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EC Tree
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-alpha-galactosyltransferase).
Word Map
2.4.1.96
dna-dependent
dna-pk
non-homologous
end-joining
radiosensitivity
dna-pkcs-deficient
rejoin
artemis
prkdc
pikks
rad3-related
dna-pkcs-dependent
The enzyme appears in viruses and cellular organisms
Synonyms
isofloridoside-phosphate synthase,
more
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galactosyltransferase, glycerol 3-phosphate 1alpha-
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galactosyltransferse, uridine diphosphogalactose-glycerol phosphate
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isofloridoside phosphate synthase/phosphatase fusion protein
isofloridoside-phosphate synthase
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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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isofloridoside phosphate synthase/phosphatase fusion protein
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isofloridoside phosphate synthase/phosphatase fusion protein
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UDP-alpha-D-galactose + sn-glycerol 3-phosphate = UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
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hexosyl group transfer
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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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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
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?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
additional information
?
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UDP-alpha-D-galactose + sn-glycerol 3-phosphate
UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
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?
UDP-alpha-D-galactose + sn-glycerol 3-phosphate
UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
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?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
Ochromonas malhamensis
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?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
Ochromonas malhamensis
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?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
Ochromonas malhamensis
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i.e. isofloridoside phosphate
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UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
Ochromonas malhamensis
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enzyme is involved in regulation of osmotic balance in Ochromonas
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?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
Ochromonas malhamensis
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enzyme is involved in regulation of osmotic balance in Ochromonas
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?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
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?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
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?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
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?
additional information
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metabolite analysis by mass spectrometry
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?
additional information
?
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metabolite analysis by mass spectrometry
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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
UDP-alpha-D-galactose + sn-glycerol 3-phosphate
UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
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?
UDP-alpha-D-galactose + sn-glycerol 3-phosphate
UDP + 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate
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?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
Ochromonas malhamensis
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enzyme is involved in regulation of osmotic balance in Ochromonas
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?
UDPgalactose + sn-glycerol 3-phosphate
UDP + alpha-D-galactosyl sn-glycerol 3-phosphate
Ochromonas malhamensis
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enzyme is involved in regulation of osmotic balance in Ochromonas
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?
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additional information
Ochromonas malhamensis
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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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additional information
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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
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0.02
sn-glycerol 3-phosphate
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6 - 9
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about 50% of activity maximum at pH 6 and pH 9
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6
calculated from sequence
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cf. EC 2.4.1.15; gene Gasu_26940
UniProt
brenda
cf. EC 2.4.1.15; gene Gasu_26940
UniProt
brenda
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UniProt
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Ochromonas malhamensis
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brenda
Peterfi
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brenda
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brenda
Peterfi
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brenda
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additional information
cells are grown in basal medium containing 25mM glucose as sole carbon source
brenda
additional information
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cells are grown in basal medium containing 25mM glucose as sole carbon source
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brenda
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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
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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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A0A0A7PA46_NEOHI
1107
0
117053
TrEMBL
Secretory Pathway (Reliability: 2 )
M2Y1U7_GALSU
890
0
101468
TrEMBL
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70000
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1 * 70000, SDS-PAGE
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?
x * 117000, calculated from sequence, x * 65400, SDS-PAGE of recombinant protein
monomer
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1 * 70000, SDS-PAGE
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proteolytic modification
Ochromonas malhamensis
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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
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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
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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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0
Ochromonas malhamensis
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30 min, enzyme in crude extract, 50% loss of activity
30
Ochromonas malhamensis
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almost complete inactivation after some min
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a combination of dithioerythritol and bovine serum gamma-globulin stabilizes the enzyme during cell destruction
Ochromonas malhamensis
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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
Ochromonas malhamensis
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unstable to repeated freezing and thawing
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expression in Escherichia coli
gene Gasu_26940, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree
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expression increases about 25fold by 35°C heat treatment for 30 min and 2fold in presence of 1400 mM NaCl
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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
Ochromonas 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
Ochromonas 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
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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
Ochromonas 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
Neoporphyra haitanensis (A0A0A7PA46)
brenda
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