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PMID: 8060125 Published · ppublish English Journal Article

Crotonobetaine reductase from Escherichia coli--a new inducible enzyme of anaerobic metabolization of L(-)-carnitine.

Antonie van Leeuwenhoek ·Vol. 65 ·No. 1 ·1994-00-00 ·Pages 63-9

Roth S, Jung K, Jung H, Hommel RK, Kleber HP

Abstract

Crotonobetaine reductase from Escherichia 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, gamma-butyrobetaine or oxygen, respectively. Fumarate caused an additional stimulation of growth and an increased expression of crotonobetaine reductase. The reaction product, gamma-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 degrees C). The Km value for crotonobetaine was determined to be 1.1 x 10(-2M). gamma-Butyrobetaine, D(+)-carnitine and choline are inhibitors of crotonobetaine reduction. For gamma-butyrobetaine (Ki = 3 x 10(-5M)) a competitive inhibition type was determined. Various properties suggest that crotonobetaine reductase is different from other reductases of anaerobic respiration.

MeSH Terms
Anaerobiosis Carnitine/metabolism Cell-Free System Escherichia coli/enzymology Multienzyme Complexes Oxidoreductases/analysis
Chemicals
Multienzyme Complexes Oxidoreductases crotonobetaine reductase Carnitine
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Roth S
Department of Biochemistry, University of Leipzig, Germany.
Jung K
Jung H
Hommel R K
Kleber H P
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18 references, click to expand
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Article Info
Journal
Antonie van Leeuwenhoek
Abbr.
Antonie Van Leeuwenhoek
ISSN
0003-6072
Published
1994-00-00
Pages
63-9
Language
English
Region
Netherlands
NLM ID
0372625
Subset
IM
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