Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.1.28 ATP
-
 Klebsiella pneumoniae
4.2.1.28 ATP
-
 Klebsiella oxytoca
4.2.1.30 GdrA GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin, the reactivating factor mediates ATP-dependent exchange of the enzyme-bound, adenine-lacking cobalamin, for free adenosylcobalamin, an adenine-containing cobalamin, through intermediary formation of apoenzyme in the presence of ATP and Mg2+ Klebsiella pneumoniae
4.2.1.30 GdrA GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin, the reactivating factor mediates ATP-dependent exchange of the enzyme-bound, adenine-lacking cobalamin, for free adenosylcobalamin, an adenine-containing cobalamin, through intermediary formation of apoenzyme in the presence of ATP and Mg2+ Klebsiella oxytoca
4.2.1.30 GdrB GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin, the reactivating factor mediates ATP-dependent exchange of the enzyme-bound, adenine-lacking cobalamin, for free adenosylcobalamin, an adenine-containing cobalamin, through intermediary formation of apoenzyme in the presence of ATP and Mg2+ Klebsiella pneumoniae
4.2.1.30 GdrB GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin, the reactivating factor mediates ATP-dependent exchange of the enzyme-bound, adenine-lacking cobalamin, for free adenosylcobalamin, an adenine-containing cobalamin, through intermediary formation of apoenzyme in the presence of ATP and Mg2+ Klebsiella oxytoca

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.30 glycerol irreversible cleavage of the Co-C bond, forming 5'-deoxyadenosine and an unknown cobalamin species. The unknown cobalamin species is converted very slowly to OH-cobalamin. The cobalamin species that is formed remains tightly bound to the enzyme, inactivating the enzyme irreversibly Klebsiella oxytoca
4.2.1.30 glycerol irreversible cleavage of the Co-C bond, forming 5'-deoxyadenosine and an unknown cobalamin species. The unknown cobalamin species is converted very slowly to OH-cobalamin. The cobalamin species that is formed remains tightly bound to the enzyme, inactivating the enzyme irreversibly Klebsiella pneumoniae

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.28 Klebsiella oxytoca
-
-
-
4.2.1.28 Klebsiella pneumoniae
-
-
-
4.2.1.30 Klebsiella oxytoca
-
-
-
4.2.1.30 Klebsiella pneumoniae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.28 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
4.2.1.28 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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.30 glycerol
-
 Klebsiella pneumoniae 3-hydroxypropanal + H2O
-
 ?
4.2.1.30 glycerol
-
 Klebsiella oxytoca 3-hydroxypropanal + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.28 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
4.2.1.28 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

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