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

TITLE=A Novel Lipoate-Protein Ligase, Mhp-LplJ, Is Required for Lipoic Acid Metabolism in Mycoplasma hyopneumoniae

JOURNAL=Frontiers in Microbiology

VOLUME=11

YEAR=2021

URL=https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2020.631433

DOI=10.3389/fmicb.2020.631433

ISSN=1664-302X

ABSTRACT=<p>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 <italic>Mycoplasma hyopneumoniae</italic> (<italic>M. hyopneumoniae</italic>) Mhp-Lpl, which had been previously shown to have lipoate-protein ligase activity against glycine cleavage system H protein (GcvH) <italic>in vitro</italic>, did not lipoylate the lipoate-dependent subunit of dihydrolipoamide dehydrogenase (PdhD). Further studies indicated that a new putative lipoate-protein ligase in <italic>M. hyopneumoniae</italic>, MHP_RS00640 (Mhp-LplJ), catalyzes free lipoic acid attachment to PdhD <italic>in vitro</italic>. 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), <italic>M. hyopneumoniae</italic> growth was arrested <italic>in vitro</italic>. Taken together, these results indicate that Mhp-LplJ plays a vital role in lipoic acid metabolism of <italic>M. hyopneumoniae</italic>, which is of great significance to further understand the metabolism of <italic>M. hyopneumoniae</italic> and develop new antimicrobials against it.</p>