A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 22.214.171.1246
View entry in original ENZYME format
View entry in raw text format (no links)
|NDP-glucose + 3-phospho-D-glycerate <=> NDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate|
- 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 catalyzes 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 126.96.36.199.
- The activity is dependent on divalent cations (Mn(2+), Co(2+),
- 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
- The enzyme from Methanococcoides burtonii is strictly specific for
GDP-glucose and 3-phospho-D-glycerate.
- This enzyme catalyzes the first glucosylation step in methylglucose
lipopolysaccharide biosynthesis in mycobacteria.
|PRIAM enzyme-specific profiles||188.8.131.526|
|KEGG Ligand Database for Enzyme Nomenclature||184.108.40.2066|
|IUBMB Enzyme Nomenclature||220.127.116.116|
|MEDLINE||Find literature relating to 18.104.22.1686|
entries corresponding to 2.4.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-