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A study of the properties of pyruvate kinase isolated from a mutant of Neurospora crassa: a comparison with the parental enzyme.

Authors
Type
Published Article
Journal
International Journal of Biochemistry
0020-711X
Publisher
Elsevier
Publication Date
Volume
15
Issue
4
Pages
523–529
Identifiers
PMID: 6221961
Source
Medline

Abstract

1. A mutant of Neurospora crassa has been isolated whose pyruvate kinase is twice as active as the wild type enzyme. 2. The purified mutant and the wild type enzymes exhibit similar immunological properties, pI values (6.4) and Arrhenius activation energy (11.2 kcal/mol). 3. Both the enzymes show hyperbolic saturation kinetics with ADP and sigmoidal kinetics with PEP. 4. The mutant enzyme displays a higher affinity for PEP and a greater extent of cooperativity in binding than the wild type. 5. Conformational alterations in the mutant enzyme are inferred on the basis of electrophoretic analyses and denaturation by urea, SDS and heat.

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