CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1150 | Aspartate Aminotransferase, domain 1 |
|
3.90.1150.10 | Aspartate Aminotransferase, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Aspartate Aminotransferase, domain 1 |
| Functional Family |
Enzyme Information
| 4.2.1.168 |
GDP-4-dehydro-6-deoxy-alpha-D-mannose 3-dehydratase.
based on mapping to UniProt Q9F118
GDP-4-dehydro-alpha-D-rhamnose + L-glutamate = GDP-4-dehydro-3,6-dideoxy- alpha-D-mannose + 2-oxoglutarate + ammonia.
-!- This enzyme, involved in beta-L-colitose biosynthesis, is a unique vitamin-B6-dependent enzyme. -!- In the first step of catalysis, the bound pyridoxal phosphate (PLP) cafactor is transaminated to the pyridoxamine 5'-phosphate (PMP) form of vitamin B(6), using L-glutamate as the amino group donor. -!- The PMP cofactor then forms a Schiff base with the sugar substrate and the resulting adduct undergoes a 1,4-dehydration to eliminate the 3-OH group. -!- Hydrolysis of the product from the enzyme restores the PLP cofactor and results in the release of an unstable enamine intermediate. -!- This intermediate tautomerizes to form an imine form, which hydrolyzes spontaneously, releasing ammonia and forming the final product.
|
UniProtKB Entries (1)
| Q9F118 |
Q9F118_ECOLX
Escherichia coli
DegT/DnrJ/EryC1/StrS family aminotransferase
|
PDB Structure
| PDB | 2GMS |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The structure of GDP-4-keto-6-deoxy-D-mannose-3-dehydratase: a unique coenzyme B6-dependent enzyme.
Protein Sci.
|
