CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.360 | Dihydrodipicolinate Reductase; domain 2 |
|
3.30.360.10 | Dihydrodipicolinate Reductase; domain 2 |
Domain Context
CATH Clusters
| Superfamily | Dihydrodipicolinate Reductase; domain 2 |
| Functional Family |
Enzyme Information
| 1.1.1.369 |
D-chiro-inositol 1-dehydrogenase.
based on mapping to UniProt P26935
1D-chiro-inositol + NAD(+) = 2D-2,3,5/4,6-pentahydroxycyclohexanone + NADH.
-!- The enzyme, found in the bacterium Bacillus subtilis, also catalyzes the reaction of EC 1.1.1.18 and can also use D-glucose and D-xylose. -!- It shows trace activity with D-ribose and D-fructose. -!- It is part of a myo-inositol/D-chiro-inositol degradation pathway leading to acetyl-CoA. -!- Formerly EC 1.1.1.n6.
|
| 1.1.1.18 |
Inositol 2-dehydrogenase.
based on mapping to UniProt P26935
Myo-inositol + NAD(+) = 2,4,6/3,5-pentahydroxycyclohexanone + NADH.
|
UniProtKB Entries (1)
| P26935 |
IOLG_BACSU
Bacillus subtilis subsp. subtilis str. 168
Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase
|
PDB Structure
| PDB | 4L8V |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Converting NAD-Specific Inositol Dehydrogenase to an Efficient NADP-Selective Catalyst, with a Surprising Twist.
Biochemistry
|
