Information on EC 2.4.1.270 - mannosylglucosyl-3-phosphoglycerate synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.270
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RECOMMENDED NAME
GeneOntology No.
mannosylglucosyl-3-phosphoglycerate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate = GDP + 2-O-[2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl]-3-phospho-D-glycerate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mannosylglucosylglycerate biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
GDP-mannose:2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate 2-O-alpha-D-mannosyltransferase
The enzyme is involved in synthesis of 2-[2-O-(alpha-D-mannopranosyl)-alpha-D-glucopyranosyl]-D-glycerate. Petrotoga miotherma and Petrotoga mobilis accumulate this compound in response to water stress imposed by salt.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
ADP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
GDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
UDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
UDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
additional information
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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
GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
GDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
A9BHJ0
the enzyme is involved in the phosphorylating pathway for synthesis of the solute mannosylglucosylglycerate. In Petrotoga mobilis two alternative pathways for the synthesis of the rare solute mannosylglucosylglycerate are proposed. The first one is a a phosphorylating pathway (with a phosphorylated intermediate) from 3-phosphoglycerate and UDP-glucose to the final solute. The second nonphosphorylating pathway (no phosphorylated intermediates) could represent an alternative route for the synthesis of mannosylglucosylglycerate in Petrotoga mobilis that could lead to the direct conversion of glucosylglycerate and GDP-mannose to mannosylglucosylglycerate. Pathway multiplicity likely reflects a crucial role for mannosylglucosylglycerate in the physiology of Petrotoga mobilis mobilis during stress adaptation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
not strictly dependent on divalent cations, but the presence of 1 mM Mn2+, Ca2+, Mg2+, or Co2+ stimulates its activity in this order of efficiency
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41 - 0.8
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
0.28 - 1
GDP-mannose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.57
substrate ADP-mannose, pH 7.5, 25C
1.72
substrate UDP-mannose, pH 7.5, 25C
3.1
substrate GDP-mannose, pH 7.5, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
pH 6.0: about 50% of maximal activity, pH 10.0: about 75% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
40% of maximum activity
60 - 95
60C: about 50% of maximal activity, 95C: about 70% of maximal activity
90
18% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51000
gel filtration
121900
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 59000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
half-life 38.5 h
40
half-life 52.8 min
60
half-life: 99 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli