Oxidative modification of a Cephalosporin C acylase from Pseudomonas strain N176 and site-directed mutagenesis of the gene

Article Abstract:

Mutation of residue Met-164 to Asn, Gln, Gly, Ser, Pro and Thr improves N176 cephalosporin acylase activity in Pseudomonas N176 strain against glutarylcephalosporanic acid. However, mutation to Leu or Phe causes a reduction in activity. Met-164 is responsible for the decrease in the enzymatic activity by oxidation with hydrogen peroxide. The residue is located in the substrate binding pocket at the active site of the enzyme and its mutation disturbs the enzyme structure.

Pseudomonas, Microbial enzymes

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Insertion-duplication mutagenesis in Streptococcus pneumoniae: targeting fragment length is a critical parameter in use as a random insertion tool

Article Abstract:

A study was conducted to examine the efficiency and specificity of the recombination of insertion plasmids supporting targeting fragments of different lengths. Strain CP1250 was utilized for all pneumococcal transformation reactions while donor DNA samples were quantitated by determining fluorescent intensities in ethidium bromide-stained agarose levels. Results indicated the specificity of targeting insertion-duplication mutagenesis.

Plasmids, Streptococcus pneumoniae

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In vivo insertional mutagenesis in Corynebacterium pseudotuberculosis: An efficient means to identity DNA sequences encoding exported proteins

Article Abstract:

Exported proteins of the animal pathogen Corynebacterium pseudotuberculosis is identified using the reporter transposon-based system TnFuZ. Results revealed that thirty-four out of 1,500 mutants had detectable alkaline phosphatase (PhoZ) activity.

Science & research, Genetic aspects, Transposons, Alkaline phosphatase, Structure, Chemical properties, Corynebacteria, Report

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