Shiv K. Sah-Teli, Mikko J. Hynönen, Werner Schmitz, James A. Geraets, Jani Seitsonen, Jan Skov Pedersen, Sarah J. Butcher, Rik K. Wierenga, Rajaram Venkatesan; Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic β-oxidation trifunctional enzyme complexes. Biochem J 15 July 2019; 476 (13): 1975–1994. doi: https://doi.org/10.1042/BCJ20190314
Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic β-oxidation trifunctional enzyme complexes
|Author:||Sah-Teli, Shiv K.1; Hynönen, Mikko J.1; Schmitz, Werner2;|
1Faculty of Biochemistry and Molecular Medicine, and Biocenter Oulu, University of Oulu, Oulu, Finland
2Theodor-Boveri-Institut für Biowissenschaften der Universität Würzburg,Würzburg, Germany
3Helsinki Institute of Life Science, University of Helsinki, Helsinki, Finland
4Forschungszentrum Jülich, Jülich, Germany
5Department of Chemistry andInterdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus, Denmark
|Online Access:||PDF Full Text (PDF, 1.3 MB)|
|Persistent link:|| http://urn.fi/urn:nbn:fi-fe2020052639149
|Publish Date:|| 2020-06-24
The trifunctional enzyme (TFE) catalyzes the last three steps of the fatty acid β-oxidation cycle. Two TFEs are present in Escherichia coli, EcTFE and anEcTFE. EcTFE is expressed only under aerobic conditions, whereas anEcTFE is expressed also under anaerobic conditions, with nitrate or fumarate as the ultimate electron acceptor. The anEcTFE subunits have higher sequence identity with the human mitochondrial TFE (HsTFE) than with the soluble EcTFE. Like HsTFE, here it is found that anEcTFE is a membrane-bound complex. Systematic enzyme kinetic studies show that anEcTFE has a preference for medium- and long-chain enoyl-CoAs, similar to HsTFE, whereas EcTFE prefers short chain enoyl-CoA substrates. The biophysical characterization of anEcTFE and EcTFE shows that EcTFE is heterotetrameric, whereas anEcTFE is purified as a complex of two heterotetrameric units, like HsTFE. The tetrameric assembly of anEcTFE resembles the HsTFE tetramer, although the arrangement of the two anEcTFE tetramers in the octamer is different from the HsTFE octamer. These studies demonstrate that EcTFE and anEcTFE have complementary substrate specificities, allowing for complete degradation of long-chain enoyl-CoAs under aerobic conditions. The new data agree with the notion that anEcTFE and HsTFE are evolutionary closely related, whereas EcTFE belongs to a separate subfamily.
|Pages:||1975 - 1994|
|Type of Publication:||
A1 Journal article – refereed
|Field of Science:||
1182 Biochemistry, cell and molecular biology
The work was funded by the Academy of Finland grants to S.S.  and to R.V. . The work was also supported by a grant from the Faculty of Biochemistry and Molecular Medicine, University of Oulu to S.S.
|Academy of Finland Grant Number:||
293369 (Academy of Finland Funding decision)
289024 (Academy of Finland Funding decision)
© 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.