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Pathway Description
Lipoic Acid Metabolism
Xenopus laevis
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2019-05-14
Last Updated: 2023-10-25
Lipoic acid is a compound derived from octanoic acid that is used as a cofactor in at least five enzyme systems, and is present in at least small amounts in most foods.However, these sources are covalently bound to other molecules, and aren't usable. Due to this, supplements of lipoic acid are synthesized chemically rather than obtained through natural sources. This pathway takes place entirely in the mitochondria, and begins with octanoyl bound to an acyl-carrier protein (ACP) from fatty acid biosynthesis. It can interact with lipoyl synthase to form lipoyl-ACP, after which it interacts with putative lipoyl transease in order to form protein N6-(lipoyl)lysine. Octanoyl-ACP can also interact with those enzymes in the opposite order, first the putative lipoyltransferase 2, forming protein N6-(octanoyl)lysine, and then lipoyl synthase to form protein N6-(lipoyl)lysine. At the same time, lipoic acid can form lipoyl-AMP after a reaction that exists in other organisms, and is likely present in Xenopus laevis, and the lipoyl-AMP can then interact with lipoyltransferase 1 to form the protein N6-(lipoyl)lysine. As all branches of the pathway produce this, it is the final and only product of this pathway.
References
Lipoic Acid Metabolism References
Gunther S, McMillan PJ, Wallace LJ, Muller S: Plasmodium falciparum possesses organelle-specific alpha-keto acid dehydrogenase complexes and lipoylation pathways. Biochem Soc Trans. 2005 Nov;33(Pt 5):977-80. doi: 10.1042/BST20050977.
Pubmed: 16246025
Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y: Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene. Eur J Biochem. 1999 Mar;260(3):761-7.
Pubmed: 10103005
Fujiwara K, Okamura-Ikeda K, Motokawa Y: Purification and characterization of lipoyl-AMP:N epsilon-lysine lipoyltransferase from bovine liver mitochondria. J Biol Chem. 1994 Jun 17;269(24):16605-9.
Pubmed: 8206978
Fujiwara K, Okamura-Ikeda K, Motokawa Y: Cloning and expression of a cDNA encoding bovine lipoyltransferase. J Biol Chem. 1997 Dec 19;272(51):31974-8. doi: 10.1074/jbc.272.51.31974.
Pubmed: 9405389
Fujiwara K, Takeuchi S, Okamura-Ikeda K, Motokawa Y: Purification, characterization, and cDNA cloning of lipoate-activating enzyme from bovine liver. J Biol Chem. 2001 Aug 3;276(31):28819-23. doi: 10.1074/jbc.M101748200. Epub 2001 May 29.
Pubmed: 11382754
Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H: Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site. J Biol Chem. 2005 Sep 30;280(39):33645-51. doi: 10.1074/jbc.M505010200. Epub 2005 Jul 25.
Pubmed: 16043486
Yasuno R, Wada H: Biosynthesis of lipoic acid in Arabidopsis: cloning and characterization of the cDNA for lipoic acid synthase. Plant Physiol. 1998 Nov;118(3):935-43.
Pubmed: 9808738
Gueguen V, Macherel D, Jaquinod M, Douce R, Bourguignon J: Fatty acid and lipoic acid biosynthesis in higher plant mitochondria. J Biol Chem. 2000 Feb 18;275(7):5016-25. doi: 10.1074/jbc.275.7.5016.
Pubmed: 10671542
Wada M, Yasuno R, Jordan SW, Cronan JE Jr, Wada H: Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase. Plant Cell Physiol. 2001 Jun;42(6):650-6. doi: 10.1093/pcp/pce081.
Pubmed: 11427685
Morris TW, Reed KE, Cronan JE Jr: Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product. J Biol Chem. 1994 Jun 10;269(23):16091-100.
Pubmed: 8206909
Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE: Assembly of the covalent linkage between lipoic acid and its cognate enzymes. Chem Biol. 2003 Dec;10(12):1293-302.
Pubmed: 14700636
Nesbitt NM, Baleanu-Gogonea C, Cicchillo RM, Goodson K, Iwig DF, Broadwater JA, Haas JA, Fox BG, Booker SJ: Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase. Protein Expr Purif. 2005 Feb;39(2):269-82. doi: 10.1016/j.pep.2004.10.021.
Pubmed: 15642479
Session AM, Uno Y, Kwon T, Chapman JA, Toyoda A, Takahashi S, Fukui A, Hikosaka A, Suzuki A, Kondo M, van Heeringen SJ, Quigley I, Heinz S, Ogino H, Ochi H, Hellsten U, Lyons JB, Simakov O, Putnam N, Stites J, Kuroki Y, Tanaka T, Michiue T, Watanabe M, Bogdanovic O, Lister R, Georgiou G, Paranjpe SS, van Kruijsbergen I, Shu S, Carlson J, Kinoshita T, Ohta Y, Mawaribuchi S, Jenkins J, Grimwood J, Schmutz J, Mitros T, Mozaffari SV, Suzuki Y, Haramoto Y, Yamamoto TS, Takagi C, Heald R, Miller K, Haudenschild C, Kitzman J, Nakayama T, Izutsu Y, Robert J, Fortriede J, Burns K, Lotay V, Karimi K, Yasuoka Y, Dichmann DS, Flajnik MF, Houston DW, Shendure J, DuPasquier L, Vize PD, Zorn AM, Ito M, Marcotte EM, Wallingford JB, Ito Y, Asashima M, Ueno N, Matsuda Y, Veenstra GJ, Fujiyama A, Harland RM, Taira M, Rokhsar DS: Genome evolution in the allotetraploid frog Xenopus laevis. Nature. 2016 Oct 20;538(7625):336-343. doi: 10.1038/nature19840.
Pubmed: 27762356
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