منابع مشابه
L-Phenylalanine inhibition of muscle pyruvate kinase.
The allosteric inhibition of M1-type pyruvate kinase from rabbit skeletal muscle by phenylalanine is reciprocally dependent on Mg2+ and phosphoenolpyruvate concentrations. At pH 8, phenylalanine acts as a competitive inhibitor with respect to Mg2+ and phosphoenolpyruvate, and vice versa. Phenylalanine introduces sigmoidicity into the dependence of the reaction velocity on [Mg2+]. In vitro kinet...
متن کاملChloroplasts of higher plants synthesize L-phenylalanine via L-arogenate.
The specific enzymological route of L-phenylalanine biosynthesis has not been established in any higher plant system. The possible pathway routes that have been identified in microorganisms utilize either phenylpyruvate or L-arogenate as a unique intermediate. We now report the presence of arogenate dehydratase (which converts L-arogenate to L-phenylalanine) in cultured-cell populations of Nico...
متن کاملRapid One-Step Separation and Purification of Recombinant Phenylalanine Dehydrogenase in Aqueous Two-Phase Systems
Background: Phenylalanine dehydrogenase (PheDH EC 1.4.1.20) is a NAD+-dependent enzyme that performs the reversible oxidative deamination of L-phenylalanine to phenylpyruvate. It plays an important role in detection and screening of phenylketonuria (PKU) diseases and production of chiral intermediates as well. The main goal of this study was to find a simple and rapid alternative method for pur...
متن کاملl-Phenylalanine Ammonia-Lyase (Maize): Evidence for a Common Catalytic Site for l-Phenylalanine and l-Tyrosine.
l-Phenylalanine ammonia-lyase (E.C. 4.3.1.5) from maize is active with l-tyrosine and l-phenylalanine and exhibits atypical Michaelis-Menten kinetics with both substrates. With phenylalanine as a substrate, the pH optimum is 8.7 and with tyrosine, 7.7. The estimated Km at high substrate concentrations is 0.27 mm for phenylalanine and 0.029 mm for tyrosine. However, the V(max) with phenylalanine...
متن کاملL-Phenylalanine and L-tyrosine catabolism by selected Streptomyces species.
L-Phenylalanine and L-tyrosine were completely catabolized through homogentisate by Streptomyces setonii 75Vi2 but only partially degraded by Streptomyces badius 252, Streptomyces sioyaensis P5, Streptomyces viridosporus T7A, and Streptomyces sp. strain V7. Intermediates of catabolism were confirmed by thin-layer, gas, and high-pressure liquid chromatography. Homogentisate 1,2-dioxygenase was p...
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ژورنال
عنوان ژورنال: Journal of the agricultural chemical society of Japan
سال: 1969
ISSN: 0002-1407,1883-6844
DOI: 10.1271/nogeikagaku1924.43.504