Motifs in the C-terminal region of the Penicillium chrysogenum ACV synthetase are essential for valine epimerization and processivity of tripeptide formation

Wu X.; Garcia-Estrada C.; Vaca I.; Martin J.-F.

Keywords: sequence, hydrolysis, catalysis, acid, proteins, enzyme, biosynthesis, overexpression, tertiary, transcription, complex, protein, gene, peptide, mechanism, alpha, release, site, plasmids, strain, mutagenesis, fungi, fungal, deletion, sulfides, drug, molecular, penicillin, data, article, ester, chrysogenum, delta, activity, genetic, synthetase, thiol, antibiotic, controlled, penicillium, study, hydrolase, amino, nonhuman, dextro, and, G, engineering, Conserved, unclassified, levo, Structure,, directed, Penicillins, Mutagenesis,, Site-Directed, Synthases, Multienzyme, Oligopeptides, Valine, epimerization, Transduction,, tripeptide, epimerase, Epimerases, Racemases, cysteinyl, (levo, aminoadipyl), thioester

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Título según SCOPUS: Motifs in the C-terminal region of the Penicillium chrysogenum ACV synthetase are essential for valine epimerization and processivity of tripeptide formation
Título de la Revista: Biochimie
Volumen: 94
Número: 2
Editorial: Elsevier B.V.
Fecha de publicación: 2012
Página de inicio: 354
Página final: 364
Idioma: English
URL: http://www.scopus.com/inward/record.url?eid=2-s2.0-84855853942&partnerID=40&md5=e0cba4d126cbf0fffbc43332ed61f578
DOI:

10.1016/j.biochi.2011.08.002

Notas: SCOPUS