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Literature summary for 4.2.1.28 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
Search for more literature for 4.2.1.28

Protein Variants

Protein Variants Comment Organism
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
Kbeta135E site-directed mutagenesis, the mutant shows 98% reduced activity compared to the wild-type enzyme Klebsiella oxytoca
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
Kbeta135R site-directed mutagenesis, the mutant shows 24% reduced activity compared to the wild-type enzyme Klebsiella oxytoca
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
Salpha224N site-directed mutagenesis, the mutant shows 95% reduced activity compared to the wild-type enzyme Klebsiella oxytoca

Inhibitors

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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)

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
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
diol dehydratase
-
 Klebsiella oxytoca

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
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]

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