Literature summary for 1.1.1.18 extracted from

Van Straaten, K.E.; Hoffort, A.; Palmer, D.R.; Sanders, D.A.
Purification, crystallization and preliminary X-ray analysis of inositol dehydrogenase (IDH) from Bacillus subtilis (2008), Acta Crystallogr. Sect. F, 64, 98-101.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of His-tagged native and selenomethionine-labeled enzyme in Escherichia coli	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant His-tagged native and selenomethionine-labeled enzyme, 12 mg/ml wild-type protein in 25 mM Tris, pH 8.0, and 13.8 mg/ml of selenomethionine-labeled enzyme in 20 mM Tris, pH 8.0, and 5 mM DTT, 4°C, modified microbatch method, equal volumes of protein solution and precipitant solution of 0.001 ml, the latter containing 20%w/v PEG 3350, 0.20 M potassium fluoride, pH 8.5-9.0, are mixed, overlaid with a 1:1 mixture of silicone and paraffin oils, X-ray anomalous diffraction structure determination and analysis at 1.75-2.0 A resolution, molecular replacement	Bacillus subtilis

Crystallization (Comment)

Organism

purified recombinant His-tagged native and selenomethionine-labeled enzyme, 12 mg/ml wild-type protein in 25 mM Tris, pH 8.0, and 13.8 mg/ml of selenomethionine-labeled enzyme in 20 mM Tris, pH 8.0, and 5 mM DTT, 4°C, modified microbatch method, equal volumes of protein solution and precipitant solution of 0.001 ml, the latter containing 20%w/v PEG 3350, 0.20 M potassium fluoride, pH 8.5-9.0, are mixed, overlaid with a 1:1 mixture of silicone and paraffin oils, X-ray anomalous diffraction structure determination and analysis at 1.75-2.0 A resolution, molecular replacement

Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
39170	-	x * 39170, His-tagged recombinant enzyme, SDS-PAGE	Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
myo-inositol + NAD+	Bacillus subtilis	first enzyme in the catabolic pathway of myo-inositol	scyllo-inosose + NADH	-	r

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged native and selenomethionine-labeled enzyme from Escherichia coli by nickel affinity chromatography to homogeneity	Bacillus subtilis

Reaction

Reaction	Comment	Organism	Reaction ID
myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+	His176 and Asp172 are proposed to act as the catalytic dyad, in which His176 is proposed to be the acid/base catalyst	Bacillus subtilis	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
myo-inositol + NAD+	first enzyme in the catabolic pathway of myo-inositol	Bacillus subtilis	scyllo-inosose + NADH	-	r
myo-inositol + NAD+	oxidation of the axial hydroxyl group of myo-inositol	Bacillus subtilis	scyllo-inosose + NADH	-	r

Subunits

Subunits	Comment	Organism
?	x * 39170, His-tagged recombinant enzyme, SDS-PAGE	Bacillus subtilis

Synonyms

Synonyms	Comment	Organism
IDH	-	Bacillus subtilis
inositol dehydrogenase	-	Bacillus subtilis
More	IDH is a member of the GFOR/IDH/MocA family	Bacillus subtilis

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Bacillus subtilis
NADH	-	Bacillus subtilis