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

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