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Literature summary for 4.2.1.30 extracted from

  • O'Brien, J.R.; Raynaud, C.; Croux, C.; Girbal, L.; Soucaille, P.; Lanzilotta, W.N.
    Insight into the mechanism of the B12-independent glycerol dehydratase from Clostridium butyricum: preliminary biochemical and structural characterization (2004), Biochemistry, 43, 4635-4645.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
glycerol dehydratase-activating enzyme activated the enzyme Clostridium butyricum

Crystallization (Commentary)

Crystallization (Comment) Organism
native, glycerol-bound and 1,2-propanediol-bound forms, capillary batch or hanging drop vapor diffusion method Clostridium butyricum

Protein Variants

Protein Variants Comment Organism
R782K forms a tight protein-protein complex with glycerol dehydratase-activating enzyme Clostridium butyricum

Organism

Organism UniProt Comment Textmining
Clostridium butyricum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
homogeneity, enzyme is inactive after purification, but can be reactivated with glycerol dehydratase-activating enzyme under anaerobic conditions Clostridium butyricum

Reaction

Reaction Comment Organism Reaction ID
glycerol = 3-hydroxypropanal + H2O mechanism Clostridium butyricum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycerol
-
Clostridium butyricum 3-hydroxypropanal + H2O
-
?

Subunits

Subunits Comment Organism
dimer crystallization data Clostridium butyricum