EC 4.3.1.23 - Tyrosine ammonia-lyase

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IntEnz Enzyme Nomenclature
EC 4.3.1.23

Names

Accepted name:
tyrosine ammonia-lyase
Other names:
TAL
tyrase
L-tyrosine ammonia-lyase
Systematic name:
L-tyrosine ammonia-lyase (trans-p-hydroxycinnamate-forming)

Reaction

Cofactor

Comments:

This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase), EC 4.3.1.24 (phenylalanine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family [1]. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine [3]. The enzyme is 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 [1,2].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00424
Structural data: CSA , EC2PDB
Gene Ontology: GO:0052883
CAS Registry Number: 1030840-68-6
UniProtKB/Swiss-Prot:

References

  1. Louie, G.V., Bowman, M.E., Moffitt, M.C., Baiga, T.J., Moore, B.S. and Noel, J.P.
    Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases.
    Chem. Biol. 13: 1327-1338 (2006). [PMID: 17185228]
  2. Watts, K.T., Mijts, B.N., Lee, P.C., Manning, A.J. and Schmidt-Dannert, C.
    Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family.
    Chem. Biol. 13: 1317-1326 (2006). [PMID: 17185227]
  3. Schwede, T.F., Rétey, J. and Schulz, G.E.
    Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile.
    Biochemistry 38: 5355-5361 (1999). [PMID: 10220322]

[EC 4.3.1.23 created 2008 (EC 4.3.1.5 created 1965, part-incorporated 2008)]