The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 4.1.99.2     
Accepted name: tyrosine phenol-lyase
Reaction: L-tyrosine + H2O = phenol + pyruvate + NH3 (overall reaction)
(1a) L-tyrosine = phenol + 2-aminoprop-2-enoate
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
Other name(s): β-tyrosinase; L-tyrosine phenol-lyase (deaminating)
Systematic name: L-tyrosine phenol-lyase (deaminating; pyruvate-forming)
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: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9059-31-8
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 (1970) 1767–1772. [PMID: 4908868]
2.  Kumagai, H., Yamada, H., Matsui, H., Ohkishi, H. and Ogata, K. Tyrosine phenol lyase. II. Cofactor requirements. J. Biol. Chem. 245 (1970) 1773–1777. [PMID: 4908869]
[EC 4.1.99.2 created 1972]
 
 


Data © 2001–2017 IUBMB
Web site © 2005–2017 Andrew McDonald