Studies in Valine Biosynthesis

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Biosynthesis of Valine and Isoleucine

The isotope studies of Strassman et al. (3, 4) first implicated cu-acetolactate and cu-aceto-cY-hydroxybutyrate as biosynthetic precursors of valine and isoleucine, respectively. The observed accumulation of acetolactate by Escherichia coli (5, 6) and of the decarboxylation products of acetolactate and acetohydroxybutyrate by Neurospora crassa (7) when mutants of these organisms are grown with ...

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Biosynthesis of Valine and Isoleucine

Evidence published in recent years has shown that the biosynthesis of valine and isoleucine proceeds by a similar sequence of reactions (24). Fig. 1 depicts the reactions considered to be involved. In this report only Reactions II, III, and IV will be considered. Reaction II, the isomerization of the Lu-hydroxy$keto acid (ac-acetolactate for valine biosynthesis and a-aceto-a-hydroxybutyrate for...

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Studies in valine biosynthesis. V. Characteristics of the purified dihydroxyacid dehydratase from spinach leaves.

An intermediate reaction in valine biosynthesis is the dehydration of Q!, /3-dihydroxyisovaleric acid to ar-ketoisovaleric acid, which undergoes transamination to form valine. A similar catalytic removal of a molecule of water from cy , ,&dihydroxy-/3methyl-n-Valerie acid is a step in isoleucine formation. The dihydroxyacid dehydratase (EC 4.2.1.9) for these steps was first observed in Neurospo...

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Studies in valine biosynthesis. III. Biological distribution of a dihydroxy acid dehydrase.

The steps in the pathway of formation of valine are: decarbosylation of pyruvate to an acetaldehyde-thiamine pyrophosphate intermediate which condenses with another molecule of pyruvate to yield ar-acetolactic acid, migration of the a-methyl carbon to form ar-keto-fl-hydroxyisovaleric acid, reduction of this acid to produce (Y ,&dihydroxyisovaleric acid, dehydration to yield ar-ketoisovaleric a...

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Multivalent repression of isoleucine- valine biosynthesis in Saccharomyces cerevisiae.

Regulation of the biosynthesis of four of the five enzymes of the isoleucine-valine pathway was studied in Saccharomyces cerevisiae. A method is described for limiting the growth of a leucine auxotroph by using valine as a competitor for the permease. Limitation for isoleucine and valine was accomplished by the use of peptides containing these amino acids conjugated with glycine as nutritional ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1961

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)94006-8