Pyruvate decarboxylase from Zymomonas mobilis. Isolation and partial characterization View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1986-11

AUTHORS

S. Bringer-Meyer, K. -L. Schimz, H. Sahm

ABSTRACT

Pyruvate decarboxylase (EC 4.1.1.1) from the ethanol producing bacterium Zymomonas mobilis was purified to homogeneity. This enzyme is an acidic protein with an isoelectric point of 4.87 and has an apparent molecular weight of 200,000±10,000. The enzyme showed a single band in sodium dodecylsulfate gel electrophoresis with a molecular weight of 56,500±4,000 which indicated that the enzyme consists of four probably identical subunits. The dissociation of the cofactors Mg2+ and thiamine pyrophosphate at pH 8.9 resulted in a total loss of enzyme activity which could be restored to 99.5% at pH 6.0 in the presence of both cofactors. For the apoenzyme the apparent Km values for Mg2+ and thiamine pyrophosphate were determined to be 24 μM and 1.28 μM. The apparent Km value for the substrate pyruvate was 0.4 mM. Antiserum prepared against this purified pyruvate decarboxylase failed to crossreact with cell extracts of the reportedly pyruvate decarboxylase positive bacteria Sarcina ventriculi, Erwinia amylovora, or Gluconobacter oxydans, or with cell extracts of Saccharomyces cerevisiae. More... »

PAGES

105-110

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00402334

DOI

http://dx.doi.org/10.1007/bf00402334

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