Tyrosine ammonia lyase (EC 4.3.1.23, L-tyrosine ammonia-lyase, TAL or Tyrase) is an enzyme in the natural phenols biosynthesis pathway. It transforms L-tyrosine into p-coumaric acid.[1][2][3]
^Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP (December 2006). "Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases". Chemistry & Biology. 13 (12): 1327–38. doi:10.1016/j.chembiol.2006.11.011. PMC2859959. PMID 17185228.
^Watts KT, Mijts BN, Lee PC, Manning AJ, Schmidt-Dannert C (December 2006). "Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family". Chemistry & Biology. 13 (12): 1317–26. doi:10.1016/j.chembiol.2006.10.008. PMID 17185227.
^Schwede TF, Rétey J, Schulz GE (April 1999). "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile". Biochemistry. 38 (17): 5355–61. doi:10.1021/bi982929q. PMID 10220322.
tyrosine, ammonia, lyase, tyrosine, ammonia, lyase, tyrosine, ammonia, lyase, tyrase, enzyme, natural, phenols, biosynthesis, pathway, transforms, tyrosine, into, coumaric, acid, tyrosine, ammonia, lyaseidentifiersec, 23databasesintenzintenz, viewbrendabrenda,. Tyrosine ammonia lyase EC 4 3 1 23 L tyrosine ammonia lyase TAL or Tyrase is an enzyme in the natural phenols biosynthesis pathway It transforms L tyrosine into p coumaric acid 1 2 3 Tyrosine ammonia lyaseIdentifiersEC no 4 3 1 23DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins TAL displaystyle xrightarrow TAL Ammonia H L tyrosine trans p hydroxycinnamate NH3See also editEC 4 3 1 24 phenylalanine ammonia lyase EC 4 3 1 25 phenylalanine tyrosine ammonia lyase References edit Louie GV Bowman ME Moffitt MC Baiga TJ Moore BS Noel JP December 2006 Structural determinants and modulation of substrate specificity in phenylalanine tyrosine ammonia lyases Chemistry amp Biology 13 12 1327 38 doi 10 1016 j chembiol 2006 11 011 PMC 2859959 PMID 17185228 Watts KT Mijts BN Lee PC Manning AJ Schmidt Dannert C December 2006 Discovery of a substrate selectivity switch in tyrosine ammonia lyase a member of the aromatic amino acid lyase family Chemistry amp Biology 13 12 1317 26 doi 10 1016 j chembiol 2006 10 008 PMID 17185227 Schwede TF Retey J Schulz GE April 1999 Crystal structure of histidine ammonia lyase revealing a novel polypeptide modification as the catalytic electrophile Biochemistry 38 17 5355 61 doi 10 1021 bi982929q PMID 10220322 External links editTyrosine ammonia lyase at the U S National Library of Medicine Medical Subject Headings MeSH www hhmi org Portal nbsp Biology nbsp This enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Tyrosine ammonia lyase amp oldid 1171068276, wikipedia, wiki, book, books, library,
