Phenylalanine ammonia lyase from Arabidopsis thaliana (AtPAL2): A potent MIO-enzyme for the synthesis of non-canonical aromatic alpha-amino acids: Part I: Comparative characterization to the enzymes from Petroselinum crispum (PcPAL1) and Rhodosporidium toruloides (RtPAL).
J Biotechnol
; 258: 148-157, 2017 Sep 20.
Article
en En
| MEDLINE
| ID: mdl-28392421
Palabras clave
(S)-2-F-Phe (Pubchem CID: 716319); (S)-3-Cl-Phe (Pubchem CID: 85680); (S)-3-F-Phe (Pubchem CID: 9976); (S)-3-OCH(3)-4-OH-Phe (Pubchem CID: 94331; (S)-4-Cl-Phe (Pubchem CID:4652); (S)-4-F-Phe (Pubchem CID: 716312); (S)-Phe (Pubchem CID: 6140); (S)-tyrosine (Pubchem CID 6057); (S)2Cl-Phe (Pubchem CID85679); Chiral synthesis; MIO enzyme; Phenylalanine ammonia lyase; Substrate range; Tyrosine ammonia lyase; Whole cell biotransformation; trans-cinnamic acid (Pubchem CID: 444539)
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Fenilanina Amoníaco-Liasa
/
Basidiomycota
/
Arabidopsis
/
Petroselinum
/
Aminoácidos Aromáticos
Idioma:
En
Revista:
J Biotechnol
Asunto de la revista:
BIOTECNOLOGIA
Año:
2017
Tipo del documento:
Article