Summary
Lipoic acid is a prosthetic group of the acyltransferase (E2) components of the pyruvate, (α-ketoglutarate, and branched chain α-keto acid dehydrogenase complexes, X component (the dihydrolipoamide dehydrogenase-binding protein) of the eucaryotic pyruvate dehydrogenase complex, and H-protein of the glycine cleavage system. The lipoyl moiety is attached in amide linkage to the ε-amino group of specific lysine residues of the proteins. Although the role of lipoic acid in these proteins has been well studied, intensive research on enzyme(s) concerning the lipoylation of proteins have not been undertaken until recently. In this chapter, we describe the recent development about the lipoylation of E2 component and H-protein as well as the historical view of the studies about lipoylation.
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Ali, S.T., and Guest, J.R. (1990) Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli. Biochem. J. 271: 139–145.
Borges, A., Hawkins, C.F., Packman, L.C. and Perham, R.N. (1990) Cloning and sequence analysis of the genes encoding the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Eur. J. Biochem. 194: 95–102.
Bradford, A.P., Howell, S., Aitken, A., James, L.A. and Yeaman, S.J. (1987a) Primary structure around the lipoate-attachment site on the E2 component of bovine heart pyruvate dehydrogenase complex. Biochem. J. 245: 919–922.
Bradford, A.P., Aitken, A., Beg, F., Cook, K.G. and Yeaman, S.J. (1987b) Amino acid sequence surrounding the lipoic acid cofactor of bovine kidney 2-oxoglutarate dehydrogenase complex. FEBS Lett. 222: 211 –214.
Brookfield, D.E., Green, J., Ali, S.T., Machado, R.S. and Guest, J.R. (1991) Evidence for two protein-lipoylation activities in Escherichia coli. FEBS Lett. 295: 13–16.
Burns, G., Brown, T., Hatter, K. and Sketch, J.R. (1988) Comparison of the amino acid sequences of the transacylase components of branched chain oxoacid dehydrogenase of Pseudomonas putida, and the pyruvate and 2-oxoglutarate dehydrogenases of Escherichia coli. Eur. J. Biochem. 176: 165–169.
Eisenberg, M.A., Parkas, O. and S.-C. Suing (1982) Purification and properties of the biotin repressor. A functional protein. J. Biol. Chem. 257: 15167–15173.
Fujiwara, K. and Motokawa, Y. (1983) Mechanism of the glycine cleavage reaction: Steady state kinetic studies of the P-protein-catalyzed reaction. J. Biol. Chem. 258: 8156–8162.
Fujiwara, K., Okamura-Ikeda, K. and Motokawa, Y. (1984) Mechanism of the glycine cleavage reaction: Further characterization of the intermediate attached to H-protein and of the reaction catalyzed by T-protein. J. Biol. Chem. 259: 10664–10668.
Fujiwara, K., Okamura-Ikeda, K. and Motokawa, Y. (1987) Amino acid sequence of the phosphopyridoxyl peptide from P-protein of the chicken liver glycine cleavage system. Biochem. Biophys. Res. Comm. 149: 621–627.
Fujiwara, K., Okamura-Ikeda, K. and Motokawa, Y. (1990) cDNA sequence, in vitro synthesis, and intramitochondrial lipoylation of H-protein of the glycine cleavage system. J. Biol. Chem. 265: 17463–17467.
Fujiwara, K., Okamura-Ikeda, K. and Motokawa, Y. (1991a) Lipoylation of H-protein of the glycine cleavage system: The effect of site-directed mutagenesis of amino acid residues around the lipoyllysine residue on the lipoate attachment. FEBS Lett. 293: 115–118.
Fujiwara, K., Okamura-Ikeda, K., Hayasaka, K. and Motokawa, Y. (1991b) The primary structure of human H-protein of the glycine cleavage system deduced by cDNA cloning. Biochem. Biophys. Res. Comm. 176: 711–716.
Fujiwara, K., Okamura-Ikeda, K. and Motokawa, Y. (1992) Expression of mature bovine H-protein of the glycine cleavage system in Escherichia coli and in vitro lipoylation of the apoform. J. Biol. Chem. 267: 20011–20016.
Fujiwara, K., Okamura-Ikeda, K. and Motokawa, Y. (1994) Purification and characterization of lipoyl-AMP:Nε- lysine lipoyltransferase from bovine liver mitochondria. J. Biol. Chem. 269: 16605–16609.
Griffin, T.A., Wynn, R.M. and Chuang, D.T. (1990) Expression and assembly of mature apotransacylase (E2bb) of bovine branched-chain α-keto acid dehydrogenase complex in Escherichia coli: Demonstration of transacylase activity and modification by lipoylation. J. Biol. Chem. 265: 12104–12110.
Hanemaaijer, R., Janssen, A., de Kok, A. and Veeger, C. (1988) The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii: Molecular cloning and sequence analysis. Eur. J. Biochem. 174: 593–599.
Kim, Y. and Oliver, D.J. (1990) Molecular cloning, transcriptional characterization, and sequencing of cDNA encoding the H-protein of the mitochondrial glycine decarboxylase complex in peas. J. Biol. Chem. 265: 848–853.
Kohara, Y., Akiyama, K. and Isono, K. (1987) The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50: 495–508.
Koyata, H. and Hiraga, K. (1991) The glycine cleavage system: Structure of a cDNA encoding human H-protein, and partial characterization of its gene in patients with hyperglycinemias. Am. J. Hum. Genet. 48: 351–361.
Lau, K.S., Griffin, T.A., Hu, C.-W.C. and Chuang, D.T. (1988) Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain α-keto acid dehydrogenase complex: Molecular cloning of human and bovine transacylase (E2) cDNAs. Biochemistry 21: 1972–1981.
Macherel, D., Lebrun, M., Gagnon, J., Neuburger, M. and Douce, R. (1990) cDNA cloning, primary structure and gene expression for H-protein, a component of the glycine-cleavage system (glycine decarboxylase) of pea (Pisum sativum) leaf mitochondria. Biochem. J. 268: 783–789.
Masaki, T., Fujihashi, T., Nakamura, K. and Soejima, M. (1981) Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1: II. Specificity and inhibition studies of Achromobacter protease I. Biochim. Biophys. Acta 660: 51–55.
Matuda, S., Nakano, K., Ohta, S., Shimura, M., Yamanaka, T., Nakagawa, S., Titani, K. and Miyata, T. (1992) Molecular cloning of dihydrolipoamide acetyltransferase of the rat pyruvate dehydrogenase complex: Sequence comparison and evolutionary relationship to other dihydrolipoamide acyltransferases. Biochim. Biophys. Acta 1131: 114–118.
Mitra, S.K. and Burma, D.P. (1965) Activation of lipoic acid and its transfer from the free pool to the protein-bound state. J. Biol. Chem. 240: 4072–4080.
Morris, T.W., Reed, K.E. and Cronan, J.E. (1994) Identification of the gene encoding lipoate-protein ligase A of Escherichia coli: Molecular clonig and characterization of the lplA gene and gene product. J. Biol. Chem. 269: 16091–16100.
Morris, T.W., Reed, K.E. and Cronan, J.E. (1995) Lipoic acid metabolism in Escherichia coli: The lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein. J. Bacteriology 111: 1–10.
Nakano, K., Matuda, S., Yamanaka, T., Tsubouchi, H., Nakagawa, S., Titani, K., Ohta, S. and Miyata, T. (1991) Purification and molecular cloning of succinyltransferase of the rat α-ketoglutarate dehydrogenase complex: Absence of a sequence motif of the putative E3 and/or El binding site. J. Biol. Chem. 266: 19013–19017.
Niu, X.-D., Browning, K.S., Behal, R.H. and Reed, L.J. (1988) Cloning and nucleotide sequence of the gene for dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 85: 7546–7550.
Okamura-Ikeda, K., Fujiwara, K. and Motokawa, Y. (1987) Mechanism of the glycine cleavage reaction: Properties of the reverse reaction catalyzed by T-protein. J. Biol. Chem. 262: 6746–6749.
Okamura-Ikeda, K., Ohmura, Y., Fujiwara, K. and Motokawa, Y. (1993) Cloning and nucleotide sequence of the gcv operon encoding the Escherichia coli glycine-cleavage system. Eur. J. Biochem. 216: 539–548.
Quinn, J., Diamond, A.G., Masters, A.K., Brookfield, D.E., Wallis, N.G. and Yeaman, S.J. (1993) Expression and lipoylation in Escherichia coli of the inner lipoyl domain of the E2 component of the human pyruvate dehydrogenase complex. Biochem. J. 289: 81–85.
Reed, L.J., Leach, F.R. and Koike, M. (1958) Studies on a lipoic acid-activating system. J. Biol. Chem. 232: 123–142.
Rosenberg, M. and Court, D. (1979) Regulatory sequences involved in the promotion and termination of RNA transcription. Ann. Rev. Genet. 13: 319–353.
Shine, J. and Dalgarno, L. (1974) The 3’-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA 71: 1342–1346.
Spencer, M.E., Darlison, M.G., Stephens, P.E., Duekenfield, I.K. and Guest, J.R. (1984) Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase. Eur. J. Biochem. 141: 361–374.
Stauffer, L.T., Steiert, P.S., Steiert, J.G. and Stauffer, G.V. (1991) An Escherichia coli protein with homology to the H-protein of the glycine cleavage enzyme complex from pea and chicken liver. DNA Sequence 2: 13–17.
Stephens, P.E., Darlison, M.G., Lewis, H.M. and Guest, J.R. (1983) The pyruvate dehydrogenase complex of Escherichia coli K12: Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component. Eur. J. Biochem. 133: 481–489.
Studier, F.W., Rosenberg, A.H., Dunn, J.J. and Dubendorff, J.W. (1990) Use of T7 RNA polymerase to direct expression of cloned genes. Meth. Enzymol. 185: 60–89.
Thekkumkara, T.J., Ho, L., Wexler, I.D., Pons, G., Liu, T.-C. and Patel, M.S. (1988) Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex. FEBS Lett. 240: 45–48.
Tsunoda, J.N. and Yasunobu, K.T. (1967) Mammalian lipoic acid activating enzyme. Arch. Biochem. Biophys. 118: 395–401.
Wallis, N.G. and Perham, R.N. (1994) Structural dependence of post–translational modification and reductive acetylation of the lipoyl domain of the pyruvate dehydrogenase multienzyme complex. J. Mol. Biol. 236: 209–216.
Westphal, A.H. and de Kok, A. (1990) The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii: 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component. Eur. J. Biochem. 187: 235–239.
Yamamoto, M., Koyata, H., Matsui, C. and Hiraga, K. (1991) The glycine cleavage system: Occurrence of two types of chicken H-protein mRNAs presumably formed by the alternative use of the polyadenylation consensus sequences in a single exon. J. Biol. Chem. 266: 3317–3322.
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© 1996 Birkhäuser Verlag Basel/Switzerland
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Motokawa, Y., Fujiwara, K., Okamura-Ikeda, K. (1996). Lipoylation of E2 component. In: Patel, M.S., Roche, T.E., Harris, R.A. (eds) Alpha-Keto Acid Dehydrogenase Complexes. MCBU Molecular and Cell Biology Updates. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-8981-0_8
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DOI: https://doi.org/10.1007/978-3-0348-8981-0_8
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