منابع مشابه
D-amino acid dehydrogenases of Pseudomonas fluorescens.
Two distinct D-amino acid dehydrogenases, each showing absolute speci&ity for methylene blue or 2,6-dichloroindophenol, respectively, were isolated from Pseudomonas @orescens (ATCC 11299B). The methylene blue-specific ~-amino acid dehydrogenase was detectable only in extracts from D-tryptophan-grown cells and was purified about 40-fold. The 2,6-dichloroindophenol-specif?c ~-amino acid dehydroge...
متن کاملProduction of Recombinant Proline Dehydrogenase Enzyme from Pseudomonas fluorescens pf-5 in E. coli System
Proline dehydrogenase (ProDH; 1.5.99.8) belongs to superfamily of amino acid dehydrogenase, which plays a significant role in the metabolic pathway from proline to glutamate. The goal of this research was gene cloning and characterization of ProDH enzyme from Pseudomonas fluorescens pf-5 strain. The gene encoding ProDH was isolated by means of PCR amplification and cloned in an IPTG inducible T...
متن کاملPseudomonas fluorescens
nas incognita have been previously described as being able to utilize citronellol, geraniol, and linalool (3, 6). Recently, a 50-megadalton (MDa) plasmid has been associated with the degradation of geraniol (9). In this report we describe the isolation of a Pseudomonas fluorescens s train capable of utilizing linalool as a sole carbon and energy source and demonstrate the presence of a transmis...
متن کاملMalic Enzyme of Escherichia coli
The TPN+-specitk malic enzyme from Escherichia coli has been purified from malate-grown cells. An approximately loo-fold purified preparation is activated by NH4+ and K+ ions. The enzyme is inhibited by acetyl coenzyme A, oxalacetate, TPNH, and DPNH in an allosteric manner. Glycine at concentration ranges above 0.5 M has been shown to activate the enzyme as well as to desensitize it reversibly ...
متن کاملThe kynureninase of Pseudomonas fluorescens.
Kotake and Nakayama (1) observed the conversion of kynurenine to anthranilic acid and alanine by a mammalian liver extract. Subsequently the enzyme responsible for this reaction in the mammal was partly purified (2,3) and the enzyme, prepared from vitamin Be-deficient animals, was shown to require pyridoxal phosphate for its maximal activity (2). During an investigation of tryptophan metabolism...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2005
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1982.tb06567.x