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Cloning and characterization of the polyhydroxybutyrate depolymerase gene of Pseudomonas stutzeri and analysis of the function of substrate-binding domains

Article Abstract:

The cloning of polyhydroxybutyrate depolymerase gene (phaZ(sub Pst)) of Pseudomonas stutzeri and the functional analysis of the substrate-binding domains have been undertaken. It was discovered that phaZ(sub Pst) is made up of 1,728 bp encoding a protein of 576 amino acids. The protein has a domain structure with a catalytic domain, a putative linker region and two putative substrate-binding domains.

Author: Doi, Yoshiharu, Ohura, Takeshi, Kasuya, Ken-ichi
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
Research, Pseudomonas, Cloning, Binding sites (Biochemistry), Active sites (Biochemistry)

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Effect of pH on intracellular accumulation of trace concentrations of Hg(II) in Escherichia coli under anaerobic conditions, as measured using a mer-lux bioreporter

Article Abstract:

The effects of pH on the uptake and accumulation of Hg(II) by Escherichia coli are examined by using a plasmid borne mer-lux bioreporter at environmentally relevant concentrations of Hg and under anaerobic conditions. The results have shown that the accumulation and toxicity of Hg(II) increased as the pH of the assay medium decreased.

Author: Kelly, Carol A., Golding, George G., Sparling, Richard
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2008
Influence, Hydrogen-ion concentration, pH, Mercury metabolism

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Expression of 3-Ketoacyl-Acyl carrier protein reductase (fabG) genes enhances production of polyhydroxyalkanoate copolymer from glucose in recombinant Escherichia coli JM109

Article Abstract:

A new expression of 3-Ketoacyl-Acyl carrier protein reductase (fabG) gene from Pseudomonas sp. 61-3 was cloned and studied. Results show that the Pseudomonas sp. 61-3 and Escherichia coli fabG proteins have different substrate specificities in vitro.

Author: Doi, Yoshiharu, Nomura, Christopher T., Taguchi, Kazunori, Gan, Zhihua, Kuwabara, Kazuhiro, Tanaka, Tomoyo, Takase, Kazuma
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2005
Nucleic acids, Chemical properties, Nucleic acid isolation, Polyhydroxyalkanoates

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Subjects list: Analysis, Genetic aspects, Physiological aspects, Escherichia coli
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