2.4.1.269: mannosylglycerate synthase
This is an abbreviated version!
For detailed information about mannosylglycerate synthase, go to the full flat file.
Word Map on EC 2.4.1.269
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2.4.1.269
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rhodothermus
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marinus
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mannosyl-3-phosphoglycerate
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glycosyltransferase
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polysaccharides
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hyperthermophile
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glycoconjugates
- 2.4.1.269
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rhodothermus
- marinus
-
mannosyl-3-phosphoglycerate
- glycosyltransferase
- polysaccharides
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hyperthermophile
- glycoconjugates
Reaction
Synonyms
MGS
ECTree
2.4.1.269 mannosylglycerate synthaseAdvanced search results
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Substrates Products on EC 2.4.1.269 - mannosylglycerate synthase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-mannose + glycolic acid
?
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the kcat/KM-value for glycolic acid is 70fold lower than the value for glycolic acid at 25°C
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?
additional information
?
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enzyme is able to efficiently synthesize mannosylglycerate and glucosylglycerate alike
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-
?
GDP-alpha-D-glucose + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + GDP
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the enzyme catalyzes the formation of the stress protectant 2-O-alpha-D-mannosyl glycerate
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-
?
GDP-alpha-D-glucose + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + GDP
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at 37°C mannosylglycerate synthase shows donor flexibility and can use alpha-GDP-D-Man, alpha-GDP-D-Glc, beta-GDP-L-fucose, alpha-UDP-D-Man and alpha-UDP-D-Glc, but not Man-1-P, as substrates. The kcat/KM-value for GDP-glucose is 2.5fold lower than the value for GDP-mannose at 25°C. The kcat/KM-value for GDP-glucose is 8.6fold lower than the value for GDP-mannose at 65°C
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-
?
GDP-alpha-D-glucose + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + GDP
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-
-
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?
GDP-mannose + D-glycerate
2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP
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-
-
?
GDP-mannose + D-glycerate
2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP
Rhodothermus marinus possesses two enzymatic systems for the synthesis of mannosylglycerate. The first one is a single-step pathway in which mannosylglycerate synthase catalyses the synthesis of 2-O-(alpha-D-mannopyranosyl)-D-glycerate in one-step from GDP-mannose and D-glycerate. The second system is a two-step pathway in which mannosyl-3-phosphoglycerate synthase (EC 2.4.1.217) catalyses the conversion of GDP-mannose and 3-phospho-D-glycerate into 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-mannopyranosyl)-D-glycerate by mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
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-
?
GDP-mannose + D-glycerate
2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP
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at 37°C mannosylglycerate synthase shows donor flexibility and can use alpha-GDP-D-Man, alpha-GDP-D-Glc, beta-GDP-L-fucose, alpha-UDP-D-Man and alpha-UDP-D-Glc, but not Man-1-P, as substrates. The kcat/KM-value for GDP-glucose is 2.5fold lower than the value for GDP-mannose at 25°C. The kcat/KM-value for GDP-glucose is 8.6fold lower than the value for GDP-mannose at 65°C
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-
?
GDP-mannose + D-glycerate
2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP
the enzyme is specific for GDP-mannose and D-glycerate. The enzyme shows no activity for the reverse reaction. No activity with: ADP-mannose, UDP-mannose (less than 3% of that of GDP mannose), GDP-glucose, UDP-glucose, ADP-glucose, mannose 1-phosphate, and mannose 6-phosphate as sugar donors, and L-glycerate, glycerol 3-phosphate, glucose 6-phosphate, glucose 1-phosphate and D-3-phosphoglycerate as sugar acceptors
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ir
GDP-mannose + D-glycerate
2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP
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-
-
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?
GDP-mannose + D-lactate
?
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the kcat/KM-value for D-lactate is 70fold lower than the value for D-glycerate at 25°C
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?
