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Literature summary extracted from

  • Kamachi, T.; Doitomi, K.; Takahata, M.; Toraya, T.; Yoshizawa, K.
    Catalytic roles of the metal ion in the substrate-binding site of coenzyme B12-dependent diol dehydratase (2011), Inorg. Chem., 50, 2944-2952.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.28 additional information Asp335 has a strong anticatalytic effect on the OH group migration despite its important role in substrate binding. The synergistic interplay of the O-C bond cleavage by Ca2+ ion and the deprotonation of the spectator OH-group by Glu170 is required to overcome the anticatalytic effect of Asp335 Klebsiella oxytoca

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.28 Ca2+ directly coordinates to substrate and is essential for structural retention and substrate binding Klebsiella oxytoca
4.2.1.28 K+ activates Klebsiella oxytoca
4.2.1.28 additional information the activation energy for the OH group migration, which is essential in the conversion of diols to corresponding aldehydes, is sensitive to the identity of the metal ion Klebsiella oxytoca

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.28 propane-1,2-diol Klebsiella oxytoca
-
 propanal + H2O
-
 ?

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.28 propane-1,2-diol = propanal + H2O reaction mechanism, quantum mechanical/molecular mechanical, QM/MM, modeling of diol dehydratase based on the crystal structure of diol dehydratase-adeninylpentylcobalamin complex, overview. The hydrogen recombination is the rate-determining step for the overall reaction Klebsiella oxytoca
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.28 additional information Asp335 has a strong anticatalytic effect on the OH group migration despite its important role in substrate binding. The synergistic interplay of the O-C bond cleavage by Ca2+ ion and the deprotonation of the spectator OH-group by Glu170 is required to overcome the anticatalytic effect of Asp335 Klebsiella oxytoca ?
-
 ?
4.2.1.28 propane-1,2-diol
-
 Klebsiella oxytoca propanal + H2O
-
 ?
4.2.1.28 propane-1,2-diol substrate binding structure and mechanism, overview Klebsiella oxytoca propanal + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.28 coenzyme B12-dependent diol dehydratase
-
 Klebsiella oxytoca