نتایج جستجو برای: l valine

تعداد نتایج: 625024  

Journal: :The Journal of biological chemistry 1966
P Datta

1. Threonine deaminase has been purified about 1400fold from extracts of the photosynthetic bacterium Rhodopseudomonas spheroides by ammonium sulfate fractionation and by chromatography on DEAE-cellulose and hydroxylapatite columns. The purified enzyme is almost completely resolved with respect to bound coenzyme, and the activity of holoenzyme is specific for pyridoxal phosphate. The enzyme is ...

The formation constants (log K), of the complexes formed between a number of amino acids(glycine , L-valine and L-alanine) with p-sulfonatocalix [4] arene at varying temperatures (25± 0.1to 65 ± 0.1 °C) in aqueous solutions and at natural pH of p-sulphonato-calix [4] arene (pH=3.2) bymeans of UV-Vis spectrophotometeric technique have been investigated. At this pH the guestmolecule is in its cat...

Journal: :Journal of bacteriology 1961
E KATZ C R WALDRON M L MELONI

Katz, Edward (Rutgers, The State University, New Brunswick, N. J.), Clarence R. Waldron, and Mary Lou Meloni. Role of valine and isoleucine as regulators of actinomycin peptide formation by Streptomyces chrysomallus. J. Bacteriol. 82:600-608. 1961-d-Valine is an effective inhibitor of actinomycin synthesis by Streptomyces chrysomallus; l-valine stimulates actinomycin production and reverses the...

Journal: :Applied and environmental microbiology 2007
Bastian Blombach Mark E Schreiner Jirí Holátko Tobias Bartek Marco Oldiges Bernhard J Eikmanns

Corynebacterium glutamicum was engineered for the production of L-valine from glucose by deletion of the aceE gene encoding the E1p enzyme of the pyruvate dehydrogenase complex and additional overexpression of the ilvBNCE genes encoding the L-valine biosynthetic enzymes acetohydroxyacid synthase, isomeroreductase, and transaminase B. In the absence of cellular growth, C. glutamicum DeltaaceE sh...

Journal: :The Biochemical journal 1989
N D Priestley J A Robinson

NAD+-dependent L-valine dehydrogenase was purified 180-fold from Streptomyces cinnamonensis, and to homogeneity, as judged by gel electrophoresis. The enzyme has an Mr of 88,000, and appears to be composed of subunits of Mr 41,200. The enzyme catalyses the oxidative deamination of L-valine, L-leucine, L-2-aminobutyric acid, L-norvaline and L-isoleucine, as well as the reductive amination of the...

Journal: :Bulletin of the Chemical Society of Japan 1981

Journal: :Bulletin of the Chemical Society of Japan 1980

Journal: :Journal of the agricultural chemical society of Japan 1960

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