EC number:4.3.1.25
| ID: | 4.3.1.25 | ||
|---|---|---|---|
| Description: | Phenylalanine/tyrosine ammonia-lyase. | ||
| Alternative Name: |
PTAL. Bifunctional PAL. | ||
| Prosite: | PDOC00424; | ||
| PDB: |
|
||
| Cath: | 1.10.274.20; 1.10.275.10; 1.20.200.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.3.1.25 |
| BRENDA Enzyme Link: | BRENDA 4.3.1.25 |
| KEGG Enzyme Link: | KEGG4.3.1.25 |
| BioCyc Enzyme Link: | BioCyc 4.3.1.25 |
| ExPASy Enzyme Link: | ExPASy4.3.1.25 |
| EC2PDB Enzyme Link: | EC2PDB 4.3.1.25 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.3.1.25 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.3.1.25 |
| IntEnz Enzyme Link: | IntEnz 4.3.1.25 |
| MEDLINE Enzyme Link: | MEDLINE 4.3.1.25 |
| RHEA:24906 | L-tyrosine = NH4(+) + trans-4-coumarate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH2;+0:4]-[*:5]>>[*:1]-[CH;+0:2]=[CH;+0:4]-[*:5].[NH3;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Probing the active site of MIO-dependent aminomutases, key catalysts in the biosynthesis of beta-amino acids incorporated in secondary metabolites. | Cooke HA, Bruner SD | 2010 Sep | 20577998 |
| Discovery of additional members of the tyrosine aminomutase enzyme family and the mutational analysis of CmdF. | Krug D, Müller R | 2009 Mar 2 | 19222035 |
| Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity. | Rösler J, Krekel F, Amrhein N, Schmid J | 1997 Jan | 9008393 |
| Preliminary data on the structure and embryogenesis of the parietal eye in Chalcides ocellatus (Lep. Scin.). | Lipari EF, Lipari D | 1982 Dec-1983 Jan | 7185228 |
| Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential dehydroalanine. | Hodgins DS | 1971 May 10 | 5102931 |
| Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases. | Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP | 2006 Dec | 17185228 |
| Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family. | Watts KT, Mijts BN, Lee PC, Manning AJ, Schmidt-Dannert C | 2006 Dec | 17185227 |
| RHEA:21384 | L-phenylalanine = NH4(+) + trans-cinnamate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH2;+0:4]-[*:5]>>[*:1]-[CH;+0:2]=[CH;+0:4]-[*:5].[NH3;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structural investigations into the stereochemistry and activity of a phenylalanine-2,3-aminomutase from Taxus chinensis. | Wybenga GG, Szymanski W, Wu B, Feringa BL, Janssen DB, Dijkstra BW | 2014 May 20 | 24786474 |
| A modern view of phenylalanine ammonia lyase. | MacDonald MJ, D'Cunha GB | 2007 Jun | 17612622 |
| Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases. | Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP | 2006 Dec | 17185228 |
| Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis. | Calabrese JC, Jordan DB, Boodhoo A, Sariaslani S, Vannelli T | 2004 Sep 14 | 15350127 |
| The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms. | Cochrane FC, Davin LB, Lewis NG | 2004 Jun | 15276452 |