Home  |  Contact

ENZYME entry: EC

Accepted Name
GDP-4-dehydro-6-deoxy-alpha-D-mannose 3-dehydratase.
Reaction catalysed
GDP-4-dehydro-alpha-D-rhamnose + L-glutamate <=> GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + 2-oxoglutarate + ammonia
  • This enzyme, involved in beta-L-colitose biosynthesis, is a unique vitamin-B6-dependent enzyme.
  • In the first step of catalysis, the bound pyridoxal phosphate (PLP) cafactor is transaminated to the pyridoxamine 5'-phosphate (PMP) form of vitamin B(6), using L-glutamate as the amino group donor.
  • The PMP cofactor then forms a Schiff base with the sugar substrate and the resulting adduct undergoes a 1,4-dehydration to eliminate the 3-OH group.
  • Hydrolysis of the product from the enzyme restores the PLP cofactor and results in the release of an unstable enamine intermediate.
  • This intermediate tautomerizes to form an imine form, which hydrolyzes spontaneously, releasing ammonia and forming the final product.
PRIAM enzyme-specific profiles4.2.1.168
KEGG Ligand Database for Enzyme Nomenclature4.2.1.168
IUBMB Enzyme Nomenclature4.2.1.168
MEDLINEFind literature relating to
Rhea expert-curated reactions4.2.1.168

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 4.2.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.2.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-