Yeast alpha-isopropylmalate isomerase. Factors affecting stability and enzyme activity.

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Yeast alpha-isopropylmalate isomerase. Factors affecting stability and enzyme activity.

Yeast alpha-isopropylmalate isomerase was found to be markedly stabilized by high concentrations of glycerol and (NH4)2SO4. Such conditions of high ionic strength inhibited the enzyme, stabilized the enzyme to heat, and affected kinetic parameters. The isomerase was found to exhibit ionic strength-dependent hysteresis when enzyme, totally but reversibly inhibited by storage under conditions of ...

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Purification of yeast alpha-isopropylmalate isomerase. High ionic strength hydrophobic chromatography.

alpha-Isopropylmalate isomerase, the second enzyme specific for leucine biosynthesis, can be purified from extracts of yeast utilizing a chromatographic procedure that allows separation of proteins in the presence of high concentrations of (NH4)2SO4. The purification procedure utilizes the stabilizing effect of glycerol and (NH4)2SO4 on the isomerase and their opposing effects on protein retent...

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A Herbicidal Inhibitor of Isopropylmalate Isomerase

N itronate com pounds resembling the aa-carboxylate reaction interm ediate in the reaction catalyzed by isopropylm alate isomerase were investigated as enzyme inhibitors and potential herbicides. The nitronic acids o f l-hydroxy-2-nitrocyclopentane-l-carboxylic acid, nitroisop ropylm alate and o f l-hydroxy-2-nitrocyclohexane-l-carboxylic acid were all po ten t inhibi­ tors o f isopropylm alate...

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Regulation of isopropylmalate isomerase synthesis in Neurospora crassa.

The capacity to synthetize isopropylmalate isomerase (EC 4.2.1.33) by Neurospora crassa increased during induction in the presence of cycloheximide but was inhibited by proflavine and other inhibitors of RNA synthesis. Turnover of the enzyme once formed appeared negligible, but the message (measured as enzyme-forming capacity) had a half-life of 4 to 8 min. A comparison of the kinetics of induc...

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The Effects of Consensus Mutations on Yeast Enzyme Triosephosphate Isomerase

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1976

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(17)33378-1