Literature summary 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.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.1.1.18 |
X-ray diffraction structure determination and analysis of enzyme mutant A12K/D35S/V36R complex with NADP+ |
Bacillus subtilis |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.1.1.18 |
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 |
1.1.1.18 |
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 |
1.1.1.18 |
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)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.1.1.18 |
myo-inositol + NAD+ |
Bacillus subtilis |
- |
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ |
i.e. scyllo-inosose |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.1.1.18 |
Bacillus subtilis |
P26935 |
- |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.1.1.18 |
myo-inositol + NAD+ |
- |
Bacillus subtilis |
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ |
i.e. scyllo-inosose |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.1.1.18 |
IDH |
- |
Bacillus subtilis |
1.1.1.18 |
myo-inositol dehydrogenase |
- |
Bacillus subtilis |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.1.1.18 |
NAD+ |
strictly dependent on |
Bacillus subtilis |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.1.1.18 |
evolution |
the enzyme is related to the GFO/MocA/IDH family of dehydrogenases |
Bacillus subtilis |