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Literature summary for 4.2.1.28 extracted from

  • Toraya, T.
    Radical catalysis of B12 enzymes: structure, mechanism, inactivation, and reactivation of diol and glycerol dehydratases (2000), Cell. Mol. Life Sci., 57, 106-127.
    View publication on PubMed
Search for more literature for 4.2.1.28

Activating Compound

Activating Compound Comment Organism Structure
ATP
-
 Klebsiella pneumoniae
ATP
-
 Klebsiella oxytoca

Organism

Organism UniProt Comment Textmining
Klebsiella oxytoca
-
-
-
Klebsiella pneumoniae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
propane-1,2-diol = propanal + H2O enzymatic radical catalysis, with adenosylcobalamin, coenzyme B12, as a cofactor. Dehydration of 1,2-diols to the corresponding aldehydes. The substrate and an essential potassium ion are located inside a betaalpha8 barrel. Two hydroxyl groups of the substrate coordinate directly to the potassium ion which binds to the negatively charged inner part of the cavity. Cobalamin bound covers the cavity to isolate the active site from the solvent. The initial migration of the hydroxyl group is stereospecific and the dehydration of a gem-diol undergoes steric control by the enzyme Klebsiella pneumoniae
a
propane-1,2-diol = propanal + H2O enzymatic radical catalysis, with adenosylcobalamin, coenzyme B12, as a cofactor. Dehydration of 1,2-diols to the corresponding aldehydes. The substrate and an essential potassium ion are located inside a betaalpha8 barrel. Two hydroxyl groups of the substrate coordinate directly to the potassium ion which binds to the negatively charged inner part of the cavity. Cobalamin bound covers the cavity to isolate the active site from the solvent. The initial migration of the hydroxyl group is stereospecific and the dehydration of a gem-diol undergoes steric control by the enzyme Klebsiella oxytoca
a

Subunits

Subunits Comment Organism
More dimer of a heterotrimer, alphabetagamma2. The enzyme dissociates into two dissimilar protein components, F and S, upon DEAE-cellulose chromatography in the absence of substrate, which are identified as the monomeric beta subunit and the trimeric alpha2gamma2 complex, respectively Klebsiella pneumoniae
More dimer of a heterotrimer, alphabetagamma2. The enzyme dissociates into two dissimilar protein components, F and S, upon DEAE-cellulose chromatography in the absence of substrate, which are identified as the monomeric beta subunit and the trimeric alpha2gamma2 complex, respectively Klebsiella oxytoca

Cofactor

Cofactor Comment Organism Structure
coenzyme B12 adenosylcobalamin. Glycerol-inactivated and oxygen inactivated enzyme undergoes rapid reactivation in the presence of the cofactor, ATP and Mg2+ Klebsiella pneumoniae
coenzyme B12 adenosylcobalamin. Glycerol-inactivated and oxygen inactivated enzyme undergoes rapid reactivation in the presence of the cofactor, ATP and Mg2+ Klebsiella oxytoca