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Literature summary extracted from

  • Daniellou, R.; Zheng, H.; Langill, D.M.; Sanders, D.A.; Palmer, D.R.
    Probing the promiscuous active site of myo-inositol dehydrogenase using synthetic substrates, homology modeling, and active site modification (2007), Biochemistry, 46, 7469-7477.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.18 D172N site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Bacillus subtilis
1.1.1.18 H176A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Bacillus subtilis
1.1.1.18 Y233F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Bacillus subtilis
1.1.1.18 Y233R site-directed mutagenesis, inactive mutant Bacillus subtilis
1.1.1.18 Y235F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Bacillus subtilis
1.1.1.18 Y235R site-directed mutagenesis, inactive mutant Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.18 diethyl dicarbonate inactivation Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.18 0.07
-
 NAD+ pH 9.0, 25°C, recombinant mutant Y233F Bacillus subtilis
1.1.1.18 0.08
-
 NAD+ pH 9.0, 25°C, recombinant wild-type enzyme Bacillus subtilis
1.1.1.18 0.11
-
 NAD+ pH 9.0, 25°C, recombinant mutant Y235F Bacillus subtilis
1.1.1.18 0.3
-
 NAD+ pH 9.0, 25°C, recombinant mutant H176A Bacillus subtilis
1.1.1.18 0.4
-
 NAD+ pH 9.0, 25°C, recombinant mutant D179N Bacillus subtilis
1.1.1.18 1.1
-
 NAD+ pH 9.0, 25°C, recombinant mutant D172N Bacillus subtilis
1.1.1.18 4
-
 myo-inositol pH 9.0, 25°C, recombinant mutant Y233F Bacillus subtilis
1.1.1.18 4.4
-
 myo-inositol pH 9.0, 25°C, recombinant wild-type enzyme Bacillus subtilis
1.1.1.18 28
-
 myo-inositol pH 9.0, 25°C, recombinant mutant D179N Bacillus subtilis
1.1.1.18 39
-
 myo-inositol pH 9.0, 25°C, recombinant mutant Y235F Bacillus subtilis
1.1.1.18 65
-
 myo-inositol pH 9.0, 25°C, recombinant mutant D172N Bacillus subtilis
1.1.1.18 118
-
 myo-inositol pH 9.0, 25°C, recombinant mutant H176A Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.18 myo-inositol + NAD+ Bacillus subtilis
-
 scyllo-inosose + NADH
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.18 Bacillus subtilis P26935
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.18 myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ ordered sequential Bi-Bi mechanism in the absence of products, residues Y233, Y235, H176, and D172 are important for activity Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.18 4-methylbenzenesulfonyl-myo-inositol + NAD+
-
 Bacillus subtilis ? + NADH + H+
-
 ?
1.1.1.18 4-O-((1S)-10-camphor-sulfonyl)-myo-inositol + NAD+
-
 Bacillus subtilis ? + NADH + H+
-
 ?
1.1.1.18 4-O-((4-methyloxycarbonyl)-benzyl)-myo-inositol + NAD+
-
 Bacillus subtilis ? + NADH + H+
-
 ?
1.1.1.18 4-O-(4-carboxybenzyl)-myo-inositol + NAD+
-
 Bacillus subtilis ? + NADH + H+
-
 ?
1.1.1.18 4-O-(trans-cinnamoyl)-myo-inositol + NAD+
-
 Bacillus subtilis ? + NADH + H+
-
 ?
1.1.1.18 4-O-allyl-myo-inositol + NAD+
-
 Bacillus subtilis ? + NADH + H+
-
 ?
1.1.1.18 4-O-alpha-D-glucopyranosyl-myo-inositol + NAD+
-
 Bacillus subtilis ? + NADH + H+
-
 ?
1.1.1.18 4-O-benzyl-myo-inositol + NAD+
-
 Bacillus subtilis ? + NADH + H+
-
 ?
1.1.1.18 4-O-methyl-myo-inositol + NAD+
-
 Bacillus subtilis ? + NADH + H+
-
 ?
1.1.1.18 4-O-[(2-methylphenyl)methyl]-myo-inositol + NAD+
-
 Bacillus subtilis ? + NADH + H+
-
 ?
1.1.1.18 4-O-[(3-methylphenyl)methyl]-myo-inositol + NAD+
-
 Bacillus subtilis ? + NADH + H+
-
 ?
1.1.1.18 additional information substrate specificity and substrate binding structure, molecular modeling, overview Bacillus subtilis ?
-
 ?
1.1.1.18 myo-inositol + NAD+
-
 Bacillus subtilis scyllo-inosose + NADH
-
 r
1.1.1.18 myo-inositol + NAD+
-
 Bacillus subtilis scyllo-inosose + NADH + H+
-
 ?
1.1.1.18 [(4-methylphenyl)methyl]-myo-inositol + NAD+
-
 Bacillus subtilis ? + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.18 More construction of an homology model of inositol dehydrogenase, to which NADH and 4-O-benzylscyllo-inosose are docked and the active site energy minimized, molecular modeling, overview Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
1.1.1.18 IDH
-
 Bacillus subtilis
1.1.1.18 myo-inositol dehydrogenase
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.18 25
-
 assay at Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.18 0.23
-
 myo-inositol pH 9.0, 25°C, recombinant mutant H176A Bacillus subtilis
1.1.1.18 1.9
-
 myo-inositol pH 9.0, 25°C, recombinant mutant D172N Bacillus subtilis
1.1.1.18 34
-
 myo-inositol pH 9.0, 25°C, recombinant mutant Y235F Bacillus subtilis
1.1.1.18 47
-
 myo-inositol pH 9.0, 25°C, recombinant mutant Y233F Bacillus subtilis
1.1.1.18 58
-
 myo-inositol pH 9.0, 25°C, recombinant wild-type enzyme Bacillus subtilis
1.1.1.18 73
-
 myo-inositol pH 9.0, 25°C, recombinant mutant D179N Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.18 9
-
 assay at Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.18 NAD+
-
 Bacillus subtilis
1.1.1.18 NADH
-
 Bacillus subtilis