δ-Aminovaleramidase of Pseudomonas putida
نویسندگان
چکیده
منابع مشابه
Pathogenic significance of Pseudomonas fluorescens and Pseudomonas putida.
Among the members of the genus Pseudomonas, P. aeruginosa and P. pseudomallei were, until recently, considered the human pathogens. However, since the early 1960s, other Pseudomonas species have been found in clinical specimens, and their number and frequency of isolation seem to be growing.' The "simple fluorescent" species, P. fluorescens and P. putida, belong to those that were thought by ea...
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In bacteria, polynucleotide phosphorylase (PNPase) is one of the main exonucleolytic activities involved in RNA turnover and is widely conserved. In spite of this, PNPase does not seem to be essential for growth if the organisms are not subjected to special conditions, such as low temperature. We identified the PNPase-encoding gene (pnp) of Pseudomonas putida and constructed deletion mutants th...
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Received: 21 April, 2009 Accepted: 8 July, 2009 Abstract Background & Aims: Dimethoate as an organophosphorus compound is commonly used for crop production which is neurotoxic in human. Pseudomonas family harbor organophosphate degrading plasmids have been known as tools for cleaning environmental pollutions. Materials & Methods: Pseudomonas Putida was isolated from contaminated soil b...
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Catechol 2,3-dioxygenase and homoprotocatechuate 2,3-dioxygenase were purified from the same strain of Pseudomonas putida. Molecular weights and subunit sizes were similar, but amino acid compositions showed some marked differences.
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The activities of six enzymes which take part in the oxidation of valine by Pseudomonas putida were measured under various conditions of growth. The formation of four of the six enzymes was induced by growth on d- or l-valine: d-amino acid dehydrogenase, branched-chain keto acid dehydrogenase, 3-hydroxyisobutyrate dehydrogenase, and methylmalonate semialdehyde dehydrogenase. Branched-chain amin...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)63026-1