메뉴 건너뛰기




Volumn 580, Issue 11, 2006, Pages 2707-2711

Structural elements to convert Escherichia coli α-xylosidase (YicI) into α-glucosidase

Author keywords

Glucosidase; Xylosidase; Glycoside hydrolase family 27; Glycoside hydrolase family 31; Site directed mutagenesis; Substrate specificity

Indexed keywords

ALPHA GLUCOSIDASE; ALPHA XYLOSIDASE; AMINO ACID; CYSTEINE; LYSINE; PHENYLALANINE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 33646168883     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.04.025     Document Type: Article
Times cited : (23)

References (17)
  • 1
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280 (1991) 309-316
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 2
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B., and Bairoch A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293 (1993) 781-788
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 3
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat B., and Bairoch A. Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 316 (1996) 695-696
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 4
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies G., and Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 3 (1995) 853-859
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 5
    • 0035006850 scopus 로고    scopus 로고
    • Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α-glucosidase from Schizosaccharomyces pombe
    • Okuyama M., Okuno A., Shimizu N., Mori H., Kimura A., and Chiba S. Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α-glucosidase from Schizosaccharomyces pombe. Eur. J. Biochem. 268 (2001) 2270-2280
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2270-2280
    • Okuyama, M.1    Okuno, A.2    Shimizu, N.3    Mori, H.4    Kimura, A.5    Chiba, S.6
  • 6
    • 0242675935 scopus 로고    scopus 로고
    • Detailed dissection of a new mechanism for glycoside cleavage: α-1,4-glucan lyase
    • Lee S.S., Yu S., and Withers S.G. Detailed dissection of a new mechanism for glycoside cleavage: α-1,4-glucan lyase. Biochemistry 42 (2003) 13081-13090
    • (2003) Biochemistry , vol.42 , pp. 13081-13090
    • Lee, S.S.1    Yu, S.2    Withers, S.G.3
  • 7
    • 0032797473 scopus 로고    scopus 로고
    • α-1,4-Glucan lyases producing 1,5-anhydro-d-fructose from starch and glycogen have sequence similarity to α-glucosidases
    • Yu S., Bojsen K., Svensson B., and Marcussen J. α-1,4-Glucan lyases producing 1,5-anhydro-d-fructose from starch and glycogen have sequence similarity to α-glucosidases. Biochim. Biophys. Acta 1433 (1999) 1-15
    • (1999) Biochim. Biophys. Acta , vol.1433 , pp. 1-15
    • Yu, S.1    Bojsen, K.2    Svensson, B.3    Marcussen, J.4
  • 8
    • 0036562135 scopus 로고    scopus 로고
    • Cloning and sequencing of the genes encoding cyclic tetrasaccharide-synthesizing enzymes from Bacillus globisporus C11
    • Aga H., Maruta K., Yamamoto T., Kubota M., Fukuda S., Kurimoto M., and Tsujisaka Y. Cloning and sequencing of the genes encoding cyclic tetrasaccharide-synthesizing enzymes from Bacillus globisporus C11. Biosci. Biotechnol. Biochem. 66 (2002) 1057-1068
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1057-1068
    • Aga, H.1    Maruta, K.2    Yamamoto, T.3    Kubota, M.4    Fukuda, S.5    Kurimoto, M.6    Tsujisaka, Y.7
  • 10
    • 3543078738 scopus 로고    scopus 로고
    • Overexpression and characterization of two unknown proteins, YicI and YihQ, originated from Escherichia coli
    • Okuyama M., Mori H., Chiba S., and Kimura A. Overexpression and characterization of two unknown proteins, YicI and YihQ, originated from Escherichia coli. Protein Expr. Purif. 37 (2004) 170-179
    • (2004) Protein Expr. Purif. , vol.37 , pp. 170-179
    • Okuyama, M.1    Mori, H.2    Chiba, S.3    Kimura, A.4
  • 11
    • 12544256784 scopus 로고    scopus 로고
    • Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate
    • Lovering A.L., Lee S.S., Kim Y.W., Withers S.G., and Strynadka N.C. Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate. J. Biol. Chem. 280 (2005) 2105-2115
    • (2005) J. Biol. Chem. , vol.280 , pp. 2105-2115
    • Lovering, A.L.1    Lee, S.S.2    Kim, Y.W.3    Withers, S.G.4    Strynadka, N.C.5
  • 12
    • 0037125202 scopus 로고    scopus 로고
    • Iterative database searches demonstrate that glycoside hydrolase families 27, 31, 36 and 66 share a common evolutionary origin with family 13
    • Rigden D.J. Iterative database searches demonstrate that glycoside hydrolase families 27, 31, 36 and 66 share a common evolutionary origin with family 13. FEBS Lett. 523 (2002) 17-22
    • (2002) FEBS Lett. , vol.523 , pp. 17-22
    • Rigden, D.J.1
  • 13
    • 0037827688 scopus 로고    scopus 로고
    • Crystal structure of rice α-galactosidase complexed with d-galactose
    • Fujimoto Z., Kaneko S., Momma M., Kobayashi H., and Mizuno H. Crystal structure of rice α-galactosidase complexed with d-galactose. J. Biol. Chem. 278 (2003) 20313-20318
    • (2003) J. Biol. Chem. , vol.278 , pp. 20313-20318
    • Fujimoto, Z.1    Kaneko, S.2    Momma, M.3    Kobayashi, H.4    Mizuno, H.5
  • 14
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L., and Park J. DaliLite workbench for protein structure comparison. Bioinformatics 16 (2000) 566-567
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 15
    • 0034126439 scopus 로고    scopus 로고
    • Purification, enzymatic characterization, and nucleotide sequence of a high-isoelectric-point α-glucosidase from barley malt
    • Frandsen T.P., Lok F., Mirgorodskaya E., Roepstorff P., and Svensson B. Purification, enzymatic characterization, and nucleotide sequence of a high-isoelectric-point α-glucosidase from barley malt. Plant Physiol. 123 (2000) 275-286
    • (2000) Plant Physiol. , vol.123 , pp. 275-286
    • Frandsen, T.P.1    Lok, F.2    Mirgorodskaya, E.3    Roepstorff, P.4    Svensson, B.5
  • 16
    • 22144485602 scopus 로고    scopus 로고
    • Expanding the range of substrate acceptance of enzymes: combinatorial active-site saturation test
    • Reetz M.T., Bocola M., Carballeira J.D., Zha D., and Vogel A. Expanding the range of substrate acceptance of enzymes: combinatorial active-site saturation test. Angew. Chem., Int. Ed. Engl. 44 (2005) 4192-4196
    • (2005) Angew. Chem., Int. Ed. Engl. , vol.44 , pp. 4192-4196
    • Reetz, M.T.1    Bocola, M.2    Carballeira, J.D.3    Zha, D.4    Vogel, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.