title: Enzymatic synthesis of beta-lactam antibiotics and N-fatty-acylated amino compounds by the acyl-transfer reaction catalyzed by penicillin V acylase from Streptomyces mobaraensis.
abstract: Penicillin V acylase from Streptomyces mobaraensis (Sm-PVA) showed high acyl-transfer activity in reactions using methyl esters of carboxylic acid (acyl donor) and amino compounds (nucleophile), to produce the corresponding amides. Moreover, Sm-PVA had broad substrate specificity, as indicated by the fact that it catalyzed the efficient synthesis of beta-lactam antibiotics, capsaicin derivatives, and N-fatty-acyl-amino acid/N-fatty-acyl-peptide derivatives.
authors.affiliation: Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University, Japan.
authors.forename: Mayuko
authors.initials: M
authors.lastname: Koreishi
authors.forename: Kazuha
authors.initials: K
authors.lastname: Tani
authors.forename: Yuuichi
authors.initials: Y
authors.lastname: Ise
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Imanaka
authors.forename: Koreyoshi
authors.initials: K
authors.lastname: Imamura
authors.forename: Kazuhiro
authors.initials: K
authors.lastname: Nakanishi
mesh_terms: D000577:Amides / Q000138:chemical synthesis; D000596:Amino Acids / Q000096:biosynthesis; D000900:Anti-Bacterial Agents / Q000096:biosynthesis*; D002211:Capsaicin / Q000138:chemical synthesis; D002384:Catalysis; D010399:Penicillin Amidase / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology* / Q000378:metabolism; D013379:Substrate Specificity; D047090:beta-Lactams / Q000138:chemical synthesis*
chemical_list: D000577:Amides; D000596:Amino Acids; D000900:Anti-Bacterial Agents; D047090:beta-Lactams; D010399:Penicillin Amidase; D002211:Capsaicin