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. 2020 May 12;25(10):2277. doi: 10.3390/molecules25102277

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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(A) LTA biosynthesis occurs at the Gram-positive bacterial cell membrane. The α-phosphoglucomutase PgcA converts glucose-6-phosphate to glucose-1-phosphate, then uridyltransferase GtaB activates uridine triphosphate (UTP) to produce UDP-glc. Glc₂-DAG is then produced from YpfP transfering two glucose molecules from UDP-Glc to DAG. Glc₂-DAG is moved to the outer membrane by LtaA followed by LtaS adding glycerol phosphate to Glc₂-DAG generate LTA. WTA biosynthesis begins in the cytoplasm where TarO plays a key role in generate the diphospho-ManNAc-GlcNAc-GroP polymer. TarGH then exports the WTA polymer to the cell membrane where the LytR-CpsA-Psr (LCP) proteins catalyze the covalent bond between the WTA and peptidoglycan. The d-alanine moieties are added by DltABC. (B) HSGN-94 and HSGN-189 inhibit LTA biosynthesis. Tunicamycin and Targocil inhibit WTA biosynthesis via inhibition of TarO and TarGH, respectively.

(A) LTA biosynthesis occurs at the Gram-positive bacterial cell membrane. The α-phosphoglucomutase PgcA converts glucose-6-phosphate to glucose-1-phosphate, then uridyltransferase GtaB activates uridine triphosphate (UTP) to produce UDP-glc. Glc₂-DAG is then produced from YpfP transfering two glucose molecules from UDP-Glc to DAG. Glc₂-DAG is moved to the outer membrane by LtaA followed by LtaS adding glycerol phosphate to Glc₂-DAG generate LTA. WTA biosynthesis begins in the cytoplasm where TarO plays a key role in generate the diphospho-ManNAc-GlcNAc-GroP polymer. TarGH then exports the WTA polymer to the cell membrane where the LytR-CpsA-Psr (LCP) proteins catalyze the covalent bond between the WTA and peptidoglycan. The d-alanine moieties are added by DltABC. (B) HSGN-94 and HSGN-189 inhibit LTA biosynthesis. Tunicamycin and Targocil inhibit WTA biosynthesis via inhibition of TarO and TarGH, respectively.