The primary structure of the subunit in bacillus thermoamyloliquefaciens kp1071 molecular weight 540,000 homohexameric α-glucosidase ii belonging to the glycosyl hydrolase family 31

Bioscience, Biotechnology and Biochemistry

Volumn 64, Issue 7, 2000, Pages 1379-1393

  Kashiwabara, Shin Ichi ^a   Azuma, Sayuri ^a   Tsuduki, Masao ^a   Suzuki, Yuzuru ^a  

^a KYOTO PREFECTURAL UNIVERSITY   (Japan)

Author keywords

Bacillus thermoamyloliquefaciens; Gene cloning; Glycosyl hydrolase family 31; Multiple sequence alignments; Thermostable homohexameric glucosidase

Indexed keywords

ALPHA GLUCOSIDASE; AMINO ACID; BACTERIAL DNA;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BACILLUS; BACTERIAL GENE; CHEMISTRY; CLASSIFICATION; DNA SEQUENCE; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; MOLECULAR WEIGHT; NUCLEOTIDE SEQUENCE; RABBIT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

ALPHA-GLUCOSIDASES; AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; BACILLUS; BASE SEQUENCE; DNA, BACTERIAL; GENES, BACTERIAL; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; RABBITS; SEQUENCE ANALYSIS, DNA; SEQUENCE ANALYSIS, PROTEIN; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0034220797     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.64.1379     Document Type: Article

References (60)

1. Suzuki, Y., Nagayama, T., Nakano, H., and Oishi, K., Purification and characterization of a maltotrio-genic a-amylase I and a maltogenic a-amylase II capable of cleaving a-16-bonds in amylopectin. Starch/ Stärke, 39, 211-214 & 246-252 (1987).
2. Suzuki, Y., Oishi, K., Nakano, H., and Nagayama, T., A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-l,6-glucosidases. Appl. Microbiol. Biotechnol., 26, 546-551 (1987).
3. Suzuki, Y., Yonezawa, K., Hattori, M., and Takii, Y., Assignment of Bacillus thermoamyloliquefaciens KP1071 a-glucosidase I to an exo-o;-l,4-glucosidase, and its striking similarity to bacillary oligo-1,6-glucosidases in Af-terminal sequence and in structural parameters calculated from the amino acid composition. Eur. J. Biochem., 205, 249-256 (1992).
4. r 540,000 homohexameric a-glucosidase with both exo-cel,4-glucosidase and oligo-l,6-glucosidase activities. Eur. J. Biochem., 245, 129-136 (1997).
5. Takii, Y., Takahashi, K., Yamamoto, K., Sogabe, Y., and Suzuki, Y., Bacillus stearothermophilus ATCC12016 a-glucosidase specific for a-1,4 bonds of maltosaccharides and a-glucans shows high amino acid sequence similarities to seven a-D-glucohydro-lases with different substrate specificity. Appl. Microbiol. Biotechnol., 44, 629-634 (1996).
6. Watanabe, K., Hata, Y., Kizaki, H., Katsube, Y., and Suzuki, Y., The refined crystal structure of Bacillus cereus oligo-l,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization. J. Mol. Biol., 269, 142-153 (1997).
7. Svensson, B., Protein engineering in the a-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol. Biol., 25, 141-157 (1994).
8. Sawai, T., Sanuki, A., and Suzuki, Y., Thermostability of a homohexameric a-glucosidase of the facultative thermophile Bacillus thermoamyloliquefaciens KP1071. Oyo Toshitu Kagaku, 45, 331 (1998).
9. Henrissat, B. and Davies, G., Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol., 1, 637-644 (1997).
10. Henrissat, B., Glycosidase families, Biochem. Soc. Transac., 26, 153-156 (1998).
11. Chiba, S., Molecular mechanism in a-glucosidase and glucoamylase. Biosci. Biotechnol. Biochem., 61, 1233-1239 (1997).
12. from the hyperthermophilic archaeon Sulfolobus solfataricus. J. Bacteriol.,180, 1287-1295 (1998).
13. Kashiwabara, S., Oda, M., and Suzuki, Y., Primary structure of a-glucosidase III of the thermophile Bacillus thermoamyloliquefaciens KP1071. In Abstracts, Annual Meeting of Japan Society for Bioscience, Biotechnology, and Agrochemistry, pp. 291, Tokyo (1997).
14. Okuyama, M., Okuno, A., Mori, H., Kimura, A., and Chiba, S., Acid residues essential for the catalytic activity of Schizosaccharomyces pombe a-glucosi-dase. J. Appl. Glycosci., 46, 372 (1999).
15. Mori, H., Okuyama, M., Kimura, A., and Chiba, S., Carboxyl groups of Asp481, Glu484, and Asp647 essential for activity of a-glucosidase from Schizosaccharomyces pombe. Abstracts Papers in 3rd Carbohydrate Bioengineering Meeting, University of Newcastle, 11th—14th April 1999, p. 7.7.
16. Chiba, S., Studies on molecular mechanisms in glycosidases. Nippon Nogeikagaku Kaishi, 73, 1001-1012 (1999).
17. Watanabe, K., Kitamura, K., Iha, H., and Suzuki, Y., Primary structure of the oligo-l,6-glucosidase of Bacillus cereus ATCC7064 deduced from the nucleotide sequence of the cloned gene. Eur. J. Biochem.,192, 609-620 (1990).
18. Trinder, P., Determination of glucose in blood using glucose oxidase with an alternative oxygen acceptor. Ann. Clin. Biochem., 6, 24-27 (1969).
19. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., Protein measurement with the Folin phenol regent. J. Biol. Chem., 193, 265-275 (1951).
20. Sanger, F., Determination of nucleotide sequence in DNA. Science, 214, 1205-1210 (1981).
21. Sambrook, J., Fritsch, E. F., and Maniatis, T., “Molecular Cloning: A Laboratory Manual” 2nd ed., Cold Spring Harbor Laboratory, Cold Spring Harbor, (1989).
22. Feinberg, A. P. and Vogelstein, B., A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem., 132, 6-13 (1983).
23. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 117, 680-685 (1970).
24. Towbin, H., Staehelin, T., and Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA, 76, 4350-4354 (1979).
25. Kashiwabara, S., Matsuki, Y., Kishimoto, T., and Suzuki, Y., Clustered proline residues around the ac-tive-site cleft in thermostable oligo-l,6-glucosidase of Bacillus flavocaldarius KP1228. Biosci. Biotechnol. Biochem., 62, 1093-1102 (1998).
26. Rosenberg, M. and Court, D., Regulatory sequences involved in the promotion and termination of RNA transcription. Annu. Rev. Genet., 13, 319-353 (1979).
27. Lewin, B., 3' Ends are generated by termination and by cleavage reactions. In “Gene” 6th ed., Oxford University Press, Oxford, pp. 913-917 (1997).
28. Fekkes, P. and Driessen, A. J. M., Protein targeting to the bacterial cytoplasmic membrane. Microbiol. Mol. Biol. Rev., 63, 161-173 (1999).
29. Zacharius, R. M., Zell, T. E., Morrison, J. H., and Woodlock, J. J., Glycoprotein staining following electrophoresis on acrylamide gel. Anal. Biochem., 30, 148-152 (1969).
30. Rost, B. and Sander, C., Combining evolutionary information and neural networks to predict protein secondary structure. Proteins: Struct. Fund. Genet., 19, 55-72 (1994).
31. Woodcock, S., Mornon, S. P., and Henrissat, B., Detection of secondary structure elements in proteins by hydrophobic cluster analysis. Protein Eng., 5, 629-635 (1992).
32. Rost, B. and Sander, C., Conservation and prediction of solvent accessibility in protein families. Proteins: Struct. Fund. Genet., 20, 216-226 (1994).
33. Hoefsloot, L. H., Hoogeveen-Westerveld, M., Kroos, M. A., van Beeumen, J., Reuser, A. J., and Oostra, B. A., Primary structure and processing of lysosomal a-glucosidase; homology with the intestinal sucrase-isomaltase complex. EMBO J., 1, 1697-1704 (1988).
34. Matsui, H., Iwanami, S., Ito, H., Mori, H., Honma, M., and Chiba, S., Cloning and sequencing of a cDNA encoding a-glucosidase from sugar beet. Biosci. Biotechnol. Biochem., 61, 875-880 (1997).
35. Tibbot, B. K. and Skadsen, R. W., Molecular cloning and characterization of a gibberellin-inducible putative a-glucosidase gene from barley. Plant Mol. Biol., 30, 229-241 (1996).
36. Sugimoto, M., Furui, S., and Suzuki, Y., Molecular cloning and characterization of a cDNA encoding a-glucosidase from spinach. Plant Mol. Biol., 33, 765-768 (1997).
37. Sugimoto, M. and Suzuki, Y., Molecular cloning, sequencing, and expression of a cDNA encoding a-glucosidase from Mucor javanicus. J. Biochem., 119, 500-505 (1996).
38. Hunzikor, W., Spiess, M., Semenza, G., and Lodish, H. F., The sucrase-isomaltase complex: primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein. Cell, 46, 227-234 (1986).
39. Chantret, I., Lacasa, M., Chevalier, G., Rut, J., Islam, I., Mantei, N., Edwards, Y., Swallow, D., and Rousset, M., Sequence of the complete cDNA and the 5' structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase. Biochem. J., 285, 915-923 (1992).
40. from Aspergillus oryzae. Biosci. Biotechnol. Biochem.,59, 1516-1521 (1995).
41. Chandrasena, G., Osterholm, D. E., Sunitha, I, and Henning, S. J., Cloning and sequencing of a full-length rat sucrase-isomaltase-encoding cDNA. Gene, 150, 355-360 (1994).
42. Alam, M. S., Nakashima, S., Deyashiki, Y., Banno, Y., Hara, A., and Nozawa, Y., Molecular cloning of a gene encoding acid a-glucosidase from Tetrahyme-na pyriformis. J. Eukaryot. Microbiol., 43, 295-303 (1996).
43. Kinsella, B. T., Hogan, S., Larkin, A., and Cantwell, B. A., Primary structure and processing of the Candida tsukubaensis a-glucosidase. Homology with the rabbit intestinal sucrase-isomaltase complex and human lysosomal a-glucosidase. Eur. J. Biochem., 202, 657-664 (1991).
44. Nakamura, A., Nishimura, I., Yokoyama, A., Lee, D.-G., Hidaka, M., Masaki, H., Kimura, A., Chiba, S., Uozumi, T., Cloning, sequencing of an a-glucosi-dase gene from Aspergillus niger and its expression in A. nidulans. J. Biotechnol., 53, 75-84 (1997).
45. and its expression in Saccharomyces cerevisiae. Gene, 95, 111-121 (1990).
46. Cid, H., Bunster, M., Arriagada, E., and Campos, M., Prediction of secondary structure of proteins by means of hydrophobicity profiles. FEBS Lett., 150, 247-254 (1982).
47. Kyte, I. and Doolittle, R. F., A simple method for displaying the hydropathic character of a protein. J. Mol. Biol., 157, 105-132 (1982).
48. Semenza, G., Anchoring and biosynthesis of stalked brush border membrane proteins: glycosidases and peptidases of enterocytes and renal tubuli. Ann. Rev. Cell Biol., 2, 255-313 (1986).
49. Naim, H. Y., Niermann, T., Kleinhans, U., Hollenberg, C. P., and Strasser, A. W. M., Striking structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal a-glucosidase and Schwanninomyces occidentalis glucoamylase are derived from a common ancestral gene. FEBS Lett., 294, 109-112 (1991).
50. Nichols, B. L., Eldering, J., Avery, S., Hahn, D., Quaroni, A., and Sterchi, E., Human small intestinal maltase-glucoamylase cDNA cloning: homology to sucrase-isomaltase. J. Biol. Chem., 273, 3076-3081 (1998).
51. and two insertions/deletions in the acid a-glucosidase locus of patients of differing phenotype. Biochem. Biophys. Res. Commun., 244, 921-927 (1998).
52. Levitt, M. and Chothia, C., Structural patterns in globular proteins. Nature, 261, 552-558 (1976).
53. Howard, S. and Withers, S. G., Labeling and identification in the postulated acid /base catalyst in the a-glucosidase from Saccharomyces cerevisiae using a novel bromoketone C-glycoside. Biochemistry, 37, 3858-3864 (1998).
54. Yu, S., Bojsen, K., Svensson, B., and Marcussen, J., a-l,4-Glucan lyases producing 1,5-anhydro-D-fruc-tose from starch and glycogen have sequence similarity to a-glucosidases. Biochim. Biophys. Acta, 1433, 1-15 (1999).
55. Chou, P. Y. and Fasman, G. D., Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol., 47, 45-148 (1978).
56. Garnier, J., Osguthorpe, D. J., and Robson, B., Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol., 120, 97-120 (1978).
57. Kashiwabara, S., Ogawa, S., Miyoshi, N., Oda, M., and Suzuki, Y., Three domains comprised in thermostable molecular weight 54,000 pullulanase of type I from Bacillus flavocaldarius KP1228. Biosci. Biotechnol. Biochem., 63, 1736-1748 (1999).
58. Watanabe, K., Chishiro, K., Kitamura, K., and Suzuki, Y., Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006. J. Biol. Chem., 266, 24287-24294 (1991).
59. Watanabe, K., Kitamura, K., and Suzuki, Y., Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-l,6-glucosidase from Bacillus coagulans ATCC7050 and the evolutionary consideration of proline residues. Appl. Environ. Microbiol., 62, 2066-2073 (1996).
60. Kizaki, H., Hata, Y., Watanabe, K., Katsube, Y., and Suzuki, Y., Polypeptide folding of Bacillus cereus ATCC7064 oligo-l,6-glucosidase revealed by 3.0 A resolution X-ray analysis. J. Biochem., 113, 646-649 (1993).