Isolation of glutamine synthetase and glutamotransferase from green peas.
نویسنده
چکیده
The enzyme system catalyzing this has been termed “glutamine synthetase” and for convenience this name will be used here. Ammonia in this reaction can be replaced by hydrasine or hydroxylamine, all three bases reacting at the same rate (4). All organic bases and amino acids tested have been found to be inactive. With hydroxylamine, a hydroxamic acid is produced, estimation of which provides a convenient colorimetric test for enzyme activity (5). More recently, the work of Schou et al. (6) and of Stumpf et al. (7-9) has revealed anot,her enzymic reaction leading to the formation of glutamylhydroxamic acid. The enzyme, which is known as glutamotransferase, catalyzes the exchange of the amide group of glutamine for either isotopic ammonia or hydroxylamine by the following reaction.
منابع مشابه
Isolation of Two Quinones with Coenzyme
3. DENES, G. Glutamine synthetase: its stereospecificity and changes induced by activating ions. Biochim. Biophys. Acta 15: 296-297. 1954. 4. DENES, G. and GAZDA, ZS. Untersuchungen iiber die enzymatische Synthese der Siiureamidund Peptidbindung. I. Die enzymatische Synthese von Glutamin in Lupinus albus. Acta Physiol. Acad. Sci. Hung. 4: 1-12. 1953. 5. ELLIOrr, W. H. Studies on the enzymic syn...
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The relationships of five feedback inhibitors for the Bacillus licheniformis glutamine synthetase were investigated. The inhibitors were distinguishable by differences in their competitive relationship for the substrates of the enzyme. Mixtures of l-glutamine and adenosine-5'-monophosphate (AMP) or histidine and AMP caused synergistic inhibition of glutamine synthesis. Histidine, alanine, and g...
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Glutamine synthetase of roots, etiolated cotyledons and green leaves from mustard plants cannot all clearly be separated by DEAE-Sephacel chromatography. However, the enzyme of the roots, etiolated cotyledons and green leaves, respectively, differed in the kinetic properties deter mined in the crude extract. The root enzyme showed a pH-optimum of about 6.9, a Km value of 3 m M for glutamate an...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 201 2 شماره
صفحات -
تاریخ انتشار 1953