2.4.1.266: glucosyl-3-phosphoglycerate synthase

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For detailed information about glucosyl-3-phosphoglycerate synthase, go to the full flat file.

Word Map on EC 2.4.1.266

2.4.1.266

mycobacteria

tuberculosis

glucosylglycerate

glycosyltransferase

lipopolysaccharide

methylglucose

gg

d-3-phosphoglycerate

gdp-mannose

planctomycetes

udp

phylum

burtonii

methylmannose

marina

deep-branching

smegmatis

mannosyl-3-phosphoglycerate

methanococcoides

mobilis

petrotoga

gdp-glucose

glucosylation

Reaction

2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate

Synonyms

glucosyl-3-phosphoglycerate synthase, glucosyl-3-phosphoglycerate synthase/phosphatase, glucosylphosphoglycerate synthase, GpgS, GpgS protein, GpgS/P, More, MSMEG_5084, RB1005, Rv1208 protein

ECTree

2 Transferases

2.4 Glycosyltransferases

2.4.1 Hexosyltransferases

2.4.1.266 glucosyl-3-phosphoglycerate synthase

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Results	in table
1807	AA Sequence
13	Cloned(Commentary)
3	Crystallization (Commentary)
7	General Information
7	Inhibitors
10	kcat/KM [mM/s]
3	Ki Value [mM]
41	KM Value [mM]
24	Metals/Ions
11	Molecular Weight [Da]
10	Natural Substrates/ Products (Substrates)
222	Organism
4	Pathway
13	PDB ID
9	pH Optimum
7	pH Range
1	pH Stability
1	pI Value
12	Protein Variants
8	Purification (Commentary)
6	Reaction
27	Reference
9	Specific Activity [micromol/min/mg]
6	Storage Stability
68	Substrates and Products (Substrate)
12	Subunits
47	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
8	Temperature Range [°C]
14	Temperature Stability [°C]
5	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 2.4.1.266 - glucosyl-3-phosphoglycerate synthase

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NDP-glucose:3-phospho-D-glycerate 2-alpha-D-glucosyltransferase

The enzyme is involved in biosynthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate via the two-step pathway in which glucosyl-3-phosphoglycerate synthase catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-glucopyranosyl)-D-glycerate by EC 3.1.3.85 glucosyl-3-phosphoglycerate phosphatase. The activity is dependent on divalent cations (Mn2+, Co2+, or Mg2+). The enzyme from Persephonella marina shows moderate flexibility on the sugar donor concerning the nucleotide moiety (UDP-glucose, ADP-glucose, GDP-glucose) but is strictly specific for glucose. The enzyme is also strictly specific for 3-phospho-D-glycerate as acceptor [1]. The enzyme from Methanococcoides burtonii is strictly specific for GDP-glucose and 3-phospho-D-glycerate [2]. This enzyme catalyses the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria [4,5].