Lysine Degradation Through The Saccharopine Pathway In Bacteria: Lkr And Sdh In Bacteria And Its Relationship To The Plant And Animal Enzymes

Lysine degradation through the saccharopine pathway has been shown only in plants and animals. Here, we show that bacteria possess the genes encoding lysine-ketoglutarate reductase (LKR) and saccharopine dehydrogenase (SDH). In Silicibacter, the contiguous lkr and sdh genes are interspersed, in another frame, by a polypeptide of unknown function. The bacterial enzyme does not contain the 110-amino-acid interdomain (ID) that intersperses the LKR and SDH domains of the plant enzyme. The ID was found in Cyanobacteria interspersing polypeptides without similarities and activities of LKR and SDH. The LKR/SDH bifunctional polypeptide of animals and plants may have arisen from a α-proteobacterium with a configuration similar to that of Silicibacter, whereas the ID in the plant enzyme may have been inherited from Cyanobacteria. © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.5866905911Azevedo, R.A., Arruda, P., Turner, W.L., Lea, P.J., The biosynthesis and metabolism of the aspartate derived amino acids in higher plants (1997) Phytochemistry, 46 (3), pp. 395-419. , DOI 10.1016/S0031-9422(97)00319-1, PII S0031942297003191Azevedo, R.A., Analysis of the aspartic acid metabolic pathway using mutant genes (2002) Amino Acids, 22, pp. 217-230Azevedo, R.A., Lancien, M., Lea, P.J., The aspartic acid metabolic pathway, an exciting and essential pathway in plants (2006) Amino Acids, 30, pp. 143-162Trupin, J.S., Broquist, H.P., Lysine biosynthesis in Neurospora crassa (1963) Fed. Proc., 22, pp. 243-250Bhattacharjee, J.K., Alpha-aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes (1985) Crit. Rev. Microbiol., 12, pp. 131-151Broquist, H.P., Trupin, J.S., Amino acid metabolism (1966) Ann. Rev. Biochem., 35, pp. 231-274Arruda, P., Sodek, L., Da Silva, W.J., Lysine-ketoglutarate reductase activity in developing maize endosperm (1982) Plant Physiol., 69, pp. 988-989Arruda, P., Kemper, E.L., Papes, F., Leite, A., Regulation of lysine catabolism in higher plants (2000) Trends in Plant Science, 5 (8), pp. 324-330. , DOI 10.1016/S1360-1385(00)01688-5Markovitz, P.J., Chuang, D.T., The bifunctional aminoadipic semialdehyde synthase in lysine degradation (1987) J. Biol. Chem., 262, pp. 9353-9358Gonçalves-Butruille, M., Szajner, P., Torigoi, E., Leite, A., Arruda, P., Purification and characterization of the bifunctional enzyme lysine-ketoglutarate reductase-saccharopine dehydrogenase from maize (1996) Plant Physiol., 11, pp. 765-771Kemper, E.L., Cord Neto, G., Papes, F., Moraes, K.C.M., Leite, A., Arruda, P., The role of Opaque2 in the control of lysine-degrading activities in developing maize endosperm (1999) Plant Cell, 11, pp. 1981-1993Kemper, E.L., Cord-Neto, G., Capella, A.N., Goncalves-Butruile, M., Azevedo, R.A., Arruda, P., Structure and regulation of the bifunctional enzyme lysine-oxoglutarate reductase-saccharopine dehydrogenase in maize (1998) European Journal of Biochemistry, 253 (3), pp. 720-729Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W., Lipman, D.J., Gapped BLAST and PSI-BLAST: A new generation of protein database search programs (1997) Nucleic Acids Research, 25 (17), pp. 3389-3402. , DOI 10.1093/nar/25.17.3389Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G., The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools (1997) Nucleic Acids Research, 25 (24), pp. 4876-4882. , DOI 10.1093/nar/25.24.4876Saitou, N., Nei, M., The neighbor-joining method: A new method for reconstructing phylogenetic trees (1987) Mol. Biol. Evol., 4 (406), p. 425Felsenstein, J., Confidence limits on phylogenies: An approach using the bootstrap (1985) Evolution, 39, pp. 783-791Kumar, S., Tamura, K., Nei, M., MEGA3: Integrated software for molecular evolutionary genetic analysis and sequence alignment (2004) Brief. Bioinf., 5, pp. 150-163Porchia, A.C., Curatti, L., Salerno, G.L., Sucrose metabolism in cyanobacteria: Sucrose synthase from Anabaena sp. strain PCC 7119 is remarkably different from the plant enzymes with respect to substrate affinity and amino-terminal sequence (1999) Planta, 210 (1), pp. 34-40. , DOI 10.1007/s004250050651Garrad, R., Schmidt, T.M., Bhattacharjee, J.K., Molecular and functional analysis of the LYS1 gene of Candida albicans (1994) Infection and Immunity, 62 (11), pp. 5027-5031Emelyanov, V.V., Rickettsiaceae, rickettsia-like endosymbionts, and the origin of mitochondria (2001) Biosci. Rep., 21, pp. 1-17Searcy, D.G., Metabolic integration during the evolutionary origin of mitochondria (2003) Cell Res., 13, pp. 229-238McFadden, G.I., Chloroplast origin and integration (2001) Plant Physiol., 125, pp. 50-5