Protein Variants | Comment | Organism |
---|---|---|
D172N | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Bacillus subtilis |
H176A | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Bacillus subtilis |
Y233F | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Bacillus subtilis |
Y233R | site-directed mutagenesis, inactive mutant | Bacillus subtilis |
Y235F | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Bacillus subtilis |
Y235R | site-directed mutagenesis, inactive mutant | Bacillus subtilis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
diethyl dicarbonate | inactivation | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.07 | - |
NAD+ | pH 9.0, 25°C, recombinant mutant Y233F | Bacillus subtilis | |
0.08 | - |
NAD+ | pH 9.0, 25°C, recombinant wild-type enzyme | Bacillus subtilis | |
0.11 | - |
NAD+ | pH 9.0, 25°C, recombinant mutant Y235F | Bacillus subtilis | |
0.3 | - |
NAD+ | pH 9.0, 25°C, recombinant mutant H176A | Bacillus subtilis | |
0.4 | - |
NAD+ | pH 9.0, 25°C, recombinant mutant D179N | Bacillus subtilis | |
1.1 | - |
NAD+ | pH 9.0, 25°C, recombinant mutant D172N | Bacillus subtilis | |
4 | - |
myo-inositol | pH 9.0, 25°C, recombinant mutant Y233F | Bacillus subtilis | |
4.4 | - |
myo-inositol | pH 9.0, 25°C, recombinant wild-type enzyme | Bacillus subtilis | |
28 | - |
myo-inositol | pH 9.0, 25°C, recombinant mutant D179N | Bacillus subtilis | |
39 | - |
myo-inositol | pH 9.0, 25°C, recombinant mutant Y235F | Bacillus subtilis | |
65 | - |
myo-inositol | pH 9.0, 25°C, recombinant mutant D172N | Bacillus subtilis | |
118 | - |
myo-inositol | pH 9.0, 25°C, recombinant mutant H176A | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
myo-inositol + NAD+ | Bacillus subtilis | - |
scyllo-inosose + NADH | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | P26935 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ | ordered sequential Bi-Bi mechanism in the absence of products, residues Y233, Y235, H176, and D172 are important for activity | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-methylbenzenesulfonyl-myo-inositol + NAD+ | - |
Bacillus subtilis | ? + NADH + H+ | - |
? | |
4-O-((1S)-10-camphor-sulfonyl)-myo-inositol + NAD+ | - |
Bacillus subtilis | ? + NADH + H+ | - |
? | |
4-O-((4-methyloxycarbonyl)-benzyl)-myo-inositol + NAD+ | - |
Bacillus subtilis | ? + NADH + H+ | - |
? | |
4-O-(4-carboxybenzyl)-myo-inositol + NAD+ | - |
Bacillus subtilis | ? + NADH + H+ | - |
? | |
4-O-(trans-cinnamoyl)-myo-inositol + NAD+ | - |
Bacillus subtilis | ? + NADH + H+ | - |
? | |
4-O-allyl-myo-inositol + NAD+ | - |
Bacillus subtilis | ? + NADH + H+ | - |
? | |
4-O-alpha-D-glucopyranosyl-myo-inositol + NAD+ | - |
Bacillus subtilis | ? + NADH + H+ | - |
? | |
4-O-benzyl-myo-inositol + NAD+ | - |
Bacillus subtilis | ? + NADH + H+ | - |
? | |
4-O-methyl-myo-inositol + NAD+ | - |
Bacillus subtilis | ? + NADH + H+ | - |
? | |
4-O-[(2-methylphenyl)methyl]-myo-inositol + NAD+ | - |
Bacillus subtilis | ? + NADH + H+ | - |
? | |
4-O-[(3-methylphenyl)methyl]-myo-inositol + NAD+ | - |
Bacillus subtilis | ? + NADH + H+ | - |
? | |
additional information | substrate specificity and substrate binding structure, molecular modeling, overview | Bacillus subtilis | ? | - |
? | |
myo-inositol + NAD+ | - |
Bacillus subtilis | scyllo-inosose + NADH | - |
r | |
myo-inositol + NAD+ | - |
Bacillus subtilis | scyllo-inosose + NADH + H+ | - |
? | |
[(4-methylphenyl)methyl]-myo-inositol + NAD+ | - |
Bacillus subtilis | ? + NADH + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | construction of an homology model of inositol dehydrogenase, to which NADH and 4-O-benzylscyllo-inosose are docked and the active site energy minimized, molecular modeling, overview | Bacillus subtilis |
Synonyms | Comment | Organism |
---|---|---|
IDH | - |
Bacillus subtilis |
myo-inositol dehydrogenase | - |
Bacillus subtilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Bacillus subtilis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.23 | - |
myo-inositol | pH 9.0, 25°C, recombinant mutant H176A | Bacillus subtilis | |
1.9 | - |
myo-inositol | pH 9.0, 25°C, recombinant mutant D172N | Bacillus subtilis | |
34 | - |
myo-inositol | pH 9.0, 25°C, recombinant mutant Y235F | Bacillus subtilis | |
47 | - |
myo-inositol | pH 9.0, 25°C, recombinant mutant Y233F | Bacillus subtilis | |
58 | - |
myo-inositol | pH 9.0, 25°C, recombinant wild-type enzyme | Bacillus subtilis | |
73 | - |
myo-inositol | pH 9.0, 25°C, recombinant mutant D179N | Bacillus subtilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | - |
assay at | Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Bacillus subtilis | |
NADH | - |
Bacillus subtilis |