Production of a fully functional, permuted single-chain penicillin G acylase

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Production of a fully functional, permuted single-chain penicillin G acylase.

Penicillin G acylase (PGA) is a heterodimeric enzyme synthesized as a single-polypeptide precursor that undergoes an autocatalytic processing to remove an internal spacer peptide to produce the active enzyme. We constructed a single-chain PGA not dependent on autoproteolytic processing. The mature sequence of the beta-domain was expressed as the N terminus of a new polypeptide, connected by a r...

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Production of Penicillin Acylase.

The production of penicillin acylase by Escherichia coli Ny.I/3-67 has been increased by phenylacetic acid and phenoxyacetic acid, which themselves strongly inhibit the function of this specific enzyme. Other carbonic acids also increased penicillin acylase production, but to a lesser degree; they also weakly inhibited enzyme function. The production of this enzyme was effectively repressed wit...

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Optimization of Enzymatic Synthesis of Ampicillin Using Cross-Linked Aggregates of Penicillin G Acylase

Penicillin G acylase from E. coli TA1 was immobilized by Cross-Linked Enzyme Aggregates (CLEA), a new method for immobilization. This biocatalyst and commercial immobilized penicillin G acylase (PGA-450) were used to study the effect of pH, temperature and substrate concentration on the synthesis of ampicillin from phenyl glycine methyl ester (PGME) and 6-aminopenicillanic acid (6-APA). Compare...

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Penicillin G Acylase, a biocatalyst and its potential application

The PGA enzyme belongs to the family of N-terminal nucleophile (Ntn) hydrolases. The enzyme Penicillin G Acylase (PGA) mainly produced from Penicillium chrysogenum, E.coli. The synthesis of PGA enzyme is depends on the physico-chemical parameters like carbon source, pH, temperature and media were optimized for higher production of enzyme. There are different methods of purification of PGA enzym...

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Optimization of Enzymatic Synthesis of Ampicillin Using Cross-Linked Aggregates of Penicillin G Acylase

Penicillin G acylase from E. coli TA1 was immobilized by Cross-Linked Enzyme Aggregates (CLEA), a new method for immobilization. This biocatalyst and commercial immobilized penicillin G acylase (PGA-450) were used to study the effect of pH, temperature and substrate concentration on the synthesis of ampicillin from phenyl glycine methyl ester (PGME) and 6-aminopenicillanic acid (6-APA). Compare...

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ژورنال

عنوان ژورنال: Protein Science

سال: 2004

ISSN: 0961-8368,1469-896X

DOI: 10.1110/ps.03436604