Phenylalanine/tyrosine ammonia-lyase (EC 4.3.1.25, PTAL, bifunctional PAL) is an enzyme with systematic nameL-phenylalanine(or L-tyrosine):trans-cinnamate(or trans-p-hydroxycinnamate) ammonia-lyase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
^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.
^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.
^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.
phenylalanine, tyrosine, ammonia, lyase, ptal, bifunctional, enzyme, with, systematic, name, phenylalanine, tyrosine, trans, cinnamate, trans, hydroxycinnamate, ammonia, lyase, this, enzyme, catalyses, following, chemical, reactionidentifiersec, 25databasesint. Phenylalanine tyrosine ammonia lyase EC 4 3 1 25 PTAL bifunctional PAL is an enzyme with systematic name L phenylalanine or L tyrosine trans cinnamate or trans p hydroxycinnamate ammonia lyase 1 2 3 4 5 This enzyme catalyses the following chemical reactionPhenylalanine tyrosine ammonia lyaseIdentifiersEC no 4 3 1 25DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins 1 L phenylalanine displaystyle rightleftharpoons trans cinnamate NH3 2 L tyrosine displaystyle rightleftharpoons trans p hydroxycinnamate NH3 This enzyme is a member of the aromatic amino acid lyase family References edit Rosler J Krekel F Amrhein N Schmid J January 1997 Maize phenylalanine ammonia lyase has tyrosine ammonia lyase activity Plant Physiology 113 1 175 9 doi 10 1104 pp 113 1 175 PMC 158128 PMID 9008393 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 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 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 Barros J Serrani Yarce JC Chen F Baxter D Venables BJ Dixon RA May 2016 Role of bifunctional ammonia lyase in grass cell wall biosynthesis Nature Plants 2 6 16050 doi 10 1038 nplants 2016 50 PMID 27255834 External links editPhenylalanine tyrosine ammonia lyase at the U S National Library of Medicine Medical Subject Headings MeSH Portal nbsp Biology Retrieved from https en wikipedia org w index php title Phenylalanine tyrosine ammonia lyase amp oldid 1187466515, wikipedia, wiki, book, books, library,
