메뉴 건너뛰기




Volumn 451, Issue 4, 2014, Pages 541-547

Introducing transglycosylation activity in Bacillus licheniformis α-amylase by replacement of His235 with Glu

Author keywords

Bacillus licheniformis thermostable; Binding subsite mapping; Site directed mutagenesis; Substrate transglycosylation; Transfer product; amylase

Indexed keywords

AMYLASE; CARBON 14; ENZYME; ENZYME H235E; GLUCOSE; GLUTAMIC ACID; GLYCOSIDE; HISTIDINE; UNCLASSIFIED DRUG; ALPHA AMYLASE, BACILLUS LICHENIFORMIS; ALPHA-AMYLASE, BACILLUS LICHENIFORMIS; MALTOOCTAOSE; OLIGOSACCHARIDE;

EID: 84908365836     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.08.019     Document Type: Article
Times cited : (12)

References (29)
  • 1
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases
    • B. Henrissat, I. Callebaut, S. Fabrega, P. Lehn, J.P. Mornon, and G. Davies Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases Proc. Natl. Acad. Sci. USA 92 1995 7090 7094
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.P.5    Davies, G.6
  • 2
    • 13544272805 scopus 로고    scopus 로고
    • Chemical modification of lysine residues in Bacillus licheniformis α-amylase: Conversion of an endo- to an exo-type enzyme
    • A.E. Habibi, K. Khajeh, and M. Nemat-Gorgani Chemical modification of lysine residues in Bacillus licheniformis α-amylase: conversion of an endo- to an exo-type enzyme J. Biochem. Mol. Biol. 37 2004 642 647
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 642-647
    • Habibi, A.E.1    Khajeh, K.2    Nemat-Gorgani, M.3
  • 3
    • 0041378007 scopus 로고    scopus 로고
    • α-Amylase from Bacillus licheniformis mutants near to the catalytic site: Effects on hydrolytic and transglycosylation activity
    • M.H. Rivera, A. López-Munguía, X. Sobern, and G. Saab-Rincón α-Amylase from Bacillus licheniformis mutants near to the catalytic site: effects on hydrolytic and transglycosylation activity Protein Eng. 16 2003 504 514
    • (2003) Protein Eng. , vol.16 , pp. 504-514
    • Rivera, M.H.1    López-Munguía, A.2    Sobern, X.3    Saab-Rincón, G.4
  • 4
    • 0030986231 scopus 로고    scopus 로고
    • Hyperthermostable mutants of Bacillus licheniformis α-amylase: Thermodynamic studies and structural interpretation
    • N. Declerck, M. Machius, R. Chambert, G. Wiegand, R. Huber, and C. Gaillardin Hyperthermostable mutants of Bacillus licheniformis α-amylase: thermodynamic studies and structural interpretation Protein Eng. 10 1997 541 549
    • (1997) Protein Eng. , vol.10 , pp. 541-549
    • Declerck, N.1    Machius, M.2    Chambert, R.3    Wiegand, G.4    Huber, R.5    Gaillardin, C.6
  • 5
    • 0037900194 scopus 로고    scopus 로고
    • Hyperthermostabilization of Bacillus licheniformis α-amylase and modulation of its stability over a 50 °c temperature range
    • N. Declerk, M. Machius, P. Joyet, G. Wiegand, R. Huber, and C. Gaillardin Hyperthermostabilization of Bacillus licheniformis α-amylase and modulation of its stability over a 50°C temperature range Protein Eng. 16 2003 287 293
    • (2003) Protein Eng. , vol.16 , pp. 287-293
    • Declerk, N.1    Machius, M.2    Joyet, P.3    Wiegand, G.4    Huber, R.5    Gaillardin, C.6
  • 6
    • 0033179308 scopus 로고    scopus 로고
    • Protein engineering of α-amylase for low pH performance
    • A. Shaw, R. Bott, and A.G. Day Protein engineering of α-amylase for low pH performance Curr. Opin. Biotechnol. 10 1999 349 352
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 349-352
    • Shaw, A.1    Bott, R.2    Day, A.G.3
  • 7
    • 84896698596 scopus 로고    scopus 로고
    • Experimental evidence for a 9-binding subsite of Bacillus licheniformis thermostable α-amylase
    • P.L. Tran, J.S. Lee, and K.H. Park Experimental evidence for a 9-binding subsite of Bacillus licheniformis thermostable α-amylase FEBS Lett. 588 2014 620 624
    • (2014) FEBS Lett. , vol.588 , pp. 620-624
    • Tran, P.L.1    Lee, J.S.2    Park, K.H.3
  • 10
    • 0021880257 scopus 로고
    • Complete nucleotide sequence of a thermophilic α-amylase gene: Homology between prokaryotic and eukaryotic α-amylases at the active sites
    • H. Ihara, T. Sasaki, A. Tsuboi, H. Yamagata, N. Tsukagoshi, and S. Udaka Complete nucleotide sequence of a thermophilic α-amylase gene: homology between prokaryotic and eukaryotic α-amylases at the active sites J. Biochem. 98 1985 95 103
    • (1985) J. Biochem. , vol.98 , pp. 95-103
    • Ihara, H.1    Sasaki, T.2    Tsuboi, A.3    Yamagata, H.4    Tsukagoshi, N.5    Udaka, S.6
  • 11
    • 84989131370 scopus 로고
    • The complete amino acid sequence of taka-amylase A
    • H. Toda, K. Kondo, and K. Narita The complete amino acid sequence of taka-amylase A Proc. Jpn. Acad. 58 1982 208 212
    • (1982) Proc. Jpn. Acad. , vol.58 , pp. 208-212
    • Toda, H.1    Kondo, K.2    Narita, K.3
  • 12
    • 0021099734 scopus 로고
    • Isolation and sequence analysis of a barley α-amylase cDNA clone
    • J.C. Rogers, and C. Milliman Isolation and sequence analysis of a barley α-amylase cDNA clone J. Biol. Chem. 258 1983 8169 8174
    • (1983) J. Biol. Chem. , vol.258 , pp. 8169-8174
    • Rogers, J.C.1    Milliman, C.2
  • 13
    • 0032942009 scopus 로고    scopus 로고
    • Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain
    • T.J. Kim, M.J. Kim, B.C. Kim, J.C. Kim, T.K. Cheong, J.W. Kim, and K.H. Park Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain Appl. Environ. Microbiol. 65 1999 1644 1651
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1644-1651
    • Kim, T.J.1    Kim, M.J.2    Kim, B.C.3    Kim, J.C.4    Cheong, T.K.5    Kim, J.W.6    Park, K.H.7
  • 14
    • 0032053544 scopus 로고    scopus 로고
    • Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose
    • H.J. Cha, H.G. Yoon, Y.W. Kim, H.S. Lee, J.W. Kim, K.S. Kweon, B.H. Oh, and K.H. Park Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose Eur. J. Biochem. 253 1998 251 262
    • (1998) Eur. J. Biochem. , vol.253 , pp. 251-262
    • Cha, H.J.1    Yoon, H.G.2    Kim, Y.W.3    Lee, H.S.4    Kim, J.W.5    Kweon, K.S.6    Oh, B.H.7    Park, K.H.8
  • 15
    • 79953191157 scopus 로고    scopus 로고
    • Functional characterization of a special thermophilic multifunctional amylase OPMA-N and its N-terminal domain
    • F. Li, X. Zhu, Y. Li, H. Cao, and Y. Zhang Functional characterization of a special thermophilic multifunctional amylase OPMA-N and its N-terminal domain Acta Biochim. Biophys. Sin. (Shanghai) 43 2011 324 334
    • (2011) Acta Biochim. Biophys. Sin. (Shanghai) , vol.43 , pp. 324-334
    • Li, F.1    Zhu, X.2    Li, Y.3    Cao, H.4    Zhang, Y.5
  • 19
    • 33751005820 scopus 로고    scopus 로고
    • The action mode of Thermusaquaticus YT-1 4-α-glucanotransferase and its chimeric enzymes introduced with starch-binding domain on amylose and amylopectin
    • J.H. Park, H.J. Kim, Y.H. Kim, H. Cha, Y.W. Kim, T.J. Kim, Y.R. Kim, and K.H. Park The action mode of Thermusaquaticus YT-1 4-α-glucanotransferase and its chimeric enzymes introduced with starch-binding domain on amylose and amylopectin Carbohydr. Polym. 67 2007 164 173
    • (2007) Carbohydr. Polym. , vol.67 , pp. 164-173
    • Park, J.H.1    Kim, H.J.2    Kim, Y.H.3    Cha, H.4    Kim, Y.W.5    Kim, T.J.6    Kim, Y.R.7    Park, K.H.8
  • 20
    • 33747333106 scopus 로고
    • Use of dinitrosalycylic acid reagent for determination by reducing sugar
    • G.L. Miller Use of dinitrosalycylic acid reagent for determination by reducing sugar Anal. Chem. 31 1959 426 428
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 21
    • 0014939925 scopus 로고
    • The action pattern of porcine pancreatic α-amylase in relationship to the substrate binding site of the enzyme
    • J.F. Robyt, and D. French The action pattern of porcine pancreatic α-amylase in relationship to the substrate binding site of the enzyme J. Biol. Chem. 245 1970 3917 3927
    • (1970) J. Biol. Chem. , vol.245 , pp. 3917-3927
    • Robyt, J.F.1    French, D.2
  • 24
    • 84902470011 scopus 로고    scopus 로고
    • Structure features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp, ST04
    • K.H. Park, J.H. Jung, S.G. Park, M.E. Lee, J.F. Holden, C.S. Park, and E.J. Woo Structure features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp, ST04 Acta Crystallogr. D70 2014 1659 1668
    • (2014) Acta Crystallogr. , vol.70 D , pp. 1659-1668
    • Park, K.H.1    Jung, J.H.2    Park, S.G.3    Lee, M.E.4    Holden, J.F.5    Park, C.S.6    Woo, E.J.7
  • 25
    • 77957259893 scopus 로고    scopus 로고
    • Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose
    • K. Yamamoto, H. Miyake, M. Kusunoki, and S. Osaki Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose FEBS J. 277 2010 4205 4214
    • (2010) FEBS J. , vol.277 , pp. 4205-4214
    • Yamamoto, K.1    Miyake, H.2    Kusunoki, M.3    Osaki, S.4
  • 26
    • 28244442802 scopus 로고    scopus 로고
    • Complexes of Thermoactinomyces vulgaris R-47 α-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α-(1,6) glycosidic linkages
    • A. Abe, H. Yoshida, T. Tonozuka, Y. Sakano, and S. Kamitori Complexes of Thermoactinomyces vulgaris R-47 α-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α-(1,6) glycosidic linkages FEBS J. 272 2005 6145 6153
    • (2005) FEBS J. , vol.272 , pp. 6145-6153
    • Abe, A.1    Yoshida, H.2    Tonozuka, T.3    Sakano, Y.4    Kamitori, S.5
  • 27
    • 84870887771 scopus 로고    scopus 로고
    • Structure of the α-1,6/α-1,4-specific glucansucrase GTFA from Lactobacillus reuteri 121
    • T. Pijning, A. Vujicic-Zagar, S. Kralj, L. Dijkhuizen, and B.W. Dijkstra Structure of the α-1,6/α-1,4-specific glucansucrase GTFA from Lactobacillus reuteri 121 Acta Crystallogr. F68 2012 1448 1454
    • (2012) Acta Crystallogr. , vol.68 F , pp. 1448-1454
    • Pijning, T.1    Vujicic-Zagar, A.2    Kralj, S.3    Dijkhuizen, L.4    Dijkstra, B.W.5
  • 28
    • 84871714045 scopus 로고
    • A novel domain arrangement in a monomeric cyclodextrin-hydolyzing enzyme from the hyperthermophiles Pyrococcus furiosus
    • J.T. Park, H.N. Song, T.Y. Jung, M.H. Lee, S.G. Park, E.J. Woo, and K.H. Park A novel domain arrangement in a monomeric cyclodextrin-hydolyzing enzyme from the hyperthermophiles Pyrococcus furiosus Biochim. Biophys. Acta 2013 1834 380 386
    • (1834) Biochim. Biophys. Acta , vol.2013 , pp. 380-386
    • Park, J.T.1    Song, H.N.2    Jung, T.Y.3    Lee, M.H.4    Park, S.G.5    Woo, E.J.6    Park, K.H.7
  • 29
    • 84875474745 scopus 로고    scopus 로고
    • Structure of a novel α-amylase AmyB from Thermotoga neapolitana that produces maltose from the nonreducing end of polysaccharides
    • S.Y. Jun, J.S. Kim, K.H. Choi, J. Cha, and N.C. Ha Structure of a novel α-amylase AmyB from Thermotoga neapolitana that produces maltose from the nonreducing end of polysaccharides Acta Crystallogr. D69 2013 442 450
    • (2013) Acta Crystallogr. , vol.69 D , pp. 442-450
    • Jun, S.Y.1    Kim, J.S.2    Choi, K.H.3    Cha, J.4    Ha, N.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.