Cloning, sequencing, and expression of the gene encoding extracellular α-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme

Applied and Environmental Microbiology

Volumn 63, Issue 9, 1997, Pages 3569-3576

  Dong, Guoqiang ^a,c   Vieille, Claire ^a   Savchenko, Alexei ^a   Zeikus, J Gregory ^a,b  

^a Michigan State University ^*  (United States)

^b MICHIGAN BIOTECHNOLOGY INSTITUTE   (United States)

^c AGRICULTURE AND AGRI FOOD CANADA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE;

ARTICLE; BINDING SITE; CALCIUM TRANSPORT; CELL MIGRATION; ENZYME ANALYSIS; ENZYME BINDING; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENE SEQUENCE; GENETIC RECOMBINATION; METAL INDUSTRY; MOLECULAR CLONING; NONHUMAN; THERMOSTABILITY;

BACILLUS LICHENIFORMIS; ESCHERICHIA COLI; PYROCOCCUS FURIOSUS;

EID: 0030826555     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.63.9.3569-3576.1997     Document Type: Article

References (47)

1. Adams, M. W. W. 1993. Enzymes and proteins from organisms that grow near and above 100°C. Annu. Rev. Microhiol. 47:627-658.
2. Adams, M. W. W., F. B. Perler, and R. M. Kelly. 1995. Extremozymes: expanding the limits of biocatalysis. Bio/Technology 13:662-668.
3. Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). 1993. Current protocols in molecular biology. Greene Publishing, New York, N.Y.
4. Bauer M. W., E. J. Bylina, R. V. Swanson, and R. M. Kelly. 1996. Comparison of a β-glucosidase and a β-mannosidase from the hyperthermophilic archaeon Pyrococcus furiosus: purification, characterization, gene cloning and sequence analysis. J. Biol. Chem. 271:23749-23755.
5. Bentley, I. S., and E. C. Williams. 1996. Starch conversion, p. 339-357. In T. Godfrey and S. I. West (ed.), Industrial enzymology, 2nd ed. Stockton Press, New York, N.Y.
6. Bernfeld, P. 1955. Amylases α-and β-. Methods Enzymol. 1:149-158.
7. Boel, E., L. Brady, A. M. Brzozowsk, Z. Derewenda, G. G. Dogson, V. J. Jensen, S. B. Petersen, H. Swift, L. Thim, and H. F. Woldike. 1990. Calcium binding in α-amylases: an X-ray diffraction study at 2.1-Å resolution of two enzymes from Aspergillus. Biochemistry 29:6244-6249.
8. Brown, S. H., H. R. Costantino, and R. M. Kelly. 1990. Characterization of amylolytic activities associated with the hyperthermophilic archaebacterium Pyrococcus furiosus. Appl. Environ. Microbiol. 56:1985-1991.
9. Brown, S. H., and R. M. Kelly. 1993. Characterization of amylolytic enzymes, having both α-1,4 and α-1,6 hydrolytic activity, from the thermophilic archaea Pyrococcus furiosus and Thermococcus litoralis. Appl. Environ. Microbiol. 59:2614-2621.
10. Buisson, G., E. Duee, R. Haser, and F. Payan. 1987. Three dimensional structure of porcine pancreatic α-amylase at 2.9 Å resolution. Role of calcium in structure and activity. EMBO J. 6:3909-3916.
11. Chan, M. K., S. Mukund, A. Kletzin, M. W. W. Adams, and D. C. Rees. 1995. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267:1463-1469.
12. Chung Y. C., T. Kobayashi, H. Kanai, T. Akiba, and T. Kudo. 1995. Purification and properties of extracellular amylase from the hyperthermophilic archaeon Thermococcus profundus DT5432. Appl. Environ. Microbiol. 61: 1502-1506.
13. Costantino, H. R., S. H. Brown, and R. M. Kelly. 1990. Purification and characterization of an α-glucosidase from a hyperthermophilic archaebactrium, Pyrococcus furiosus, exhibiting a temperature optimum of 105 to 115°C. J. Bacteriol. 172:3654-3660.
14. Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
15. DiRuggiero, J., F. T. Robb, R. Jagus, H. H. Klump, K. M. Borgest, M. Kessel, X. Mai, and M. W. W. Adams. 1993. Characterization, cloning, and in vitro expression of the extremely thermostable glutamate dehydrogenase from the hyperthermophilic archaeon, ES4. J. Biol. Chem. 268:17767-17774.
16. Dong, G., C. Vieille, and J. G. Zeikus. 1997. Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme. Appl. Environ. Microbiol. 63:3577-3584.
17. Fiala, G., and K. O. Stetter. 1986. Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archacbacteria growing optimally at 100°C. Arch. Microbiol. 145:56-61.
18. Fukusumi, S., A. Kamizono, S. Horinouchi, and T. Beppu. 1988. Cloning and nucleotide sequence of a heat-stable amylase gene from an anaerobic thermophile, Dictyoglomus thermophilum. Eur. J. Biochem. 174:15-21.
19. Hain, J., W.-D. Reiter, U. Hudepohl, and W. Zillig. 1992. Elements of an archaeal promoter defined by mutational analysis. Nucleic Acids Res. 20: 5423-5428.
20. Henikoff, S. 1984. Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene 28:351-359.
21. Horinouchi, S., S. Fukusumi, T. Ohshima, and T. Beppu. 1988. Cloning and expression in Escherichia coli of two additional amylase genes of a strictly anaerobic thermophile. Dictyoglomus thermophilum, and their nucleotide sequences with extremely low guanine-plus-cytosine contents. Eur. J. Biochem. 176:243-253.
22. 8-barrel domain and evolutionary relationship of other amylolytic enzymes. J. Protein Chem. 12:791-805.
23. Koch, R., A. Spreinat, K. Lemke, and G. Antranikian. 1991. Purification and properties of a hyperthermoactive α-amylase from archaebacterium Pyrococcus woesei. Arch. Microbiol. 155:572-578.
24. Koch, R., P. Zablowski, A. Spreinat, and G. Antranikian. 1990. Extremely thermostable amylolytic enzyme from archaebacterium Pyrococcus furiosus. FEMS Microbiol. Lett. 71:21-26.
25. Laderman, K. A., K. Asada, T. Uemori, H. Mukai, Y. Taguchi, I. Kato, and C. B. Anfinsen. 1993. α-Amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus, cloning and sequencing of the gene and expression in Escherichia coli. J. Biol. Chem. 268:24402-24407.
26. Laderman, K. A., B. R. Davis, H. C. Krutzsch, M. S. Lewis, Y. V. Griko, P. L. Privalov, and C. B. Anfinsen. 1993. The purification and characterization of an extremely thermostable α-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. J. Biol. Chem. 268:24394-24401.
27. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
28. Machius, M., G. Wiegand, and R. Huber. 1995. Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution. J. Mol. Biol. 246:545-559.
29. Perrin, D. D., and B. Dempsey (ed.). 1979. Buffers for pH and metal ion control. Chapman and Hall, Ltd., London, United Kingdom.
30. Qian, M., R. Haser, G. Buisson, E. Duée, and F. Payan. 1994. The active center of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2-Aα. Biochemistry 33: 6284-6294.
31. Qian, M., R. Haser, and F. Payan. 1993. Structure and molecular model refinement of pig pancreatic α-amylase at 2.1 Å resolution. J. Mol. Biol. 231:785-799.
32. Reiter, W.-D., P. Palm, and W. Zillig. 1988. Transcription termination in the archeabacterium Sulfolobus: signal structures and linkage to transcription initiation. Nucleic Acids Res. 16:2445-2459.
33. Rüdiger, A., P. L. Jorgensen, and G. Antranikian. 1995. Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyrococcus woesei after cloning and expression of its gene in Escherichia coli. Appl. Environ. Microbiol. 61:567-575.
34. Schumann, J., A. Wrba, R. Jaenicke, and K. O. Stetter. 1991. Topographical and enzymatic characterization of amylases from the extremely thermophilic eubacterium Thermotoga maritima. FEBS Lett. 282:122-126.
35. Teplyakov, A. V., I. P. Kuranova, E. H. Harutyunyan, B. K. Vainshtein, C. Frömmel, W. E. Höhne, and K. S. Wilson. 1990. Crystal structure of thermitase at 1.4 Å resolution. J. Mol. Biol. 214:261-279.
36. Tiboni, O., P. Cammarano, and A. M. Sanangelantoni. 1993. Cloning and sequencing of the gene encoding glutamine synthetase 1 from the archaeum Pyrococcus woesei: anomalous phylogenies inferred from analysis of archaeal and bacterial glutamine synthetase I sequences. J. Bacteriol. 175:2961-2969.
37. Tomazic, S. J., and A. M. Klibanov. 1988. Mechanisms of irreversible thermal inactivation of Bacillus α-amylases. J. Biol. Chem. 263:3086-3091.
38. Tomazic, S. J., and A. M. Klibanov. 1988. Why is one Bacillus α-amylase more resistant against irreversible thermoinactivation than another? J. Biol. Chem. 263:3092-3096.
39. Vieille, C., D. S. Burdette, and J. G. Zeikus. 1996. Thermozymes. Biotechnol. Annu. Rev. 2:1-83.
40. Vieille, C., J. M. Hess, R. M. Kelly, and J. G. Zeikus. 1995. xylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana. Appl. Environ. Microbiol. 61:1867-1875.
41. Violet, M., and J.-C. Meunier. 1989. Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis α-amylase. Biochem. J. 263:665-670.
42. Volkin, D. B., and C. R. Middaugh. 1992. The effect of temperature on protein structure, p. 215-247. In T. J. Ahern and M. C. Manning (ed.), Stability of protein pharmaceuticals, part A. Chemical and physical pathways of protein degradation. Plenum Press, New York, N.Y.
43. Voorhorst, W. G. B., R. I. L. Eggen, A. C. M. Geerling, C. Platteeuw, R. J. Siezen, and W. M. de Vos. 1996. Isolation and characterization of the hyperthermostable serine protease, pyrolysin, and its gene from the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 271:20426-20431.
44. Voorhorst, W. G. B., R. I. L. Eggen, E. J. Luesink, and W. M. de Vos. 1995. Characterization of the celB gene coding for β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coli. J. Bacteriol. 177:7105-7111.
45. Watson, M. E. E. 1984. Compilation of published signal sequences. Nucleic Acids Res. 12:5145-5264.
46. Yasukawa, T., C. Kanei-Ishii, T. Maekawa, J. Fujimoto, T. Yamamoto, and S. Ishii. 1995. Increase of solubility of foreign proteins in Escherichia coli by coproduction of the bacterial thioredoxin. J. Biol. Chem. 270:25328-25331.
47. Zwickl, P., S. Fabry, C. Bogedain, A. Haas, and R. Hensel. 1990. Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus woesei: characterization of the enzyme, cloning and sequencing of the gene, and expression in Escherichia coli. J. Bacteriol. 172: 4329-4338.