Production of high levels of soluble recombinant Streptomyces clavuligerus isopenicillin N synthase in Escherichia coli
Author:
Publisher
Elsevier BV
Subject
Process Chemistry and Technology,Biochemistry,Bioengineering,Catalysis
Reference28 articles.
1. Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes
2. Cloning and expression of the isopenicillin N synthetase gene from Penicillium chrysogenum
3. High-level expression of the Streptomyces clavuligerus isopenicillin N synthase gene in Escherichia coli
4. Production ofStreptomyces clavuligerus isopenicillin N synthase inEscherichia coli using two-cistron expression systems
5. Formation of Soluble Recombinant Proteins in Escherichia Coli is Favored by Lower Growth Temperature
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1. Glycosaminoglycan-binding properties and kinetic characterization of human heparin cofactor II expressed in Escherichia coli;Analytical Biochemistry;2010-11
2. Functional analysis of a conserved aspartate D218 in Cephalosporium acremonium isopenicillin N synthase;FEMS Microbiology Letters;2006-01-17
3. The Invariant F283 and Its Strategic Position in the Hydrophobic Cleft of Streptomyces jumonjinensis Isopenicillin N Synthase Active Site Are Functionally Important;Biochemical and Biophysical Research Communications;2001-05
4. Construction of Streptomyces jumonjinensis isopenicillin N synthase double mutants, Ser119Ala/Glu120Gly and Thr308Ala/Thr309Val, overcomes insoluble expression in Escherichia coli;Journal of Molecular Catalysis B: Enzymatic;2001-04
5. PCR cloning, heterologous expression, and characterization of isopenicillin N synthase fromStreptomyces lipmaniiNRRL 3584;Canadian Journal of Microbiology;2000-02-01
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