EC 4.1.99.2 - Tyrosine phenol-lyase

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IntEnz Enzyme Nomenclature
EC 4.1.99.2

Names

Accepted name:
tyrosine phenol-lyase
Other names:
β-tyrosinase
L-tyrosine phenol-lyase (deaminating)
Systematic name:
L-tyrosine phenol-lyase (deaminating; pyruvate-forming)

Reaction

Cofactor

Comments:

A pyridoxal-phosphate protein. 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 catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme also slowly catalyses similar reactions with D-tyrosine, S-methyl-L-cysteine, L-cysteine, L-serine and D-serine.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00667
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050371
CAS Registry Number: 9059-31-8
UniProtKB/Swiss-Prot: (11) [show] [UniProt]

References

  1. Kumagai, H., Yamada, H., Matsui, H., Ohkishi, H. and Ogata, K.
    Tyrosine phenol lyase. I. Purification, crystallization, and properties.
    J. Biol. Chem. 245 : 1767-1772 (1970). [PMID: 4908868]
  2. Kumagai, H., Yamada, H., Matsui, H., Ohkishi, H. and Ogata, K.
    Tyrosine phenol lyase. II. Cofactor requirements.
    J. Biol. Chem. 245 : 1773-1777 (1970). [PMID: 4908869]

[EC 4.1.99.2 created 1972]