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一种新型硫辛酸蛋白连接酶Mhp-LplJ是[具体生物]中硫辛酸代谢所必需的。

A Novel Lipoate-Protein Ligase, Mhp-LplJ, Is Required for Lipoic Acid Metabolism in .

作者信息

Jin Jin, Chen Huan, Wang Ning, Zhu Kemeng, Liu Huanhuan, Shi Dongfang, Xin Jiuqing, Liu Henggui

机构信息

State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.

Department of Preventive Veterinary Medicine, College of Veterinary Medicine, Northeast Agricultural University, Harbin, China.

出版信息

Front Microbiol. 2021 Jan 18;11:631433. doi: 10.3389/fmicb.2020.631433. eCollection 2020.

DOI:10.3389/fmicb.2020.631433
PMID:33584596
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7873978/
Abstract

Lipoic acid is a conserved cofactor necessary for the activation of several critical enzyme complexes in the aerobic metabolism of 2-oxoacids and one-carbon metabolism. Lipoate metabolism enzymes are key for lipoic acid biosynthesis and salvage. In this study, we found that () Mhp-Lpl, which had been previously shown to have lipoate-protein ligase activity against glycine cleavage system H protein (GcvH) , did not lipoylate the lipoate-dependent subunit of dihydrolipoamide dehydrogenase (PdhD). Further studies indicated that a new putative lipoate-protein ligase in , MHP_RS00640 (Mhp-LplJ), catalyzes free lipoic acid attachment to PdhD . In a model organism, Mhp-LplJ exhibited lipoate and octanoate ligase activities against PdhD. When the enzyme activity of Mhp-LplJ was disrupted by lipoic acid analogs, 8-bromooctanoic acid (8-BrO) and 6,8-dichlorooctanoate (6,8-diClO), growth was arrested . Taken together, these results indicate that Mhp-LplJ plays a vital role in lipoic acid metabolism of , which is of great significance to further understand the metabolism of and develop new antimicrobials against it.

摘要

硫辛酸是2-氧代酸有氧代谢和一碳代谢中几种关键酶复合物激活所必需的保守辅因子。硫辛酸代谢酶是硫辛酸生物合成和补救的关键。在本研究中，我们发现，先前已证明对甘氨酸裂解系统H蛋白（GcvH）具有硫辛酸-蛋白连接酶活性的（）Mhp-Lpl，不会使二氢硫辛酰胺脱氢酶（PdhD）的硫辛酸依赖性亚基硫辛酸化。进一步研究表明， 中的一种新的假定硫辛酸-蛋白连接酶MHP_RS00640（Mhp-LplJ）催化游离硫辛酸与PdhD结合。在一种模式生物中，Mhp-LplJ对PdhD表现出硫辛酸和辛酸连接酶活性。当Mhp-LplJ的酶活性被硫辛酸类似物8-溴辛酸（8-BrO）和6,8-二氯辛酸（6,8-diClO）破坏时，生长停滞。综上所述，这些结果表明Mhp-LplJ在 的硫辛酸代谢中起重要作用，这对于进一步了解 的代谢以及开发针对它的新型抗菌药物具有重要意义。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/1ac9873bcbf9/fmicb-11-631433-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/b89bfd5824de/fmicb-11-631433-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/1d98a4e325ed/fmicb-11-631433-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/8dd68578b447/fmicb-11-631433-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/af069c18b07f/fmicb-11-631433-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/b21e05a7f5dc/fmicb-11-631433-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/7af6502a4264/fmicb-11-631433-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/16f2b0fb7bc5/fmicb-11-631433-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/1ac9873bcbf9/fmicb-11-631433-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/b89bfd5824de/fmicb-11-631433-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/1d98a4e325ed/fmicb-11-631433-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/8dd68578b447/fmicb-11-631433-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/af069c18b07f/fmicb-11-631433-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/b21e05a7f5dc/fmicb-11-631433-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/7af6502a4264/fmicb-11-631433-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/16f2b0fb7bc5/fmicb-11-631433-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8872/7873978/1ac9873bcbf9/fmicb-11-631433-g008.jpg

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