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Literature summary extracted from

  • Toraya, T.; Honda, S.; Mori, K.
    Coenzyme B12-dependent diol dehydratase is a potassium ion-requiring calcium metalloenzyme: evidence that the substrate-coordinated metal ion is calcium (2010), Biochemistry, 49, 7210-7217.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.28 overexpression in Escherichia coli strain JM109 Klebsiella oxytoca

General Stability

EC Number General Stability Organism
4.2.1.28 calcium-deprived apoenzyme is unstable when incubated at 37°C in the absence of both Ca2+ and substrate Klebsiella oxytoca

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.28 EDTA EDTA inhibition of apoenzyme is reversible at least in the initial phase Klebsiella oxytoca
4.2.1.28 EGTA
-
 Klebsiella oxytoca
4.2.1.28 additional information no inhibition by 5 mM of 1,10-phenanthroline, 2,2'-dipyridyl, citrate, succinate, tartrate, malate, and salicylate Klebsiella oxytoca

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.28 Ca2+ 1.6-1.9 mol/mol of enzyme. CaCl2 and substrate show not only a stabilizing effect but also some activating effect of about 30% Klebsiella oxytoca
4.2.1.28 Cr2+ 0.10 mol/mol of enzyme Klebsiella oxytoca
4.2.1.28 Cu2+ 0.16 mol/mol of enzyme Klebsiella oxytoca
4.2.1.28 Fe2+ 0.09 mol/mol of enzyme Klebsiella oxytoca
4.2.1.28 K+ selectively activates diol dehydratase Klebsiella oxytoca
4.2.1.28 Mg2+ 0.19-0.26 mol/mol of enzyme Klebsiella oxytoca
4.2.1.28 Mn2+ 0.09 mol/mol of enzyme Klebsiella oxytoca
4.2.1.28 additional information no requirements of divalentmetal ions for catalysis, metal contents in purified recombinant enzyme Klebsiella oxytoca
4.2.1.28 NH4+ selectively activates diol dehydratase Klebsiella oxytoca
4.2.1.28 Zn2+ 0.12 mol/mol of enzyme Klebsiella oxytoca

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.28 207300
-
-
 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
-
 ?
4.2.1.28 propane-1,2-diol Klebsiella oxytoca ATCC 8724
-
 propanal + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.28 Klebsiella oxytoca
-
-
-
4.2.1.28 Klebsiella oxytoca ATCC 8724
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
4.2.1.28 reconstitution of calcium-containing apoenzyme from calcium-deprived apoenzyme and Ca2+, overview Klebsiella oxytoca

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.1.28 additional information ATCC8724 cells grown without aeration in glycerol-1,2-propanediol medium 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
-
 Klebsiella oxytoca ATCC 8724 propanal + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.28 adenosylcobalamin-dependent diol dehydratase
-
 Klebsiella oxytoca
4.2.1.28 AdoCbl-dependent diol dehydratase
-
 Klebsiella oxytoca
4.2.1.28 coenzyme B12-dependent diol dehydratase
-
 Klebsiella oxytoca
4.2.1.28 diol dehydratase
-
 Klebsiella oxytoca
4.2.1.28 DL-1,2-propanediol hydrolyase
-
 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

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 adenosylcobalamin i.e. coenzyme B12 or AdoCbl, dependent on Klebsiella oxytoca