Accession | TIGR01226 |
Name | phe_am_lyase |
Function | phenylalanine ammonia-lyase |
Trusted Cutoff | 519.15 |
Domain Trusted Cutoff | 519.15 |
Noise Cutoff | 301.90 |
Domain Noise Cutoff | 301.90 |
Isology Type | equivalog |
EC Number | 4.3.1.24 |
HMM Length | 680 |
Gene Ontology Term | GO:0009698: phenylpropanoid metabolic process biological_process |
| GO:0016841: ammonia-lyase activity molecular_function |
Author | Haft DH |
Entry Date | May 4 2001 1:48PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | Members of this subfamily of MIO prosthetic group enzymes are phenylalanine ammonia-lyases. They are found, so far, in plants and fungi. From phenylalanine, this enzyme yields cinnaminic acid, a precursor of many important plant compounds. This protein shows extensive homology to histidine ammonia-lyase, the first enzyme of a histidine degradation pathway. Note that members of this family from plant species that synthesize taxol are actually phenylalanine aminomutase, and are covered by exception model TIGR04473. |
References | RN [1]
RM PMID:20577998
RT Probing the active site of MIO-dependent aminomutases, key catalysts in the biosynthesis of beta-amino acids incorporated in secondary metabolites.
RA Cooke HA, Bruner SD
RL Biopolymers. 2010 Sep;93(9):802-10. doi: 10.1002/bip.21500. |