_EC 4.3.1.25 Phenylalanine/tyrosine ammonia-lyase. 3 PDB entries  
EC 4.-.-.- Lyases. [3,764 PDB entries]
EC 4.3.-.- Carbon-nitrogen lyases. [264 PDB entries]
EC 4.3.1.- Ammonia-lyases. [107 PDB entries]
EC 4.3.1.25 Phenylalanine/tyrosine ammonia-lyase. [3 PDB entries]    
1t6j

Reaction: (1) L-phenylalanine = trans-cinnamate + ammonia. (2) L-tyrosine = trans-p-hydroxycinnamate + ammonia.
 


L-phenylalanine
=
trans-cinnamate
+ ammonia

L-tyrosine
=
trans-p-hydroxycinnamate
+ ammonia
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Bifunctional Pal. Ptal.
Cofactor(s): Mio.
Comments: 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.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 3 PDB entries in enzyme class E.C.4.3.1.25

  PDB code Protein
1t6j
Crystal structure of phenylalanine ammonia lyase from rhodos toruloides
Source: Rhodosporidium toruloides. Organism_taxid: 5286. Gene: pal. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (647 residues) CATH domains: 1.10.275.10 1.20.200.10 1.10.274.20
Bound ligand:   Het Group CIN corresponds to enzyme product Trans-cinnamate
1t6p
Crystal structure of phenylalanine ammonia lyase from rhodosporidium toruloides
Source: Rhodosporidium toruloides. Organism_taxid: 5286. Gene: pal. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H (654 residues) CATH domains: 1.10.275.10 1.20.200.10 1.10.274.20
1y2m
Crystal structure of phenylalanine ammonia-lyase from yeast rhododporidium toruloides
Source: Rhodosporidium toruloides. Organism_taxid: 5286. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (665 residues) CATH domains: 1.10.275.10 1.20.200.10 1.10.274.20