Differences in substrate specificity of V. cholerae FabH enzymes suggest new approaches for the development of novel antibiotics and biofuels

Hou, Jing; Zheng, Heping; Tzou, Wen‐Shyong; Cooper, David R.; Chruszcz, Maksymilian; Chordia, Mahendra D.; Kwon, Keehwan; Grabowski, Marek; Minor, Wladek

doi:10.1111/febs.14588

Title: Differences in substrate specificity of V. cholerae FabH enzymes suggest new approaches for the development of novel antibiotics and biofuels

Journal Article · Sat Jun 30 00:00:00 EDT 2018 · Federation of European Biochemical Societies (FEBS) Journal

DOI:https://doi.org/10.1111/febs.14588· OSTI ID:1458567

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^[1]; Tzou, Wen‐Shyong ^[2];

^[1];

^[3]; Chordia, Mahendra D. ^[1]; Kwon, Keehwan ^[4];

^[1];

^[1]

Department of Molecular Physiology and Biological Physics University of Virginia Charlottesville VA USA, Center for Structural Genomics of Infectious Diseases (CSGID) Consortium Charlottesville VA USA
Department of Molecular Physiology and Biological Physics University of Virginia Charlottesville VA USA, Department of Bioscience and Biotechnology and Center of Excellence for the Oceans National Taiwan Ocean University Keelung Taiwan
Department of Chemistry and Biochemistry University of South Carolina Columbia SC USA
Center for Structural Genomics of Infectious Diseases (CSGID) Consortium Charlottesville VA USA, Infectious Diseases Group J. Craig Venter Institute Rockville MD USA

Vibrio cholerae , the causative pathogen of the life‐threatening infection cholera, encodes two copies of β‐ketoacyl‐acyl carrier protein synthase III (vcFabH1 and vcFabH2). vcFabH1 and vcFabH2 are pathogenic proteins associated with fatty acid synthesis, lipid metabolism, and potential applications in biofuel production. Our biochemical assays characterize vcFabH1 as exhibiting specificity for acetyl‐CoA and CoA thioesters with short acyl chains, similar to that observed for FabH homologs found in most gram‐negative bacteria. vcFabH2 prefers medium chain‐length acyl‐CoA thioesters, particularly octanoyl‐CoA, which is a pattern of specificity rarely seen in bacteria. Structural characterization of one vcFabH1 and six vcFabH2 structures determined in either apo form or in complex with acetyl‐CoA/octanoyl‐CoA indicate that the substrate‐binding pockets of vcFabH1 and vcFabH2 are of different sizes, accounting for variations in substrate chain‐length specificity. An unusual and unique feature of vcFabH2 is its C‐terminal fragment that interacts with both the substrate‐entrance loop and the dimer interface of the enzyme. Our discovery of the pattern of substrate specificity of both vcFabH1 and vcFabH2 can potentially aid the development of novel antibacterial agents against V. cholerae . Additionally, the distinctive substrate preference of FabH2 in V. cholerae and related facultative anaerobes conceivably make it an attractive component of genetically engineered bacteria used for commercial biofuel production.

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Sponsoring Organization:: USDOE

Grant/Contract Number:: DE‐AC02‐06CH11357

OSTI ID:: 1458567

Journal Information:: Federation of European Biochemical Societies (FEBS) Journal, Journal Name: Federation of European Biochemical Societies (FEBS) Journal Vol. 285 Journal Issue: 15; ISSN 1742-464X

Publisher:: Wiley-BlackwellCopyright Statement

Country of Publication:: United Kingdom

Language:: English

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