CATH Classification

Domain Context

CATH Clusters

Superfamily Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Functional Family Tyrosine phenol-lyase

Enzyme Information

4.1.99.2
Tyrosine phenol-lyase.
based on mapping to UniProt P31013
L-tyrosine + H(2)O = phenol + pyruvate + NH(3).
-!- The enzyme cleaves a carbon-carbon bond, releasing phenol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10. -!- The enzyme also slowly catalyzes similar reactions with D-tyrosine, S-methyl-L-cysteine, L-cysteine, L-serine and D-serine.

UniProtKB Entries (1)

P31013
TPL_CITFR
Citrobacter freundii
Tyrosine phenol-lyase

PDB Structure

PDB 2EZ1
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions
Milic, D., Matkovic-Calogovic, D., Demidkina, T.V., Kulikova, V.V., Sinitzina, N.I., Antson, A.A.
Biochemistry