Antonie van Leeuwenhoek

, Volume 65, Issue 1, pp 63–69 | Cite as

Crotonobetaine reductase fromEscherichia coli — a new inducible enzyme of anaerobic metabolization of L(-)-carnitine

  • Sylke Roth
  • Kirsten Jung
  • Heinrich Jung
  • Rolf K. Hommel
  • Hans-Peter Kleber
Research Articles
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Accepted:

Abstract

Crotonobetaine reductase fromEscherichia coli 044 K74 is an inducible enzyme detectable only in cells grown anaerobically in the presence of L(-)-carnitine or crotonobetaine as inducers. Enzyme activity was not detected in cells cultivated in the presence of inducer plus glucose, nitrate, γ-butyrobetaine or oxygen, respectively. Fumarate caused an additional stimulation of growth and an increased expression of crotonobetaine reductase. The reaction product, γ-butyrobetaine, was identified by autoradiography. Crotonobetaine reductase is localized in the cytoplasm, and has been characterized with respect to pH (pH 7.8) and temperature optimum (40–45 °C). The K m value for crotonobetaine was determined to be 1.1×10−2M. γ-Butyrobetaine,D(+)-carnitine and choline are inhibitors of crotonobetaine reduction. For γ-butyrobetaine (K i =3×10−5M) a competitive inhibition type was determined. Various properties suggest that crotonobetaine reductase is different from other reductases of anaerobic respiration.

Key words

L(-)-carnitine crotonobetaine crotonobetaine reductase Escherichia coli 
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Copyright information

© Kluwer Academic Publishers 1994

Authors and Affiliations

  • Sylke Roth
    • 1
  • Kirsten Jung
    • 1
  • Heinrich Jung
    • 1
  • Rolf K. Hommel
    • 1
  • Hans-Peter Kleber
    • 1
  1. 1.Department of Biochemistry, Biosciences DivisionUniversity of LeipzigLeipzigGermany

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