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Information on EC 2.4.1.96 - sn-glycerol-3-phosphate 1-galactosyltransferase
for references in articles please use BRENDA:EC2.4.1.96
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.96 sn-glycerol-3-phosphate 1-galactosyltransferase
IUBMB Comments
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-α-galactosyltransferase).
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
isofloridoside-phosphate synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
galactosyltransferase, glycerol 3-phosphate 1alpha-
-
-
-
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galactosyltransferse, uridine diphosphogalactose-glycerol phosphate
-
-
-
-
isofloridoside phosphate synthase/phosphatase fusion protein
isofloridoside-phosphate synthase
-
-
-
-
JFP-synthase
-
-
-
-
UDP-Gal:sn-glycero-3-phosphoric acid 1-alpha-galactosyl-transferase
-
-
-
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UDPgalactose:sn-glycerol-3-phosphate alpha-D-galactosyltransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + sn-glycerol 3-phosphate = UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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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).
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CAS REGISTRY NUMBER
COMMENTARY
9076-70-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-galactose + sn-glycerol 3-phosphate
UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
UDP-alpha-D-galactose + sn-glycerol 3-phosphate
UDP + isofloridoside phosphate
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + sn-glycerol 3-phosphate
UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + sn-glycerol 3-phosphate
UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
Products: -
?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
-
Substrates: -
Products: -
Products: -
?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
-
Substrates: -
Products: i.e. isofloridoside phosphate
Products: i.e. isofloridoside phosphate
?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
-
Substrates: enzyme is involved in regulation of osmotic balance in Ochromonas
Products: -
Products: -
?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: metabolite analysis by mass spectrometry
Products: -
Products: -
?
additional information
?
-
Substrates: metabolite analysis by mass spectrometry
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-galactose + sn-glycerol 3-phosphate
UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
-
Substrates: enzyme is involved in regulation of osmotic balance in Ochromonas
Products: -
Products: -
?
UDP-alpha-D-galactose + sn-glycerol 3-phosphate
UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + sn-glycerol 3-phosphate
UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
Substrates: -
Products: -
Products: -
?
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
proteolytic activation mechanism might be the first step in the activation of IFP-synthase after cell shrinkage due to osmotic water loss. About 1 h later when proteolytic activation is no longer evident and the isofloridoside pool is almost filled up a second maximum of active IFP-synthase is evident. This type of enzyme exhibits different molecular properties and might by involved in the turnover of the isofloridoside pool
-
additional information
-
enzyme appears to exist as an inactive proenzyme which can be activated by incubation of crude cell extracts with endogenous or exogenous proteases
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
cells are grown in basal medium containing 25mM glucose as sole carbon source
brenda
additional information
-
cells are grown in basal medium containing 25mM glucose as sole carbon source
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
key enzyme isofloridoside phosphate synthase catalyzes the formation of isofloridoside phosphate from glycerol-3-phosphate and UDP-galactose. The intermediate is dephosphorylated by the isofloridoside phosphate phosphatase reaction to yield isofloridoside
physiological function
-
key enzyme isofloridoside phosphate synthase catalyzes the formation of isofloridoside phosphate from glycerol-3-phosphate and UDP-galactose. The intermediate is dephosphorylated by the isofloridoside phosphate phosphatase reaction to yield isofloridoside
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 117000, calculated from sequence, x * 65400, SDS-PAGE of recombinant protein
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
enzyme appears to exist as an inactive proenzyme which can be activated by incubation of crude cell extracts with endogenous or exogenous proteases
proteolytic modification
-
proteolytic activation mechanism might be the first step in the activation of IFP-synthase after cell shrinkage due to osmotic water loss. About 1 h later when proteolytic activation is no longer evident and the isofloridose pool is almost filled up a second maximum of active IFP-synthase is evident. This type of enzyme exhibits different molecular properties and might by involved in the turnover of the isofloridoside pool
proteolytic modification
-
proteolytic activation mechanism might be the first step in the activation of IFP-synthase after cell shrinkage due to osmotic water loss. About 1 h later when proteolytic activation is no longer evident and the isofloridose pool is almost filled up a second maximum of active IFP-synthase is evident. This type of enzyme exhibits different molecular properties and might by involved in the turnover of the isofloridoside pool
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
a combination of dithioerythritol and bovine serum gamma-globulin stabilizes the enzyme during cell destruction
-
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
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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
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Gasu_26940, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression increases about 25fold by 35°C heat treatment for 30 min and 2fold in presence of 1400 mM NaCl
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kauss, H.; Schobert, B.
First demonstration of UDP-Gal:sn-glycero-3-phosphoric acid 1-alpha-galactosyl-transferase and its possible role in osmoregulation
FEBS Lett.
19
131-135
1971
Poterioochromonas malhamensis
brenda
Kauss, H.; Quader, H.
In vitro activation of a galactosyl transferase involved in the osmotic regulation of Ochromonas
Plant Physiol.
58
295-298
1976
Poterioochromonas malhamensis
brenda
Thomson, K.S.
Purification of UDOgalactose:sn-glycerol-3-phosphate alpha-D-galactosyltransferase from Poterioochromonas malhamensis
Biochim. Biophys. Acta
759
154-159
1983
Poterioochromonas malhamensis
-
brenda
Kauss, H.; Thomson, K.S.; Thomson, M.; Jeblick, W.
Osmotic regulation. Physiological significance of proteolytic and nonproteolytic activation of isofloridoside-phosphate synthase
Plant Physiol.
63
455-459
1979
Poterioochromonas malhamensis, Poterioochromonas malhamensis Peterfi
brenda
Kauss, H.; Thomson, K.S.; Tetour, M.; Jeblick, W.
Proteolytic activation of a galactosyl tranferase involved in osmotic regulation
Plant Physiol.
61
35-37
1978
Poterioochromonas malhamensis
brenda
Pade, N.; Linka, N.; Ruth, W.; Weber, A.P.; Hagemann, M.
Floridoside and isofloridoside are synthesized by trehalose 6-phosphate synthase-like enzymes in the red alga Galdieria sulphuraria
New Phytol.
205
1227-1238
2015
Galdieria sulphuraria (M2Y1U7), Galdieria sulphuraria 074G (M2Y1U7)
brenda
Sun, M.; Zhu, Z.; Chen, J.; Yang, R.; Luo, Q.; Wu, W.; Yan, X.; Chen, H.
Putative trehalose biosynthesis proteins function as differential floridoside-6-phosphate synthases to participate in the abiotic stress response in the red alga Pyropia haitanensis
BMC Plant Biol.
19
325
2019
Pyropia haitanensis (A0A0A7PA46)
brenda
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