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Article

Structural basis for the broad substrate specificity of two acyl-CoA dehydrogenases FadE5 from mycobacteria.

Proceedings of the National Academy of Sciences of the United States of America - 14 Jul 2020

Chen Xiaobo, Chen Jiayue, Yan Bing, Zhang Wei, Guddat Luke W, Liu Xiang, Rao Zihe

Abstract excerpt

FadE, an acyl-CoA dehydrogenase, introduces unsaturation to carbon chains in lipid metabolism pathways. Here, we report that FadE5 from Mycobacterium tuberculosis (MtbFadE5) and Mycobacterium smegmatis (MsFadE5) play roles in drug resistance and exhibit broad specificity for linear acyl-CoA substrates but have a preference for those with long carbon chains. Here, the structures of MsFadE5 and MtbFadE5, in the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 32601219
DOI: 10.1073/pnas.2002835117
PMCID: PMC7368279

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