzyme activity during nutrient limitation. Addition of nutrients causes an increase in enzyme activity and a decrease in the content of starch and floridoside
-
-
?
UDPgalactose + sn-glycerol 3-phosphate
UDP + 2-(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 + 2-(alpha-D-galactosyl)-sn-glycerol 3-phosphate
show the reaction diagram
UDP-galactose + sn-glycerol 3-phosphate
UDP + 2-(alpha-D-galactosyl)-sn-glycerol 3-phosphate
show the reaction diagram
-
the enzyme is involved in synthesis and degradation of floridoside. Decrease in enzyme activity during nutrient limitation. Addition of nutrients causes an increase in enzyme activity and a decrease in the content of starch and floridoside
-
-
?
UDPgalactose + sn-glycerol 3-phosphate
UDP + 2-(alpha-D-galactosyl)-sn-glycerol 3-phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor or activator found
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
UDP
-
5 mM, competitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor or activator found
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8
sn-glycerol 3-phosphate
-
-
2.7
UDPgalactose
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
-
HPLC gel filtration
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene Gasu_10960, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree. Complementation of a salt-sensitive, glucosylglycerol-defective mutant of Synechocystis sp. PCC 6803 with Gasu_10960
-