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Literature summary for 4.2.1.28 extracted from

  • Kinoshita, K.; Kawata, M.; Ogura, K.; Yamasaki, A.; Watanabe, T.; Komoto, N.; Hieda, N.; Yamanishi, M.; Tobimatsu, T.; Toraya, T.
    Histidine-alpha143 assists 1,2-hydroxyl group migration and protects radical intermediates in coenzyme B12-dependent diol dehydratase (2008), Biochemistry, 47, 3162-3173.
    View publication on PubMed
Search for more literature for 4.2.1.28

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli Klebsiella oxytoca

Protein Variants

Protein Variants Comment Organism
Halpha143A site-directed mutagenesis, the mutant shows residual activity compared to the wild-type enzyme Klebsiella oxytoca
Halpha143E site-directed mutagenesis, the mutant is inactive and does not form (alphabeta)2 complexes Klebsiella oxytoca
Halpha143K site-directed mutagenesis, the mutant is inactive and does not form (alphabeta)2 complexes Klebsiella oxytoca
Halpha143L site-directed mutagenesis, the mutant shows residual activity compared to the wild-type enzyme Klebsiella oxytoca
Halpha143Q site-directed mutagenesis, the mutant shows residual activity compared to the wild-type enzyme, irreversible inactivation by O2 in the absence of substrate at a much lower rate than the wild type, preference of the Halpha143Q mutant for (R)- and (S)-1,2-propanediols, kinetic parameters for each enantiomer, overview Klebsiella oxytoca

Inhibitors

Inhibitors Comment Organism Structure
O2 irreversible inactivation Klebsiella oxytoca
Propane-1,2-diol mechanism-based inactivation obeying first-order reaction kinetics Klebsiella oxytoca

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic analysis of mutant enzymes, overview Klebsiella oxytoca
0.22
-
 Propane-1,2-diol pH 8.0, 37°C, wild-type enzyme Klebsiella oxytoca
0.26
-
 Cobalamin pH 8.0, 37°C, mutant Halpha143Q Klebsiella oxytoca
0.3
-
 Propane-1,2-diol pH 8.0, 37°C, mutant Halpha143Q Klebsiella oxytoca
0.9
-
 Cobalamin pH 8.0, 37°C, wild-type enzyme Klebsiella oxytoca

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ in the cob(II)alamin cofactor 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
-
-
-

Oxidation Stability

Oxidation Stability Organism
O2 causes irreversible inactivation Klebsiella oxytoca

Reaction

Reaction Comment Organism Reaction ID
propane-1,2-diol = propanal + H2O minimal mechanism for AdoCbl-dependent diol dehydratase involving the cob(II)alamin cofactor and active-site structure of the enzyme, overview Klebsiella oxytoca
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information hydrogen bonding interaction between the hydroxyl group on C2 of substrate and the side chain of residue Hisalpha143 is important not only for catalysis but also for protecting radical intermediates, overview Klebsiella oxytoca ?
-
 ?
propane-1,2-diol
-
 Klebsiella oxytoca propanal + H2O
-
 ?

Synonyms

Synonyms Comment Organism
AdoCbl-dependent diol dehydratase
-
 Klebsiella oxytoca
coenzyme B12-dependent diol dehydratase
-
 Klebsiella oxytoca
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
0.03
-
 Propane-1,2-diol pH 8.0, 37°C, mutant Halpha143L Klebsiella oxytoca
5.1
-
 Propane-1,2-diol pH 8.0, 37°C, mutant Halpha143A Klebsiella oxytoca
121
-
 Propane-1,2-diol pH 8.0, 37°C, mutant Halpha143Q Klebsiella oxytoca
354
-
 Propane-1,2-diol 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
cob(II)alamin dependent on Klebsiella oxytoca