CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.274 | Enzyme I; Chain A, domain 2 |
|
1.10.274.20 | Phenylalanine ammonia-lyase 1; domain 3 |
Domain Context
CATH Clusters
| Superfamily | Phenylalanine ammonia-lyase 1; domain 3 |
| Functional Family |
Enzyme Information
| 4.3.1.25 |
Phenylalanine/tyrosine ammonia-lyase.
based on mapping to UniProt P11544
(1) L-phenylalanine = trans-cinnamate + ammonia. (2) 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 4.3.1.23 and EC 4.3.1.24. -!- The enzyme from some monocots, including maize, and from the yeast Rhodosporidium toruloides, deaminate L-phenylalanine and L-tyrosine with similar catalytic efficiency. -!- Formerly EC 4.3.1.5.
|
UniProtKB Entries (1)
| P11544 |
PALY_RHOTO
Rhodotorula toruloides
Phenylalanine/tyrosine ammonia-lyase
|
PDB Structure
| PDB | 1T6J |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis.
Biochemistry
|
