CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.200 | Fumarase C; Chain A, domain 2 |
|
1.20.200.10 | Fumarase/aspartase (Central domain) |
Domain Context
CATH Clusters
| Superfamily | Fumarase/aspartase (Central domain) |
| Functional Family | Histidine ammonia-lyase |
Enzyme Information
| 4.3.1.23 |
Tyrosine ammonia-lyase.
based on mapping to UniProt Q8GMG0
L-tyrosine = trans-p-hydroxycinnamate + ammonia.
-!- Member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3, EC 4.3.1.24 and EC 4.3.1.25. -!- Far more active with tyrosine than with phenylalanine as substrate, but the substrate specificity can be switched by mutation of a single amino acid (H89F) in the enzyme from the bacterium Rhodobacter sphaeroides. -!- Formerly EC 4.3.1.5.
|
| 5.4.3.6 |
Tyrosine 2,3-aminomutase.
based on mapping to UniProt Q8GMG0
L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate.
|
UniProtKB Entries (1)
| Q8GMG0 |
TAM_STRGL
Streptomyces globisporus
MIO-dependent tyrosine 2,3-aminomutase
|
PDB Structure
| PDB | 2OHY |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway
Biochemistry
|
