Abstract
InPenaeus vannamei, α-amylase is the most important glucosidase and is present as at least two major isoenzymes which have been purified. In order to obtain information on their structure, a hepatopancreas cDNA library constructed in phage lambda-Zap II (Strategene) was screened using a synthetic oligonucleotide based on the amino acid sequence of a V8 staphylococcal protease peptide ofP. vannamei α-amylase. Three clones were selected: AMY SK 37 (EMBL sequence accession number: X 77318) is the most complete of the analyzed clones and was completely sequenced. It contains the complete cDNA sequence coding for one of the major isoenzymes of shrimp amylase. The deduced amino acid sequence shows the existence of a 511-residue-long pre-enzyme containing a highly hydrophobic signal peptide of 16 amino acids. Northern hybridization of total RNA with the amylase cDNA confirms the size of the messenger at around 1,600 bases. AMY SK 28, which contains the complete mature sequence of amylase, belonged to the same family characterized by a common 3′ terminus and presented four amino acid changes. Some other variants of this family were also partially sequenced. AMY SK 20 was found to encode a minor variant of the protein with a different 3′ terminus and 57 amino acid changes.
Phylogenetic analysis established with the conserved amino acid regions of the (β/α) eight-barrel domain and with the total sequence ofP. vannamei showed close evolutionary relationships with mammals (59–63% identity) and with insect α-amylase (52–62% identity). The use of conserved sequences increased the level of similarity but it did not alter the ordering of the groupings. Location of the secondary structure elements confirmed the high level of sequence similarity of shrimp α-amylase with pig α-amylase.
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Abele LO, Felgenhauer BE (1986) Phylogenetic and phenetic relationships among the lower Decapods. J Crust Biol 6:385–400
Abele LG (1991) Comparison of morphological and molecular phylogeny of the Decapoda. Memoirs of the Queensland Museum 31: 101–108
Boer PM, Hickey DA (1986) The α-amylase gene inDrosophila melanogaster: nucleotide sequence, gene structure and expression. Nucleic Acid Res 14:8399–8411
Burkenroad MD (1963) The evolution of the Eucarida (Crustacea, Eumalacostaca) in relation to fossil record. Tulane Studies Geol 2:3–16
Cisne JL (1974) Trilobites and the origin of arthropods. Science 186: 13–18
Chirgwin JJ, Przbyla AE, MacDonald RJ, Rutter WJ (1979) Isolation of biologicaly active ribonucleic acid from sources enriched in ribonucleases. Biochemistry 18:5294–5299
Davis BT (1964) Disc electrophoresis. II—Method and application to human serum proteins. Ann NY Acad Sci 321:404–428
Dessen P, Fondrat C, Valencien C, Mugnier C (1990) BISANCE: French service for access to biomolecular sequence databases. Comp Appl Biosci 6:355–356
Felgenhauer BE, Abele GL (1983) Phylogenetic relationships among shrimp-like Decapods. In: Schram FR (ed) Crustaceans issue 1: Crustacean phylogeny. AA Balkema, Rotterdam, Netherlands pp 291–311
Glaessner MF (1969) Decapoda. In: Moore RC (ed) Treatise on invertebrate Paleontology. part R, Arthropoda 4, 11 R399–R533. Geological Society of America, Boulder, Colorado and the University of Kansas Press, Lawrence
Grossman GL, James AA (1993) The salivary gland of the vector mosquitoAedes aegypti expresses a novel member of the amylase gene family. Insect Mol Biol 1:223–232
Hagenbuchle O, Bovery R, Young RA (1980) Tissue specific expression of mouse α-amylase genes: nucleotide sequence of isoenzyme mRNAs from pancreatic and salivary glands. Cell 21:179–187
Hein J (1990) Unified approach to aligment and phylogenies. In: Doolittle RF (ed) Methods in Enzymology Acad Press NY, 183: 626–644
Hickey DA, Benkel BF, Boer PH, Genest Y, Abukashwa S, Ben David G (1987) Enzyme encoding genes as molecular clocks: the molecular evolution of animal alpha-amylases. J Mol Evol 26:252–256
Huang N, Stebbins GL, Rodriguez RL (1992) Classification and evolution of α-amylases in plants. Proc Natl Acad Sci USA 89:7526–7530
Ikeo K, Takahashi K, Gojoborit J (1995) Different evolution histories of Kringle and protease domains in serine proteases: a typical example of domain evolution. J Mol Evol 40:331–334
Janecek S (1992) New conserved amino acid region of α-amylase in the third loop of their (β/α)8-barrel domain. Biochem J 288:1069–1075
Janecek S (1994a) Sequence similarities and evolutionary relationships of microbial, plant and α-amylases. Eur J Biochem 224:519–524
Janecek S (1994b) Parallel β/α-barrels of α-amylase, cyclodextrin, glycosyltransferase and oligo-1-6 glucosidase versus the barrel of β-amylase: evolutionary distance is a reflection of unrelated sequence. Febs Lett 353:119–123
Jespersen H, McGregor E, Henrissat B, Sierks MR, Svensson B (1993) Starch and glycogen-debranching and branching enzymes: prediction of structural features of the (β/α)8-barrel domain and evolutionary relationships to other amylolytic enzymes. J Prof Chem 12:791–805
Keller P, Kaufman DL, Allan BJ, Williams BL (1971) Isoenzymes of human parotid α-amylases. Biochemistry 10:4867–4874
Kim W, Abele LG (1990) Molecular phylogeny of selected decapod crustaceans based on 18S rRNA nucleotide sequences. J Crust Biol 10:1–13
Kyte J, Doolytle RF (1982) A single method for displaying the hydropathic character of a protein. J Mol Biol 157:105–132
Le Moullac G (1995) Adaptation des enzymes digestives à l'alimentation chez la crevettePenaeus vannamei (Crustacea Decapoda). Thèse EPHE, 120 p
Levy JN, Gemmil RM, Doane WW (1985) Molecular cloning of alpha-amylase fromDrosophila melanogaster. II Clone organisation and verification. Genetics 11:313–324
McDonald RJ, GreRar MM, Swain WF, Pietet RL, Thomas G, Rutter WJ (1980) Structure of a family of rat amylase genes. Nature 287: 117–122
McGregor EA (1993) Relationships between structure and activity in the α-amylase family of starch metabolising enzymes. Starch 45: 232–237
McKay RM, Baird S, Dove MJ, Errat JA, Gines M, Moranelli F, Nasim A, Willick GE, Yaguchi M (1985) Glucanase gene diversity in prokaryotic and eukaryotic organisms. Biosystems 18:279–292
Nakajima R, Imanaka T, Aiba S (1986) Comparison of amino acid sequences of eleven α-amylases. Appl Microbiol Biotech 23:353–360
Nakamura Y, Ogama M, Nishida T, Emi M, Kosaki G, Himeno S, Matsubara K (1984) Sequence of cDNAs for human salivary and pancreatic α-amylases. Gene 28:263–270
Ovendeen JR, Brasher DJ, White RWG (1992) Mitochondrial analysis of the red rock lobsterJasus edwardsii supports an apparent absence of population subdivision throughout Australasia. Mar Biol 112:319–326
Palumbi SR, Benzie J (1991) Large mitochondrial DNA differences between morphologically similar Penaeid shrimps. Mol Mar Biol Biotech 1:27–34
Pasero L, Mazzei-Pierron Y, Abadie B, Chicheportiche Y, Marchis-Mouren G (1986) Complete amino-acid sequence and location of the five disulfide bridges in porcine b pancreatic α-amylases. Biochim Biophys Acta 869:147–157
Pictet R, McDonald RJ, Swain WF, Grebar MM, Hobart PM, Crawform R, Shen LD, Bell G, Rutter WJ (1981) Differentiation of the pancreas: an analysis of the structure of the amylase and insulin genes. Fortsh Zool B 26:227–245
Raimbaud E, Buleon A, Perez S, Henrissat B (1989) Hydrophobic cluster analysis of the primary sequences of α-amylases. Int J Biol Macromol 2:217–225
Schram FR (1982) The fossil record and evolution of crustacea. In: Abele LG (ed) The biology of crustacea. Acad Press NY, London, 1:241–304
Sellos D, Van-Wormhoudt A (1992) Molecular cloning of a c-DNA that encodes a serine protease with chymotryptic and collagenolytic activities in the hepatopancreas of the shrimpPenaeus vannamei (Crustacea, Decapoda). FEBS Lett 309:219–224
Van Wormhoudt A (1980) Régulation d'activité de l'α-amylase à différentes températures d'adaptation et en fonction de l'ablation des pédoncules oculaires et du stade de mue chezPalaemon serratus. Biochem System Ecol 8:193–203
Van Wormhoudt A (1983) Variations immunoquantitatives de l' α-amylase au cours du cycle d'intermue à différences saisons chezPalaemon serratus (Crustacea Decapoda). Mar Biol 74:127–132
Van Wormhoudt A, Favrel P (1988) Electrophoretic characterization ofPalaemon elegans (Crustacea Decapoda) α-amylase system: study of amylase polymorphism during the intermolt cycle. Comp Biochem Physiol 89B:201–207
Van Wormhoudt A, Bourreau G, Le Moullac G (1995) Amylase polymorphism in Crustacea Decapoda: electrophoretic and immunological studies. Biochem System Ecol 23:139–149
Van Wormhoudt A, Le Moullac G, Klein B, Sellos D (1996) Adjustment of the expression of digestive enzymes to casein level in food inPenaeus vannamei. Br J Nutr 55 (in press)
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Van Wormhoudt, A., Sellos, D. Cloning and sequencing analysis of three amylase cDNAs in the shrimpPenaeus vannamei (Crustacea decapoda): evolutionary aspects. J Mol Evol 42, 543–551 (1996). https://doi.org/10.1007/BF02352284
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DOI: https://doi.org/10.1007/BF02352284