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Cloning and characterization of penicillin V acylase from Streptomyces mobaraensis

Paper ID Volume ID Publish Year Pages File Format Full-Text
25320 43567 2007 13 PDF Available
Title
Cloning and characterization of penicillin V acylase from Streptomyces mobaraensis
Abstract

We report on the molecular cloning and characterization of penicillin V acylase (PVA) from an actinomycete, Streptomyces mobaraensis (Sm-PVA), which was originally isolated as an acylase that efficiently hydrolyzes the amide bond of various N-fatty-acyl-l-amino acids and N-fatty-acyl-peptides as well as capsaicin (8-methyl-N-vanillyl-6-nonenamide). In addition, the purified Sm-PVA hydrolyzed penicillin V with the highest activity (kcat) among the PVAs so far reported, penicillin G, and 2-nitro-5-phenoxyacetamide benzoic acid. The BLAST search revealed that the Sm-PVA precursor is composed of a polypeptide that is characteristic of enzymes belonging to the β-lactam acylase family with four distinct segments; a signal sequence (43 amino acids), an α subunit (173 amino acids), a linker peptide (28 amino acids), and a β subunit (570 amino acids). The mature, active Sm-PVA is a heterodimeric protein with α and β subunits, in contrast to PVAs isolated from Bacillus sphaericus and B. subtilis, which have a homotetrameric structure. The amino acid sequence of Sm-PVA showed identities to PVA from S. lavendulae, N-acylhomoserine lactone-degrading acylase from Streptomyces sp., cyclic lipopeptide acylase from Streptomyces sp., and aculeacin A acylase from Actinoplanes utahensis with 68, 67, 67, and 41% identities, respectively.

Keywords
β-Lactam acylase family; Penicillin V acylase; Actinomycete; Streptomyces mobaraensis; Penicillin V; Capsaicin
First Page Preview
Cloning and characterization of penicillin V acylase from Streptomyces mobaraensis
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 128, Issue 4, 10 March 2007, Pages 788–800
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering