Enzymatic characterization of recombinant alpha-amylase in the Drosophila melanogaster species subgroup: is there an effect of specialization on digestive enzyme?
Feller, Georges ; Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie
Da Lage, Jean-Luc
Language :
English
Title :
Enzymatic characterization of recombinant alpha-amylase in the Drosophila melanogaster species subgroup: is there an effect of specialization on digestive enzyme?
Abe, K. (1958) Genetical and biochemical studies on amylase in Drosophila melanogaster. Jpn. J. Genet. 33, 138-145.
Araki, H., Inomata, N., and Yamazaki, T. (2001) Molecular evolution of duplicated amylase gene regions in Drosophila melanogaster: evidence of positive selection in the coding regions and selective constraints in the cis-regulatory regions. Genetics 157, 667-677.
Araki, H., Yoshizumi, S., Inomata, N., and Yamazaki, T. (2005) Genetic coadaptation of the amylase gene system in Drosophila melanogaster: evidence for the selective advantage of the lowest AMY activity and of its epistatic genetic background. J. Heredity 96, 388-395.
Bar-Even, A., Noor, E., Savir, Y., Liebermeister, W., Davidi, D., Tawfik, D. S., and Milo, R. (2011) The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters. Biochemistry 50, 4402-4410.
Benner, S. A. (1989) Enzyme kinetics and molecular evolution. Chem. Rev. 89, 789-806.
Bernfeld, P. (1955) Amylases, α and β. Methods Enzymol. 1, 149-158.
Beynon, R. J., and Bond, J. S. (2001) Proteolytic Enzymes: APractical Approach. Oxford University Press, Oxford; New York.
Bui, A. K. T., Bacic, A., and Pettolino, F. (2006) Polysaccharide composition of the fruit juice of Morinda citrifolia (Noni). Phytochemistry 67, 1271-1275.
Chandler, J. A., Morgan Lang, J., Bhatnagar, S., Eisen, J. A., and Kopp, A. (2011) Bacterial communities of diverse Drosophilaspecies: ecological context of a host-microbe model system. PLoS Genet. 7(9), e1002272.
Chapman, R. F. (1998) The Insects: Structure and Function. 4thed. Cambridge University Press, Cambridge, UK.
Cipolla, A., Delbrassine, F., Da Lage, J. L., and Feller, G. (2012) Temperature adaptations in psychrophilic, mesophilic and thermophilic chloride-dependent alpha-amylases. Biochimie94, 1943-1950.
D'Amico, S., Gerday, C., and Feller, G. (2001) Structural determinants of cold adaptation and stability in a large protein. J. Biol. Chem. 276, 25791-25796.
D'Amico, S., Sohier, J. S., and Feller, G. (2006) Kinetics and energetics of ligand binding determined by microcalorimetry: insights into active site mobility in a psychrophilic alpha-amylase. J. Mol. Biol. 358, 1296-1304.
Daïnou, O., Cariou, M. L., David, J. R., and Hickey, D. (1987) Amylase gene duplication: an ancestral trait in the Drosophila melanogaster species subgroup. Heredity 59, 245-251.
De Jong, G. A., and Scharloo, W. (1976) Environmental determination of selective significance or neutrality of amylase variants in Drosophila melanogaster. Genetics 84, 77-94.
Dean, M. D., and Ballard, J. W. (2004) Linking phylogenetics with population genetics to reconstruct the geographic origin of a species. Mol. Phyl. Evol. 32, 998-1009.
Doane, W. W. (1969) Amylase variants in Drosophila melanogaster: linkage studies and characterization of enzyme extracts. J. Exp. Zool. 171, 321-341.
Edgar, R. C. (2004) MUSCLE: Multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797.
Grinna, L. S., and Tschopp, J. F. (1989) Size distribution and general structural features of N-linked oligosaccharides from the methylotrophic yeast, Pichia pastoris. Yeast 5, 107-115.
Haq, I. (2002) Calorimetry in the fast lane: The use of ITC for obtaining enzyme kinetics constants. Microcal, LLC application note.
Hickey, D. A. (1977) Selection for amylase allozymes in Drosophila melanogaster. Evolution 31, 800-804.
Hickey, D. A. (1979) The geographical pattern of an enzyme polymorphism in D. melanogaster. Genetica 51, 1-4.
Hoorn, A. J. W., and Scharloo, W. (1978) The functional significance of amylase polymorphism in Drosophila melanogasterI. Properties of two amylase variants. Genetica 49, 173-180.
Inomata, N., Shibata, H., Okuyama, E., and Yamazaki, T. (1995) Evolutionary relationships and sequence variation of α-amylase variants encoded by duplicated genes in the Amylocus of Drosophila melanogaster. Genetics 141, 237-244.
Klarenberg, A. J., and Scharloo, W. (1986) Nonrandom association between structural Amy and regulatory map variants in Drosophila melanogaster. Genetics 114, 875-884.
Kikkawa, H. (1964) An electrophoretic study on amylase in Drosophila melanogaster. Jpn. J. Genet. 39, 401-411.
Kluh, I., Horn, M., Hyblova, J., Hubert, J., Doleckova-Maresova, L., Voburka, Z., Kudlikova, I., Kocourek, F., and Mares, M. (2005) Inhibitory specificity and insecticidal selectivity of α-amylase inhibitor from Phaseolus vulgaris. Phytochemistry66, 31-39
Kumagai, Y., Satoh, T., Inoue, A. and Ojima, T. (2013) Enzymaticproperties and primary structures of two alpha-amylase isozymes from the Pacific abalone Haliotis discus hannai. Comp. Biochem. Physiol. 164B, 80-88.
Lachaise, D., Capy, P., Cariou, M. L., Joly, D., Lemeunier, F., and David, J. R. (2004) Nine relative from one African ancestor: population biology and evolution of the Drosophila melanogaster subgroup species. In: The Evolution of Population Biology-Modern Synthesis (eds.: R. S. Singh and M. Uyenoyama), 315-342. Cambridge University Press, New York.
Lachaise, D., Cariou, M.-L., David, J., Lemeunier, F., Tsacas, L., and Ashburner, M. (1988) Historical biogeography of the Drosophila melanogaster species subgroup. Evol. Biol., 22, 159-225.
Lachaise, D., Harry, M., Solignac, M., Lemeunier, F., Bénassi, V., and Cariou, M.-L. (2000) Evolutionary novelties in islands: Drosophila santomea, a new melanogaster sister species from São Tom. Proc. Royal Soc. London Series B: Biological Sciences 267, 1487-1495.
Larson, S. B., Greenwood, A., Cascio, D., Day, J., and McPherson, A. (1994) Refined molecular structure of pig pancreatic α-amylase at 2. 1 Å resolution. J. Mol. Biol. 235, 1560-1584.
Legrand, D., Tenaillon, M. I., Matyot, P., Gerlach, J., Lachaise, D., and Cariou, M.-L. (2009) Species-wide genetic variation and demographic history of Drosophila sechellia, a species lacking population structure. Genetics 182, 1197-1206.
Lemeunier, F., Tsacas, L., David, J., and Ashburner, M. (1986) The melanogaster species group. In: The Genetics and Biology of Drosophila (eds,:M. Ashburner, H. L. Carson and J. N. Thompson Jr.), pp. 147-256. Academic Press, London, New York.
Levy, J. N., Gemmill, R. M., and Doane, W. W. (1985) Molecular cloning of alpha-amylase genes from Drosophila melanogaster. II. Clone organization and verification. Genetics 110, 313-324.
Milanovic, M., and Andjelkovic, M. (1992) Adaptive significance of amylase polymorphism in Drosophila. VI. Properties of two amylase variants and the effect of food components on amylase activity in Drosophila subobscura. Comp. Biochem. Physiol. 101B, 611-616.
Milanovic, M., Andjelkovic, M., and Stamenkovic-Bojic, G. (1989) Adaptive significance of amylase polymorphism in Drosophila. IV. A comparative study of biochemical properties of the alpha-amylase in Drosophila melanogaster, D. hydei, D. subobscura, and D. busckii. Comp. Biochem. Physiol. 93B, 629-634.
Miller, C. D., Murai, M., and Pen, F. (1956) The use of Pandanusfruit as food in Micronesia. Pac. Sci. 10, 3-16.
Powell, J. R., and Andjelkovic, M. (1983) Population genetics of Drosophila amylase. IV. Selection in laboratory populations maintained on different carbohydrates. Genetics 103, 675-689.
Prigent, S., Matoub, M., Rouland, C., and Cariou, M. L. (1998) Metabolic evolution in alpha-amylases from Drosophila virilisand D. repleta, two species with different ecological niches. Comp. Biochem. Physiol. 119B, 407-412.
Pytelkova, J., Hubert, J., Lepsik, M., Sobotnik, J., Sindelka, R., Krizkova, I., Horn, M., and Mares, M. (2009) Digestive alpha-amylases of the flour moth Ephestia kuehniella: adaptation to alkaline environment and plant inhibitors. FEBS J. 276, 3531-3546.
Qian, M., Haser, R., and Payan, F. (1995) Carbohydrate binding sites in a pancreatic α-amylase-substrate complex, derived from X-ray structure analysis at 2. 1 Å resolution. Protein Sci. 4, 747-755.
Ramasubbu, N., Ragunath, C., and Mishra, P. J. (2003) Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase. J. Mol. Biol. 325, 1061-1076.
Rio, B., Couturier, G., Lemeunier, F., and Lachaise, D. (1983) Evolution d'une spécialisation saisonière chez Drosophila erecta (Dipt., Drosophilidae). Ann. Soc. Ent. Fr. 19, 235-248.
R'Kha, S., Capy, P., and David, J. R. (1991) Host-plant specialization in the Drosophila melanogaster species complex: a physiological, behavioral, and genetical analysis. Proc. Natl. Acad. Sci. USA 88, 1835-1839.
Robyt, J. F., and French, D. (1970) The action pattern of porcine pancreatic alpha-amylase in relationship to the substrate binding site of the enzyme. J. Biol. Chem. 245, 3917-3927.
Rooney, L. W., and Pflugfelder, R. L. (1986) Factors affecting starch digestibility with special emphasis on sorghum and corn. J. Animal Sci. 63, 1607-1623.
Rosalizan, M. S., Rohani, M. Y., and Khatijah, I. (2010) Physico-chemical characteristics of Morinda citrifolia fruit during growth and maturation. J. Trop. Agric. Food Sci. 38, 21-30.
Rydberg, E. H., Sidhu, G., Vo, H. C., Hewitt, J., Cote, H. C., Wang, Y., Numao, S., MacGillivray, R. T., Overall, C. M., Brayer, G. D., et al. (1999) Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris. Protein Sci. 8, 635-643.
Shanbhag, S., and Tripathi, S. (2009) Epithelial ultrastructure and cellular mechanisms of acid and base transport in the Drosophila midgut. J. Exp. Biol. 212, 1731-1744.
Shibata, H., and Yamazaki, T. (1994) A comparative study of the enzymological features of alpha-amylase in the Drosophila melanogaster species subgroup. Jpn. J. Genet. 69, 251-258.
Shibata, H., and Yamazaki, T. (1995) Molecular evolution of the duplicated Amy locus in the Drosophila melanogaster species subgroup: concerted evolution only in the coding region and an excess of nonsynonymous substitutions in speciation. Genetics 141, 223-236.
Somero, G. N. (2004) Adaptation of enzymes to temperature: searching for basic "strategies". Comp. Biochem. Physiol. 139B, 321-333.
Todd, M. J., and Gomez, J. (2001) Enzyme kinetics determined using calorimetry: a general assay for enzyme activity?Ann. Biochem. 296, 179-187.
Tsacas, L., and Bächli, G. (1981) Drosophila sechellia, n. sp., huitième espèce du sous-groupe melanogaster des Iles Seychelles (Diptera, Drosophilidae). Rev. Fr. Entomol. 3, 146-150.
Tsacas, L., and Lachaise, D. (1974) Quatre nouvelles espèces de la Côte d'Ivoire du genre Drosophila, groupe melanogaster, et discussion de l'origine du sous-groupe melanogaster(Diptera: Drosophilidae). Ann. Univ. Abidjan Ser. E 7, 193-211.
Vanderborre, G., Smagghe, G., Ghesquière, B., Menschaert, G., Rao, R. N., Gevaert, K., and Van Damme, E. J. M. (2011) Diversity in protein glycosylation among insect species. PLoS One 6, e16682.
Yamate, N., and Yamazaki, T. (1999) Is the difference in alpha-amylase activity in the strains of Drosophila melanogasterwith different allozymes due to transcriptional or posttranscriptional control? Biochem. Genet. 37, 345-356.
Yamazaki, T., and Matsuo, Y. (1984) Genetic analysis of natural populations of Drosophila melanogaster in Japan. III. Genetic variability of inducing factors of amylase and fitness. Genetics 108, 223-235.
