Analysis of Catalytic Residues of Thermoactinomyces vulgaris R-47 α-Amylase II (TVA II) by Site-directed Mutagenesis

Bioscience, Biotechnology and Biochemistry

Volumn 64, Issue 12, 2000, Pages 2692-2695

  Ichikawa, Kazuhiro ^a   Tonozuka, Takashi ^a   Yokota, Takehiro ^a   Shimura, Yoichiro ^a   Sakano, Yoshiyuki ^a  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

Author keywords

Catalytic residue; Transglycosylation; amylase

Indexed keywords

AMYLASE; GLUCOSE; MALTOHEXAOSE; MALTOSE; OLIGOSACCHARIDE;

ARTICLE; COMPARATIVE STUDY; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; GLYCOSYLATION; HYDROLYSIS; METABOLISM; MICROMONOSPORACEAE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

ALPHA-AMYLASE; CATALYTIC DOMAIN; GLUCOSE; GLYCOSYLATION; HYDROLYSIS; MALTOSE; MICROMONOSPORACEAE; MUTAGENESIS, SITE-DIRECTED; OLIGOSACCHARIDES; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0034567454     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.64.2692     Document Type: Article

References (22)

1. Tonozuka, T., Mogi, S., Shimura, Y., Ibuka, A., Sakai, H., Matsuzawa, H., Sakano, Y., and Ohta, T., Comparison of primary structures and substarte specificities of two pullulan-hydrolyzing a-amylases, TVA I and TVA II, fromThermoactinomyces vulgarisR-47.Biochim. Biophys. Acta,1252,35-42 (1995).
2. 2-o'-isomalt-osylisomaltose usingThermoactinomyces vulgarisR-47 a-amylase II (TYA II).Carbohydr. Res.,261, 157-162 (1994).
3. Matsuura, Y., Kusunoki, M., Harada, W., and Kakudo, M., Structure and possible catalytic residues of Taka-amylase A.J. Biochem.,95,697-702 (1984).
4. Nagashima, T., Tada, S., Kitajima, K., Gomi, K., Kumagai, C., and Toda, H., Site-directed mutagenesis of catalytic active-site residues of Taka-amylase A.Biosci. Biotechnol. Biochem.,56,207-210 (1992).
5. Kuriki, T., Takata, H., Okada, S., and Imanaka, T., Analysis of the active center ofBacillus stearother-mophilusneopullulanase.J. BacterioL,173, 6147-6152 (1991).
6. Podkovyrov, S. M., Burdette, D., and Zeikus, J. G., Analysis of the catalytic center of cyclomaltodex-trinase fromThermoanaerobacter ethanolicus39E.FEBS Lett.,317,259-262 (1993).
7. Matsuura, Y., Kusunoki, M., and Kakudo, M., Structure and catalytic implications of Taka-Amylase A.Denpun kagaku,38, 137-139 (1991).
8. Kuriki, T. and Imanaka, T., The Concept of thea-amylase family: Structural similarity and common catalytic mechanism.J. Biosci. Bioeng.,87,557-565 (1999).
9. Hasegawa, K., Kubota, M., and Matsuura, Y., Role of catalytic residues in a-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase.Protein Eng.,12,819-824 (1999).
10. Kamitori, S., Kondo, S., Okuyama, K., Yokota, T., Shimura, Y., Tonozuka, T., and Sakano, Y., Crystal structure ofThermoactinomyces vulgarisR-47a-amylase II (TVA II) hydrolyzing cyclodextrins and pullulan at 2.6A resolution.J. Mol. Biol.,287,907-921 (1999).
11. Kunkel, T. A., Rapid and efficient site-specific mutagenesis without phenotypic selection.Proc. Natl. Acad. Sci. USA,82,488-492 (1985).
12. Tonozuka, T., Ohtsuka, M., Mogi, S., Sakai, H., Ohta, T., and Sakano, Y., A neopullulanase-type Gf-amylase gene fromThermoactinomyces vulgarisR-47.Biosci. Biotechnol. Biochem.,57,395-401 (1993).
13. Somogyi, M., Notes on sugar determination.J. Biol. Chem.,195,19-23 (1952).
14. Knegtel, R. M. A., Strokopytov, B., Penninga, D., Faber, O. G., Rozeboom, H. J., Kalk, K. H., Dijkhuizen, L., and Dijkstra, B. W., Crystallogra-phic studies of the interaction of cyclodextrin glycosyltransferase fromBacillus circulansstrain 251 with natural substrates and products.J. Biol. Chem.,270,29256-29264 (1995).
15. Chauvaux, S., Beguin, P., and Aubert, J. P., Site-directed mutagenesis of essential carboxylic residues inClostridium thermocellumendoglucanase CelD.J. Biol. Chem.,267,4472-4478 (1992).
16. Brzozowski, A. M. and Davies, G. J., Structure of theAspergillus oryzaea-amylase complexed with the inhibitor acarbose at 2.0 A resolution.Biochemistry,36,10837-10845 (1997).
17. Dauter, Z., Dauter, M., Brzozowski, A. M., Christensen, S., Borchert, T. V., Beier, L., Wilson, K. S., and Davies, G. J., X-ray structure of Novamyl, the five-domain “maltogenic” ce-amylase from Bacillus stearothermophilus:maltose and acarbose complexes at 1.7 Â resolution.Biochemistry,38,8385-8392 (1999).
18. Tsukagoshi, N., Furukawa, M., Nagaba, H., Kirita, N., Tsuboi, A., and Udaka, S., Isolation of a cDNA encodingAspergillus oryzaeTaka-amylase A: evidence for multiple related genes.Gene,84,319-327 (1989).
19. Pasero, L., Mazzei-Pierron, Y., Abadie, B., Chicheportiche, Y., and Marchis-Mouren, G., Complete amino acid sequence and location of the five disulfide bridges in porcine pancreatic a-amylase.Biochim. Biophys. Acta,869,147-157 (1986).
20. Kuriki, T. and Imanaka, T., Nucleotide sequence of the neopullulanase gene fromBacillus stearothermophilus. J. Gen. Microbiol.,135,1521-1528 (1989).
21. Podkovyrov, S. M. and Zeikus, J. G., Structure of the gene encoding cyclomaltodextrinase fromClostridium thermohydrosulfuricum39E and characterization of the enzyme purified fromEscherichia coli. J. BacterioL,174,5400-5405 (1992).
22. Lawson, C. L., van Montfort, R., Strokopytov, B., Rozeboom, H. J., Kalk, K. EL, de Vries, G., Penninga, D., Dijkhuizen, L., and Dijkstra, B. W., Nucleotide sequence and X-ray structure of cyclodextrin glycosyltranferase fromBacillus circulansstrain 251 in a maltose-dependent crystal form.J. Mol. Biol.,236,590-600 (1994).