CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.150 | Divalent-metal-dependent TIM barrel enzymes |
Domain Context
CATH Clusters
| Superfamily | Divalent-metal-dependent TIM barrel enzymes |
| Functional Family | Xylose isomerase |
Enzyme Information
| 5.3.1.5 |
Xylose isomerase.
based on mapping to UniProt P15587
D-xylopyranose = D-xylulose.
-!- The enzyme catalyzes the interconversion of aldose and ketose sugars with broad substrate specificity. -!- The enzyme binds the closed form of its sugar substrate (in the case of glucose, only the alpha anomer) and catalyzes ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. -!- Isomerization proceeds via a hydride-shift mechanism.
|
UniProtKB Entries (1)
| P15587 |
XYLA_STROL
Streptomyces olivochromogenes
Xylose isomerase
|
PDB Structure
| PDB | 1XYM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acid.
Biochemistry
|
