KEGG   ENZYME: 4.3.1.23Help
Entry
EC 4.3.1.23                 Enzyme                                 

Name
tyrosine ammonia-lyase;
TAL;
tyrase;
L-tyrosine ammonia-lyase
Class
Lyases;
Carbon-nitrogen lyases;
Ammonia-lyases
BRITE hierarchy
Sysname
L-tyrosine ammonia-lyase (trans-p-hydroxycinnamate-forming)
Reaction(IUBMB)
L-tyrosine = trans-p-hydroxycinnamate + NH3 [RN:R00737]
Reaction(KEGG)
R00737;
(other) R06132
Show
Substrate
L-tyrosine [CPD:C00082]
Product
trans-p-hydroxycinnamate [CPD:C00811];
NH3 [CPD:C00014]
Comment
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].
History
EC 4.3.1.23 created 2008 (EC 4.3.1.5 created 1965, part-incorporated 2008)
Pathway
ec00350  Tyrosine metabolism
Orthology
K10774  tyrosine ammonia-lyase
Genes
HHA: Hhal_1820
HCO: LOKO_01494
RME: Rmet_0231(hutH)
RSP: RSP_3574(hutH)
RSH: Rsph17029_3256
RSK: RSKD131_3741
RCP: RCAP_rcc01072(hutH)
AMI: Amir_4353
SRU: SRU_0717
Taxonomy
Reference
1  [PMID:17185228]
  Authors
Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP.
  Title
Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases.
  Journal
Chem Biol 13:1327-38 (2006)
DOI:10.1016/j.chembiol.2006.11.011
  Sequence
[rsp:RSP_3574]
Reference
2  [PMID:17185227]
  Authors
Watts KT, Mijts BN, Lee PC, Manning AJ, Schmidt-Dannert C.
  Title
Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family.
  Journal
Chem Biol 13:1317-26 (2006)
DOI:10.1016/j.chembiol.2006.10.008
  Sequence
[rsp:RSP_3574]
Reference
3  [PMID:10220322]
  Authors
Schwede TF, Retey J, Schulz GE.
  Title
Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile.
  Journal
Biochemistry 38:5355-61 (1999)
DOI:10.1021/bi982929q
Other DBs
ExplorEnz - The Enzyme Database: 4.3.1.23
IUBMB Enzyme Nomenclature: 4.3.1.23
ExPASy - ENZYME nomenclature database: 4.3.1.23
BRENDA, the Enzyme Database: 4.3.1.23
CAS: 1030840-68-6

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