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

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

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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 ORG GREENS UNFLAVOURED 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 DRY/DAMAGED SHAMPOO 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.