Pyruvate Dehydrogenase of Escherichia coli K 12
نویسندگان
چکیده
منابع مشابه
Molecular structure of the pyruvate dehydrogenase complex from Escherichia coli K-12.
The pyruvate dehydrogenase core complex from E. coli K-12, defined as the multienzyme complex that can be obtained with a unique polypeptide chain composition, has a molecular weight of 3.75 x 10(6). All results obtained agree with the following numerology. The core complex consists of 48 polypeptide chains. There are 16 chains (molecular weight = 100,000) of the pyruvate dehydrogenase componen...
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The monocarboxylate pyruvate is an important metabolite and can serve as sole carbon source for Escherichia coli. Although specific pyruvate transporters have been identified in two bacterial species, pyruvate transport is not well understood in E. coli. In the present study, pyruvate transport was investigated under different growth conditions. The transport of pyruvate shows specific activiti...
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Pyruvate is an important intermediate of central carbon metabolism and connects a variety of metabolic pathways in Escherichia coli Although the intracellular pyruvate concentration is dynamically altered and tightly balanced during cell growth, the pyruvate transport system remains unclear. Here, we identified a pyruvate transporter in E. coli using high-throughput transposon sequencing. The t...
متن کاملL-Threonine dehydrogenase of Escherichia coli K-12.
A rapid method for purifying L-threonine dehydrogenase from Escherichia coli K-12 cells, grown on a medium containing L_-threonine as carbon source, has been developed. The procedure consists of three fractionation steps of which the last is adsorption and elution of the enzyme from a column of Blue dextran-Sepharose. Homogeneous and stable samples of the dehydrogenase are obtained. L-Threonine...
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The binding of pyruvate dehydrogenase and dihydrolipoyl dehydrogenase (flavoprotein) to dihydrolipoyl transacetylase, the core enzyme of the E. coli pyruvate dehydrogenase complex [EC 1.2.4.1:pyruvate:lipoate oxidoreductase (decaryboxylating and acceptor-acetylating)], has been studied using sedimentation equilibrium analysis and radioactive enzymes in conjunction with gel filtration chromatogr...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1970
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1970.tb00879.x