Biochemical and structural characterization of the BioZ enzyme engaged in bacterial biotin synthesis pathway

Sitao Zhang, Yongchang Xu, Hongxin Guan, Tao Cui, Yuling Liao, Wenhui Wei, Jun Li, Bachar H. Hassan, Huimin Zhang, Xu Jia, Songying Ouyang () and Youjun Feng ()
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Sitao Zhang: Provincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal University
Yongchang Xu: Zhejiang University School of Medicine
Hongxin Guan: Provincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal University
Tao Cui: Northwestern Polytechnical University
Yuling Liao: College of Life Sciences, South China Agricultural University
Wenhui Wei: Zhejiang University School of Medicine
Jun Li: Zhejiang University School of Medicine
Bachar H. Hassan: Stony Brook University
Huimin Zhang: Zhejiang University School of Medicine
Xu Jia: Chengdu Medical College
Songying Ouyang: Provincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal University
Youjun Feng: Zhejiang University School of Medicine

Nature Communications, 2021, vol. 12, issue 1, 1-18

Abstract: Abstract Biotin is an essential micro-nutrient across the three domains of life. The paradigm earlier step of biotin synthesis denotes “BioC-BioH” pathway in Escherichia coli. Here we report that BioZ bypasses the canonical route to begin biotin synthesis. In addition to its origin of Rhizobiales, protein phylogeny infers that BioZ is domesticated to gain an atypical role of β-ketoacyl-ACP synthase III. Genetic and biochemical characterization demonstrates that BioZ catalyzes the condensation of glutaryl-CoA (or ACP) with malonyl-ACP to give 5’-keto-pimeloyl ACP. This intermediate proceeds via type II fatty acid synthesis (FAS II) pathway, to initiate the formation of pimeloyl-ACP, a precursor of biotin synthesis. To further explore molecular basis of BioZ activity, we determine the crystal structure of Agrobacterium tumefaciens BioZ at 1.99 Å, of which the catalytic triad and the substrate-loading tunnel are functionally defined. In particular, we localize that three residues (S84, R147, and S287) at the distant bottom of the tunnel might neutralize the charge of free C-carboxyl group of the primer glutaryl-CoA. Taken together, this study provides molecular insights into the BioZ biotin synthesis pathway.

Date: 2021
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DOI: 10.1038/s41467-021-22360-4

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