Literature summary for 1.1.1.18 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.

Cloned(Commentary)

Cloned (Comment)	Organism
gene iolG	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Protein Variants	Comment	Organism
K97V	site-directed mutagenesis, inactive mutant	Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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	?	-	?
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

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	gene iolG	-

Reaction

Reaction	Comment	Organism	Reaction ID
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
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	?	-	?
additional information	structure-function analysis, overview	Bacillus subtilis	?	-	?
myo-inositol + NAD+	-	Bacillus subtilis	scyllo-inosose + NADH + H+	-	?
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

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
BsIDH	-	Bacillus subtilis
inositol dehydrogenase	-	Bacillus subtilis
iolG	-	Bacillus subtilis

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Bacillus subtilis

General Information

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