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Literature summary for 1.1.1.18 extracted from

  • Zheng, H.; Bertwistle, D.; Sanders, D.A.; Palmer, D.R.
    Converting NAD-specific inositol dehydrogenase to an efficient NADP-selective catalyst, with a surprising twist (2013), Biochemistry, 52, 5876-5883.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray diffraction structure determination and analysis of enzyme mutant A12K/D35S/V36R complex with NADP+ Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
A12K/D35S/V36R site-directed mutagenesis, the triple mutant has a value of 570000 M/s in reaction with NADP+, higher than that of the wild-type IDH with NAD+. The binding of the coenzyme in the mutant is altered such that although the nicotinamide ring maintains the required position for catalysis, the coenzyme has twisted by nearly 90°, so the adenine moiety no longer binds to a hydrophobic cleft in the Rossmann fold as in the wild-type enzyme Bacillus subtilis
D35S/V36R site-directed mutagenesis, the double mutant prefers NADP+ to NAD+ by a factor of 5. The mutant is an excellent catalyst with a second-order rate constant with respect to NADP of 370000 M/s Bacillus subtilis
additional information convertion of NAD+-specific inositol dehydrogenase to an efficient NADP+-selective catalyst to enhance understanding of coenzyme selectivity and to create an enzyme capable of recycling NADP+ in biocatalytic processes Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
myo-inositol + NAD+ Bacillus subtilis
-
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ i.e. scyllo-inosose ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P26935
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
myo-inositol + NAD+
-
Bacillus subtilis 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ i.e. scyllo-inosose ?

Synonyms

Synonyms Comment Organism
IDH
-
Bacillus subtilis
myo-inositol dehydrogenase
-
Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
NAD+ strictly dependent on Bacillus subtilis

General Information

General Information Comment Organism
evolution the enzyme is related to the GFO/MocA/IDH family of dehydrogenases Bacillus subtilis