ENZYME entry: EC 3.1.3.85

Accepted Name
Glucosyl-3-phosphoglycerate phosphatase.
Reaction catalysed
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H(2)O <=> 2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Comment(s)
  • The enzyme is involved in biosynthesis of 2-O-(alpha-D- glucopyranosyl)-D-glycerate via the two-step pathway in which EC 2.4.1.266 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 glucosyl-3-phosphoglycerate phosphatase.
  • In vivo the enzyme catalyzes the dephosphorylation of 2-O-(alpha-D- mannopyranosyl)-3-phospho-D-glycerate with lower efficiency.
  • Divalent metal ions (Mg(2+), Mn(2+) or Co(2+)) stimulate activity.
Cross-references
BRENDA3.1.3.85
EC2PDB3.1.3.85
ExplorEnz3.1.3.85
PRIAM enzyme-specific profiles3.1.3.85
KEGG Ligand Database for Enzyme Nomenclature3.1.3.85
IUBMB Enzyme Nomenclature3.1.3.85
IntEnz3.1.3.85
MEDLINEFind literature relating to 3.1.3.85
MetaCyc3.1.3.85
UniProtKB/Swiss-Prot
Q12XX5, GPMPP_METBU;  C0QRP9, GPMPP_PERMH;  

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.1.3.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-