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Lipoyl Synthase Requires Two Equivalents of S-Adenosyl-l-methionine To Synthesize One Equivalent of Lipoic Acid†

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Departments of Biochemistry and Molecular Biology and of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802
Cite this: Biochemistry 2004, 43, 21, 6378–6386
Publication Date (Web):May 4, 2004
https://doi.org/10.1021/bi049528x
Copyright © 2004 American Chemical Society
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    Abstract

    Lipoyl synthase (LipA) catalyzes the formation of the lipoyl cofactor, which is employed by several multienzyme complexes for the oxidative decarboxylation of various α-keto acids, as well as the cleavage of glycine into CO2 and NH3, with concomitant transfer of its α-carbon to tetrahydrofolate, generating N5,N10-methylenetetrahydrofolate. In each case, the lipoyl cofactor is tethered covalently in an amide linkage to a conserved lysine residue located on a designated lipoyl-bearing subunit of the complex. Genetic and biochemical studies suggest that lipoyl synthase is a member of a newly established class of metalloenzymes that use S-adenosyl-l-methionine (AdoMet) as a source of a 5‘-deoxyadenosyl radical (5‘-dA•), which is an obligate intermediate in each reaction. These enzymes contain iron−sulfur clusters, which provide an electron during the cleavage of AdoMet, forming l-methionine in addition to the primary radical. Recently, one substrate for lipoyl synthase has been shown to be the octanoylated derivative of the lipoyl-bearing subunit (E2) of the pyruvate dehydrogenase complex [Zhao, S., Miller, J. R., Jian, Y., Marletta, M. A., and Cronan, J. E., Jr. (2003) Chem. Biol. 10, 1293−1302]. Herein, we show that the octanoylated derivative of the lipoyl-bearing subunit of the glycine cleavage system (H-protein) is also a substrate for LipA, providing further evidence that the cofactor is synthesized on its target protein. Moreover, we show that the 5‘-dA• acts directly on the octanoyl substrate, as evidenced by deuterium transfer from [octanoyl-d15]H-protein to 5‘-deoxyadenosine. Last, our data indicate that 2 equiv of AdoMet are cleaved irreversibly in forming 1 equiv of [lipoyl]H-protein and are consistent with a model in which two LipA proteins are required to synthesize one lipoyl group.

    †

     This work was supported by NIH Grant GM-63847 (S.J.B.) and NIH Minority Predoctoral Fellowship Grant GM-64033 (N.M.N.).

    ‡

     Department of Biochemistry and Molecular Biology, The Pennsylvania State University.

    §

     Department of Chemistry, The Pennsylvania State University.

    *

     To whom correspondence should be addressed. Phone:  814-865-8793. Fax:  814-863-7024. E-mail:  [email protected].

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