Structural elements responsible for the glucosidic linkage-selectivity of a glycoside hydrolase family 13 exo-glucosidase

FEBS Letters

Volumn 589, Issue 7, 2015, Pages 865-869

  Saburi, Wataru ^a   Rachi Otsuka, Hiroaki ^a   Hondoh, Hironori ^a,b   Okuyama, Masayuki ^a   Mori, Haruhide ^a   Kimura, Atsuo ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b HIROSHIMA UNIVERSITY   (Japan)

Author keywords

Dextran glucosidase; Glycoside hydrolase family 13; Oligo 1,6 glucosidase; Substrate specificity; Glucosidase

Indexed keywords

ASPARTIC ACID; DEXTRAN GLUCOSIDASE; GLUTAMIC ACID; GLYCOSIDASE; ISOMALTOSE; LYSINE; MALTOSE; OLIGO 1,6 GLUCOSIDASE; PROTEIN VARIANT; UNCLASSIFIED DRUG; VALINE; BACTERIAL PROTEIN;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; GLUCOSIDIC LINKAGE SELECTIVITY; HYDROLYSIS; HYDROPHOBICITY; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS; STREPTOCOCCUS MUTANS; STRUCTURE ANALYSIS; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM;

STREPTOCOCCUS MUTANS;

BACTERIAL PROTEINS; CATALYTIC DOMAIN; GLYCOSIDE HYDROLASES; ISOMALTOSE; KINETICS; MALTOSE; MUTAGENESIS, SITE-DIRECTED; STREPTOCOCCUS MUTANS; SUBSTRATE SPECIFICITY;

EID: 84924362759     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2015.02.023     Document Type: Article

References (14)

1. V. Lombard, H. Golaconda Ramulu, E. Drula, P.M. Coutinho, and B. Henrissat The Carbohydrate-active enzymes database (CAZy) in 2013 Nucleic Acids Res. 42 2014 D490 D495
2. M.R. Stam, E.G. Danchin, C. Rancurel, P.M. Coutinho, and B. Henrisssat Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins Protein Eng. Des. Sel. 19 2006 555 562
3. E.A. MacGregor, Š. Janeček, and B. Svensson Relationship of sequence and structure to specificity in the α-amylase family of enzymes Biochim. Biophys. Acta 1546 2001 1 20
4. K. Yamamoto, A. Nakayama, Y. Yamamoto, and S. Tabata Val216 decides the substrate specificity of α-glucosidase in Saccharomyces cerevisiae Eur. J. Biochem. 271 2004 3414 3420
5. Y. Tsujimoto, H. Tanaka, R. Takemura, T. Yokogawa, A. Shimonaka, H. Matsui, S. Kashiwabara, K. Watanabe, and Y. Suzuki Molecular determinants of substrate recognition in thermostable α-glucosidases belonging to glycoside hydrolase family 13 J. Biochem. 142 2007 87 93
6. W. Saburi, H. Mori, S. Saito, M. Okuyama, and A. Kimura Structural elements in dextran glucosidase responsible for high specificity to long chain substrate Biochim. Biophys. Acta 1764 2006 688 698
7. W. Saburi, M. Kobayashi, H. Mori, M. Okuyama, and A. Kimura Replacement of the catalytic nucleophile aspartyl residue of dextran glucosidase by cysteine sulfinate enhances transglycosylation activity J. Biol. Chem. 288 2013 31670 31677
8. H. Hondoh, W. Saburi, H. Mori, M. Okuyama, T. Nakada, Y. Matsuura, and A. Kimura Substrate recognition mechanism of α-1,6-glucosidic linkage hydrolyzing enzyme, dextran glucosidase from Streptococcus mutans J. Mol. Biol. 378 2008 913 922
9. M. Kobayashi, H. Hondoh, H. Mori, W. Saburi, M. Okuyama, and A. Kimura Calcium ion-dependent increase in thermostability of dextran glucosidase from Streptococcus mutans Biosci. Biotechnol. Biochem. 75 2011 1557 1563
10. G. Sarkar, and S.S. Sommer The "megaprimer" method of site-directed mutagenesis Biotechniques 8 1990 404 407
11. M. Nakao, T. Nakayama, M. Harada, A. Kakudo, H. Ikemoto, S. Kobayashi, and Y. Shibano Purification and characterization of a Bacillus sp. SAM1606 thermostable α-glucosidase with transglucosylation activity Appl. Microbiol. Biotechnol. 41 1994 337 343
12. M. Inohara-Ochiai, T. Nakayama, R. Goto, M. Nakao, T. Ueda, and Y. Shibano Altering substrate specificity of Bacillus sp. SAM1606 α-glucosidase by comparative site-specific mutagenesis J. Biol. Chem. 272 1997 1601 1607
13. A. Noguchi, M. Yano, Y. Ohshima, H. Hemmi, M. Inohara-Ochiai, M. Okada, K.S. Min, T. Nakayama, and T. Nishino Deciphering the molecular basis of the broad substrate specificity of α-glucosidase from Bacillus sp. SAM1606 J. Biochem. 134 2003 543 550
14. K. Yamamoto, H. Miyake, M. Kusunoki, and S. Osaki Steric hindrance by 2 amino acid residues determines the substrate specificity of isomaltase from Saccharomyces cerevisiae J. Biosci. Bioeng. 112 2011 545 550