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Literature summary extracted from

  • Ogura, K.; Kunita, S.; Mori, K.; Tobimatsu, T.; Toraya, T.
    Roles of adenine anchoring and ion pairing at the coenzyme B12-binding site in diol dehydratase catalysis (2008), FEBS J., 275, 6204-6216.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.28 Kbeta135A site-directed mutagenesis, the mutant shows 42% reduced activity compared to the wild-type enzyme, the mutant is less sensitive to inhibitor CN-cobalamin Klebsiella oxytoca
4.2.1.28 Kbeta135E site-directed mutagenesis, the mutant shows 98% reduced activity compared to the wild-type enzyme Klebsiella oxytoca
4.2.1.28 Kbeta135Q site-directed mutagenesis, the mutant shows 27% reduced activity compared to the wild-type enzyme, the mutant is less sensitive to inhibitor CN-cobalamin Klebsiella oxytoca
4.2.1.28 Kbeta135R site-directed mutagenesis, the mutant shows 24% reduced activity compared to the wild-type enzyme Klebsiella oxytoca
4.2.1.28 Salpha224A site-directed mutagenesis, the mutant shows 81% reduced activity compared to the wild-type enzyme, mechanism-based complete inactivation of the Salpha224A holoenzyme during catalysis by propan-1,2-diol leading to accumulation of cobalamin, mechanism, overview Klebsiella oxytoca
4.2.1.28 Salpha224N site-directed mutagenesis, the mutant shows 95% reduced activity compared to the wild-type enzyme Klebsiella oxytoca

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.28 CN-cobalamin
-
 Klebsiella oxytoca
4.2.1.28 Propane-1,2-diol leads to inactivation of wild-type and mutant enzymes during catalysis, kinetics, overview Klebsiella oxytoca

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.28 0.12
-
 Propan-1,2-diol pH 8.0, 37°C, mutant Kbeta135R Klebsiella oxytoca
4.2.1.28 0.15
-
 Propan-1,2-diol pH 8.0, 37°C, wild-type enzyme and mutant Salpha224A Klebsiella oxytoca
4.2.1.28 0.39
-
 Propan-1,2-diol pH 8.0, 37°C, mutant Kbeta135A and mutant Kbeta135Q Klebsiella oxytoca
4.2.1.28 0.4
-
 Propan-1,2-diol pH 8.0, 37°C, mutant Kbeta135E Klebsiella oxytoca
4.2.1.28 1.9
-
 Propan-1,2-diol pH 8.0, 37°C, mutant Salpha224N Klebsiella oxytoca

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.28 Co2+ in the cobalamin cofactor, presence of a positive charge at the beta135 residue increases the affinity for cobalamins but is not essential for catalysis, and the introduction of a negative charge there prevents the enzyme-cobalamin interaction 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
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.28 propane-1,2-diol
-
 Klebsiella oxytoca propanal + H2O
-
 ?
4.2.1.28 propane-1,2-diol Co-C bond formation during reaction Klebsiella oxytoca propanal + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.28 diol dehydratase
-
 Klebsiella oxytoca

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.28 37
-
 assay at Klebsiella oxytoca

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.28 7.7
-
 CN-cobalamin pH 8.0, 37°C, mutant Kbeta135E Klebsiella oxytoca
4.2.1.28 17
-
 CN-cobalamin pH 8.0, 37°C, mutant Salpha224A Klebsiella oxytoca
4.2.1.28 64
-
 CN-cobalamin pH 8.0, 37°C, mutant Kbeta135R Klebsiella oxytoca
4.2.1.28 196
-
 CN-cobalamin pH 8.0, 37°C, mutant Kbeta135A Klebsiella oxytoca
4.2.1.28 211
-
 CN-cobalamin pH 8.0, 37°C, mutant Kbeta135Q Klebsiella oxytoca
4.2.1.28 254
-
 CN-cobalamin pH 8.0, 37°C, mutant Salpha224N Klebsiella oxytoca
4.2.1.28 336
-
 CN-cobalamin pH 8.0, 37°C, wild-type enzyme Klebsiella oxytoca

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.28 8
-
 assay at Klebsiella oxytoca

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.28 Cobalamin roles of adenine anchoring and ion pairing at the coenzyme B12-binding site, overview. Presence of a positive charge at the beta135 residue increases the affinity for cobalamins but is not essential for catalysis, and the introduction of a negative charge there prevents the enzyme-cobalamin interaction Klebsiella oxytoca

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.2.1.28 0.00014
-
 CN-cobalamin pH 8.0, 37°C, mutant Kbeta135A Klebsiella oxytoca
4.2.1.28 0.00051
-
 CN-cobalamin pH 8.0, 37°C, mutant Kbeta135R Klebsiella oxytoca
4.2.1.28 0.00063
-
 CN-cobalamin pH 8.0, 37°C, mutant Salpha224A Klebsiella oxytoca
4.2.1.28 0.0015
-
 CN-cobalamin pH 8.0, 37°C, wild-type enzyme Klebsiella oxytoca
4.2.1.28 0.0023
-
 CN-cobalamin pH 8.0, 37°C, mutant Salpha224N Klebsiella oxytoca
4.2.1.28 0.0044
-
 CN-cobalamin pH 8.0, 37°C, mutant Kbeta135Q Klebsiella oxytoca
4.2.1.28 0.463
-
 CN-cobalamin pH 8.0, 37°C, mutant Kbeta135E Klebsiella oxytoca