The anaerobic metabolism of malate of Saccharomyces bailii and the partial purification and characterization of malic enzyme View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1982-05

AUTHORS

J. T. Kuczynski, F. Radler

ABSTRACT

1. The main pathway of the anaerobic metabolism of L-malate in Saccharomyces bailii is catalyzed by a L-malic enzyme. 2. The enzyme was purified more than 300-fold. During the purification procedure fumarase and pyruvate decarboxylase were removed completely, and malate dehydrogenase and oxalacetate decarboxylase were removed to a very large extent. 3. Manganese ions are not required for the reaction of malic enzyme of Saccharomyces bailii, but the activity of the enzyme is increased by manganese. 4. The reaction of L-malic enzyme proceeds with the coenzymes NAD and (to a lesser extent) NADP. 5. The Km-values of the malic enzyme of Saccharomyces bailii were 10 mM for L-malate and 0.1 mM for NAD. 6. A model based on the activity and substrate affinity of malic enzyme, the intracellular concentration of malate and phosphate, and its action on fumarase, is proposed to explain the complete anaerobic degradation of malate in Saccharomyces bailii as compared with the partial decomposition of malate in Saccharomyces cerevisiae. More... »

PAGES

266-270

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00405891

DOI

http://dx.doi.org/10.1007/bf00405891

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1012907546

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7049107


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