The Pyruvate Dehydrogenase Complex of E. coli K-12 Structure and Synthesis

  • U. Henning
  • O. Vogel
  • W. Busch
  • J. E. Flatgaard
Part of the Colloquium der Gesellschaft für Biologische Chemie 13.–15. April 1972 in Mosbach/Baden book series (MOSBACH, volume 23)

Abstract

Since the pioneering experiments of Gunsalus and Hager [1] and of Koike, Reed, and Carroll [2, 3] α-ketoacid dehydrogenase complexes from a number of sources have been studied from many aspects. These enzymes catalyze an oxidative decarboxylation according to:
$$R - \mathop C\limits^{\mathop \parallel \limits^0 } - C{O_2}H + CoA + NAD + \to C{O_2} + R - \mathop C\limits^{\mathop \parallel \limits^0 } - S - CoA + NADH + H + $$
(1)
This overall reaction, proceeding with enzyme bound intermediates, requires three different enzyme components present in the complex : an α-ketoacid dehydrogenase (enzyme 1, E 1), a dihydrolipoamide transacetylase (E 2), and a dihydrolipoamide dehydrogenase (E 3). In the case of the pyruvate dehydrogenase complex they effect reaction (1) by the following sequence of reactions:
$$Pyruvate + TPP - E1 \to C{0_2} + {\text{Hydroxyethyl - TPP - E1}}$$
(2)
$${\text{Hydroxyethyl - TPP - E1 + Lipoyl - E2}} \to {\text{S - acetyl - dihydrolipoyl - E2 + TPP - E1}}$$
(3)
$${\text{S - Acetyl - dihydrolipoyl - E2 + CoA}} \to {\text{Acetyl - CoA}} + {\text{Dihydrolipoyl - E2}}$$
(4)
$${\text{Dihydrolipoyl - E2 + FAD - E3}} \to {\text{Lipoyl - E2 + reducedFAD - E3}}$$
(5)

Keywords

Recombination Titration Sedimentation Electrophoresis Serine 

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Copyright information

© Springer-Verlag Berlin · Heidelberg 1972

Authors and Affiliations

  • U. Henning
    • 1
  • O. Vogel
    • 1
  • W. Busch
    • 1
  • J. E. Flatgaard
    • 1
  1. 1.Max-Planck-Institut für BiologieTübingenGermany

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