Role of Trp140 at subsite -6 on the maltohexaose production of maltohexaose-producing amylase from alkalophilic Bacillus sp.707

Protein Science

Volumn 15, Issue 3, 2006, Pages 468-477

  Kanai, Ryuta ^a   Haga, Keiko ^b   Akiba, Toshihiko ^a   Yamane, Kunio ^c   Harata, Kazuaki ^a  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^b UNIVERSITY OF TSUKUBA   (Japan)

^c NATIONAL FOOD RESEARCH INSTITUTE   (Japan)

Author keywords

Crystal structure; G6 amylase; Site directed mutagenesis; Stacking interaction

Indexed keywords

AMYLASE; AMYLOSE; CARBOHYDRATE DERIVATIVE; INDOLE; LEUCINE; MALTOHEXAOSE; OLIGOSACCHARIDE; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVITY; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL;

ALPHA-GLUCOSIDASES; BACILLUS; BACTERIAL PROTEINS; BINDING SITES; CATALYTIC DOMAIN; HORDEUM; LIGANDS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OLIGOSACCHARIDES; TRYPTOPHAN;

BACILLUS SP. 707;

EID: 33644545736     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.051877006     Document Type: Article

References (27)

1. Allen, J.D. and Thoma, J.A. 1976. Subsite mapping of enzymes. Application of the depolymerase computer model to two α-amylases. Biochem. J. 159: 105-120.
2. Andre, G., Buleon, A., Haser, R., and Tran, V. 1999. Amylose chain behavior in an interacting context. III. Complete occupancy of the AMY2 barley α-amylase cleft and comparison with biochemical data. Biopolymers 50: 751-762.
3. Bak-Jensen, K.S., Andre, G., Gottschalk, T.E., Paes, G., Tran, V., and Svensson, B. 2004. Tyrosine 105 and threonine 212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley α-amylase 1. J. Biol. Chem. 279: 10093-10102.
4. Brünger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., et al. 1998. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54: 905-921.
5. Brzozowski, A.M., Lawson, D.M., Turkenburg, J.P., Bisgaard-Frantzen, H., Svendsen, A., Borchert, T.V., Dauter, Z., Wilson, K.S., and Davies, G.J. 2000. Structural analysis of a chimeric bacterial α-amylase. High-resolution analysis of native and ligand complexes. Biochemistry 39: 9099-9107.
6. Chan, S.J., Weiss, J., Konrad, M., White, T., Bahl, C., Yu, S.D., Marks, D., and Steiner, D.F. 1981. Biosynthesis and periplasmic segregation of human proinsulin in Escherichia coli. Proc. Natl. Acad. Sci. 78: 5401-5405.
7. Conrad, B., Hoang, V., Polley, A., and Hofemeister, J. 1995. Hybrid Bacillus amyloliquefaciens X Bacillus licheniformis α-amylases construction, properties and sequence determinants. Eur. J. Biochem. 230: 481-490.
8. Davies, G.J., Brzozowski, A.M., Dauter, Z., Rasmussen, M.D., Borchert, T.V., and Wilson, K.S. 2005. Structure of a Bacillus halmapalus family 13 α-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 ̊ resolution. Acta Crystallogr. D Biol. Crystallogr. 61: 190-193.
9. Hagihara, H., Igarashi, K., Hayashi, Y., Endo, K., Ikawa-Kitayama, K., Ozaki, K., Kawai, S., and Ito, S. 2001. Novel α-amylase that is highly resistant to chelating reagents and chemical oxidants from alkalophilic Bacillus isolate KSM-K38. Appl. Environ. Microbiol. 67: 1744-1750.
10. Igarashi, K., Hatada, Y., Hagihara, H., Saeki, K., Takaiwa, M., Uemura, T., Ara, K., Ozaki, K., Kawai, S., Kobayashi, T., et al. 1998. Enzymatic properties of a novel liquefying α-amylase from an alkalophilic Bacillus isolate and entire nucleotide and amino acid sequences. Appl. Environ. Microbiol.64: 3282-3289.
11. Kainuma, K., Kobayashi, S., Ito, T., and Suzuki, S. 1972. Isolation and action pattern of maltohexaose producing amylase from Aerobacter-aerogenes. FEBS Lett. 26: 281-285.
12. Kandra, L., Gyémánt, G., Remenyik, J., Hovánszki, G., and Lipták, A. 2002. Action pattern and subsite mapping of Bacillus licheniformis α-amylase (BLA) with modified maltooligosaccharide substrates. FEBS Lett. 518: 79-82.
13. Kanai, R., Haga, K., Akiba, T., Yamane, K., and Harata, K. 2004. Biochemical and crystallographic analyses of maltohexaose-producing amylase from alkalophilic Bacillus sp. 707. Biochemistry 43: 14047-14056.
14. Kimura, K., Tsukamoto, A., Ishii, Y., Takano, T., and Yamane, K. 1988. Cloning of a gene for maltohexaose producing amylase of an alkalophilic Bacillus and hyper-production of the enzyme in Bacillus subtilis. Appl. Microbiol. Biotech. 27: 372-377.
15. Kraulis, P.J. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950.
16. Laskowski, A.R., MacArthur, M.W., Moss, D.S., and Thornton, J.M. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283-291.
17. Machius, M., Declerck, N., Huber, R., and Wiegand, G. 1998. Activation of Bacillus licheniformis α-amylase through a disorder→order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad. Structure 6: 281-292.
18. Maeda, I., Kiribuchi, S., and Nakamura, M. 1978. Digestion of barley starch granules by the combined action of α- and β-amylases purified from barley and barley malt. Agric. Biol. Chem. 42: 259-267.
19. Momma, M. 2000. Cloning and sequencing of the maltohexaose-producing amylase gene of Klebsiella pneumoniae. Biosci. Biotechnol. Biochem. 64: 428-431.
20. Nakamura, A., Haga, K., Ogawa, S., Kuwano, K., Kimura, K., and Yamane, K. 1992. Functional relationships between cyclodextrin glucanotransferase from an alkalophilic Bacillus and α-amylases: Site-directed mutagenesis of the conserved two Asp and one Glu residues. FEBS Lett. 296: 37-40.
21. Nakamura, A., Haga, K., and Yamane, K. 1994. Four aromatic residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: Effects of replacements on substrate binding and cyclization characteristics. Biochemistry 33: 9929-9936.
22. Nonaka, T., Fujihashi, M., Kita, A., Hagihara, H., Ozaki, K., Ito, S., and Miki, K. 2003. Crystal structure of calcium-free α-amylase from Bacillus sp. strain KSM-K38 (AmyK38) and its sodium ion binding sites. J. Biol. Chem. 278: 24818-24824.
23. Otwinowski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326.
24. Robert, X., Haser, R., Mori, H., Svensson, B., and Aghajari, N. 2005. Oligosaccharide binding to barley α-amylase 1. J. Biol.Chem. 280: 32968-32978.
25. Saito, N. 1973. A thermophilic extracellular α-amylase from Bacillus licheniformis. Arch. Biochem. Biophys. 155: 290-298.
26. Suvd, D., Fujimoto, Z., Takase, K., Matsumura, M., and Mizuno, H. 2001. Crystal structure of Bacillus stearothermophilus α-amylase: Possible factors determining the thermostability. J. Biochem. 129: 461-468.
27. Wallace, A.C., Laskowski, R.A., and Thornton, J.M. 1995. LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8: 127-134.