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. Author manuscript; available in PMC: 2015 Oct 1.
Published in final edited form as: Mol Microbiol. 2014 Sep 1;94(1):156–171. doi: 10.1111/mmi.12753

Fig. 1.

Fig. 1

Lipoate synthesis and scavenging pathways.

(A) Lipoate synthesis as observed in E. coli. Octanoyl groups from octanoyl-ACP (acyl carrier protein) are transferred to E2 proteins (and the H-protein) by an octanoyltransferase (LipB) followed by the insertion of sulfur atoms by a lipoate synthase (LipA).

(B) Lipoate synthesis as observed in B. subtilis. Octanoyl groups are transferred specifically to the H-protein by octanoyltransferase (LipM) and are subsequently distributed to the E2 proteins by an amidotransferase (LipL). As in E. coli, sulfur insertion is catalyzed by a lipoate synthase (LipA).

(C) Lipoate scavenging as observed in E. coli. Lipoate scavenged from the external environment is attached to E2 proteins (and the H-protein) by an ATP-dependent lipoate ligase (LplA).

(D) Lipoate scavenging as observed in B. subtilis. The lipoate ligase (LplJ) has specificity for the H-protein.