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Literature summary extracted from

  • van Straaten, K.E.; Zheng, H.; Palmer, D.R.; Sanders, D.A.
    Structural investigation of myo-inositol dehydrogenase from Bacillus subtilis: implications for catalytic mechanism and inositol dehydrogenase subfamily classification (2010), Biochem. J., 432, 237-247.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.18 gene iolG Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.18 purified wild-type BsIDH and K97V mutant in apo-, holo- and ternary complexes with inositol and inosose, mixing of 0.002 ml of protein solution containing 10mg/ml protein in 25 mM Tris pH 8.0, with 0.002 ml reservoir solution containing 0.1-0.2 M tri-sodium citrate, pH 5.4, and 1.6-2.9 M ammonium sulfate, for the holo-enzyme complexes with 0.1 M tri-sodium citrate pH 5.4, 2.6 M ammonium sulfate and either inositol or inosose at 4 mg/0.1 ml mother liquid, cryoprotection with 25% ethylene glycol, X-ray diffraction structure determination and analysis at 2.3 A resolution Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.18 K97V site-directed mutagenesis, inactive mutant 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 additional information Bacillus subtilis the enzyme shows a broad substrate spectrum while remaining highly stereoselective. BsIDH is able to oxidize the mono-saccharides alpha-D-glucose and alpha-D-xylose but not beta-D-glucose, D-mannose and D-galactose ?
-
 ?
1.1.1.18 myo-inositol + NAD+ Bacillus subtilis the NAD+-dependent enzyme catalyses the oxidation of the axial hydroxyl group of myo-inositol to form scyllo-inosose scyllo-inosose + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.18 Bacillus subtilis
-
 gene iolG
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.18 myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ Lys97, Asp172, and His176 are the catalytic triad involved in the catalytic mechanism, overview Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.18 additional information the enzyme shows a broad substrate spectrum while remaining highly stereoselective. BsIDH is able to oxidize the mono-saccharides alpha-D-glucose and alpha-D-xylose but not beta-D-glucose, D-mannose and D-galactose Bacillus subtilis ?
-
 ?
1.1.1.18 additional information structure-function analysis, overview Bacillus subtilis ?
-
 ?
1.1.1.18 myo-inositol + NAD+
-
 Bacillus subtilis scyllo-inosose + NADH + H+
-
 ?
1.1.1.18 myo-inositol + NAD+ the NAD+-dependent enzyme catalyses the oxidation of the axial hydroxyl group of myo-inositol to form scyllo-inosose Bacillus subtilis scyllo-inosose + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.18 tetramer BsIDH is a tetramer, with an arrangement consisting of 2 long continuous beta-sheets, formed from all 4 monomers, in which the central 2 strands are crossed over to form the core of the tetramer. Each subunit in the tetramer consists of two domains, an N-terminal Rossmann fold domain containing the cofactor-binding site, and a C-terminal domain containing the inositol-binding site, structure-function analysis, overview Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
1.1.1.18 BsIDH
-
 Bacillus subtilis
1.1.1.18 inositol dehydrogenase
-
 Bacillus subtilis
1.1.1.18 iolG
-
 Bacillus subtilis

Cofactor

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

General Information

EC Number General Information Comment Organism
1.1.1.18 metabolism inositol dehydrogenase is responsible for the first step in myo-inositol degradation Bacillus subtilis