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Literature summary for 1.2.1.104 extracted from

  • Akiyama, S.K.; Hammes, G.G.
    Elementary steps in the reaction mechanism of the pyruvate dehydrogenase multienzyme complex from Escherichia coli kinetics of acetylation and deacetylation (1980), Biochemistry, 19, 4208-4213 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli
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General Information

General Information Comment Organism
physiological function the time course for acetylation can be analyzed in terms of two kinetic processes. At long times 10 nmol of acetyl groups is incorporated per mg of enzyme complex. The slower process is much too slow to be of catalytic significance. The rate constant for the faster process is not dependent on enzyme concentration and reaches a limiting value of 40-65 per s at high pyruvate concentrations. The minimum molar turnover number of the enzyme complex is 420 per s (17.5 per s per pyruvate decarboxylase). The acetylated lipoic acids are deacetylated by coenzyme A at a rate much faster than that of acetylation. Complete deacetylation is obtained only if the deacetylation is carried out within seconds of the acetylation Escherichia coli