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Literature summary for 4.2.1.28 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
Search for more literature for 4.2.1.28

Inhibitors

Inhibitors Comment Organism Structure
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

Metals/Ions Comment Organism Structure
Ca2+ directly coordinates to substrate and is essential for structural retention and substrate binding Klebsiella oxytoca
K+ activates Klebsiella oxytoca
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)

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

Organism

Organism UniProt Comment Textmining
Klebsiella oxytoca
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
propane-1,2-diol
-
 Klebsiella oxytoca propanal + H2O
-
 ?
propane-1,2-diol substrate binding structure and mechanism, overview Klebsiella oxytoca propanal + H2O
-
 ?

Synonyms

Synonyms Comment Organism
coenzyme B12-dependent diol dehydratase
-
 Klebsiella oxytoca