메뉴 건너뛰기




Volumn 100, Issue 17, 2016, Pages 7529-7539

Glucansucrase Gtf180-ΔN of Lactobacillus reuteri 180: enzyme and reaction engineering for improved glycosylation of non-carbohydrate molecules

Author keywords

Acceptor reaction; Catechol; Enzyme engineering; Glucansucrase; Glycosylation; Lactobacillus reuteri

Indexed keywords

BIOCHEMICAL ENGINEERING; BIOSYNTHESIS; CRYSTAL STRUCTURE; GLYCOSYLATION; MOLECULES; PHENOLS; SUGAR (SUCROSE);

EID: 84962769058     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-016-7476-x     Document Type: Article
Times cited : (22)

References (33)
  • 1
    • 84991876885 scopus 로고    scopus 로고
    • Phenolic compounds with cosmetic and therapeutic applications
    • Auriol D, Nalin R, Robe P, Lefevre F (2012) Phenolic compounds with cosmetic and therapeutic applications. EP2027279.
    • (2012) EP2027279
    • Auriol, D.1    Nalin, R.2    Robe, P.3    Lefevre, F.4
  • 2
    • 33646021626 scopus 로고    scopus 로고
    • Leuconostoc mesenteroides glucansucrase synthesis of flavonoid glucosides by acceptor reactions in aqueous-organic solvents
    • COI: 1:CAS:528:DC%2BD28XjslClsb4%3D
    • Bertrand A, Morel S, Lefoulon F, Rolland Y, Monsan P, Remaud-Simeon M (2006) Leuconostoc mesenteroides glucansucrase synthesis of flavonoid glucosides by acceptor reactions in aqueous-organic solvents. Carb Res 341:855–863
    • (2006) Carb Res , vol.341 , pp. 855-863
    • Bertrand, A.1    Morel, S.2    Lefoulon, F.3    Rolland, Y.4    Monsan, P.5    Remaud-Simeon, M.6
  • 3
  • 4
    • 80052752535 scopus 로고    scopus 로고
    • Operational stability of immobilized sucrose phosphorylase: continuous production of α-glucose-1-phosphate at elevated temperatures
    • De Winter K, Cerdobbel A, Soetaert W, Desmet T (2011) Operational stability of immobilized sucrose phosphorylase: continuous production of α-glucose-1-phosphate at elevated temperatures. Process Biochem 46:2074–2078
    • (2011) Process Biochem , vol.46 , pp. 2074-2078
    • De Winter, K.1    Cerdobbel, A.2    Soetaert, W.3    Desmet, T.4
  • 5
    • 84865272107 scopus 로고    scopus 로고
    • Enzymatic glycosylation of small molecules: Challenging substrates require tailored catalysts
    • COI: 1:CAS:528:DC%2BC38XhtFGhtbzJ, PID: 22887462
    • Desmet T, Soetaert W, Bojarova P, Kren V, Dijkhuizen L, Eastwick-Field V, Schiller A (2012) Enzymatic glycosylation of small molecules: Challenging substrates require tailored catalysts. Chem Eur J 18:10786–10801
    • (2012) Chem Eur J , vol.18 , pp. 10786-10801
    • Desmet, T.1    Soetaert, W.2    Bojarova, P.3    Kren, V.4    Dijkhuizen, L.5    Eastwick-Field, V.6    Schiller, A.7
  • 6
    • 83655201119 scopus 로고    scopus 로고
    • Broadening the synthetic potential of disaccharide phosphorylases through enzyme engineering
    • COI: 1:CAS:528:DC%2BC3MXhs1Cit7zJ
    • Desmet T, Soetaert W (2012) Broadening the synthetic potential of disaccharide phosphorylases through enzyme engineering. Proc Biochem 47:11–17
    • (2012) Proc Biochem , vol.47 , pp. 11-17
    • Desmet, T.1    Soetaert, W.2
  • 7
    • 84938125572 scopus 로고    scopus 로고
    • Creating space for large acceptors: Rational biocatalyst design for resveratrol glycosylation in an aqueous system
    • COI: 1:CAS:528:DC%2BC2MXpvFWgsr8%3D, PID: 26074151
    • Dirks-Hofmeister ME, Verhaeghe T, De Winter K, Desmet T (2015) Creating space for large acceptors: Rational biocatalyst design for resveratrol glycosylation in an aqueous system. Angew Chem Int Ed Engl 54:9289–9292
    • (2015) Angew Chem Int Ed Engl , vol.54 , pp. 9289-9292
    • Dirks-Hofmeister, M.E.1    Verhaeghe, T.2    De Winter, K.3    Desmet, T.4
  • 8
    • 77954674591 scopus 로고    scopus 로고
    • Purification and characterization of a novel glucansucrase from Leuconostoc lactis EG001
    • COI: 1:CAS:528:DC%2BC3cXhtVGksLfF, PID: 19853426
    • Kim YMM, Yeon MJ, Choi NSS, Chang YHH, Jung MY, Song JJ, Kim JS (2010) Purification and characterization of a novel glucansucrase from Leuconostoc lactis EG001. Microbiol Res 165:384–391
    • (2010) Microbiol Res , vol.165 , pp. 384-391
    • Kim, Y.M.M.1    Yeon, M.J.2    Choi, N.S.S.3    Chang, Y.H.H.4    Jung, M.Y.5    Song, J.J.6    Kim, J.S.7
  • 9
    • 4344560401 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of Lactobacillus reuteri 121 reuteransucrase
    • COI: 1:CAS:528:DC%2BD2cXmtFGrtL8%3D
    • Kralj S, van Geel-Schutten GH, van der Maarel MJEC, Dijkhuizen L (2004) Biochemical and molecular characterization of Lactobacillus reuteri 121 reuteransucrase. Microbiology (SGM) 150:2099–2112
    • (2004) Microbiology (SGM) , vol.150 , pp. 2099-2112
    • Kralj, S.1    van Geel-Schutten, G.H.2    van der Maarel, M.J.E.C.3    Dijkhuizen, L.4
  • 10
    • 84953409272 scopus 로고    scopus 로고
    • Redesign of the active site of sucrose phosphorylase through a clash-induced cascade of loop shifts
    • COI: 1:CAS:528:DC%2BC2MXhvFeqsrvJ, PID: 26527586
    • Kraus M, Grimm C, Seibel J (2016) Redesign of the active site of sucrose phosphorylase through a clash-induced cascade of loop shifts. Chembiochem 17:33–36
    • (2016) Chembiochem , vol.17 , pp. 33-36
    • Kraus, M.1    Grimm, C.2    Seibel, J.3
  • 11
    • 49449087287 scopus 로고    scopus 로고
    • Glycosyltransferases: structures, functions, and mechanisms
    • COI: 1:CAS:528:DC%2BD1cXos1ekurY%3D, PID: 18518825
    • Lairson LL, Henrissat B, Davies GJ, Withers SG (2008) Glycosyltransferases: structures, functions, and mechanisms. Annu Rev Biochem 77:521–555
    • (2008) Annu Rev Biochem , vol.77 , pp. 521-555
    • Lairson, L.L.1    Henrissat, B.2    Davies, G.J.3    Withers, S.G.4
  • 12
    • 84861726054 scopus 로고    scopus 로고
    • Glycosidic bond specificity of glucansucrases: on the role of acceptor substrate binding residues
    • COI: 1:CAS:528:DC%2BC38XnslKjurw%3D
    • Leemhuis H, Pijning T, Dobruchowska JM, Dijkstra BW, Dijkhuizen L (2012) Glycosidic bond specificity of glucansucrases: on the role of acceptor substrate binding residues. Biocat Biotrans 30:366–376
    • (2012) Biocat Biotrans , vol.30 , pp. 366-376
    • Leemhuis, H.1    Pijning, T.2    Dobruchowska, J.M.3    Dijkstra, B.W.4    Dijkhuizen, L.5
  • 13
    • 84872202291 scopus 로고    scopus 로고
    • Glucansucrases: three-dimensional structures, reactions, mechanism, α-glucan analysis and their implications in biotechnology and food applications
    • COI: 1:CAS:528:DC%2BC38XhtFGrs73M, PID: 22796091
    • Leemhuis H, Pijning T, Dobruchowska JM, van Leeuwen SS, Kralj S, Dijkstra BW, Dijkhuizen L (2013) Glucansucrases: three-dimensional structures, reactions, mechanism, α-glucan analysis and their implications in biotechnology and food applications. J Biotechnol 163:250–272
    • (2013) J Biotechnol , vol.163 , pp. 250-272
    • Leemhuis, H.1    Pijning, T.2    Dobruchowska, J.M.3    van Leeuwen, S.S.4    Kralj, S.5    Dijkstra, B.W.6    Dijkhuizen, L.7
  • 14
    • 84958213635 scopus 로고    scopus 로고
    • Engineering a carbohydrate-processing transglycosidase into glycosyltransferase for natural product glycodiversification
    • Liang C, Zhang Y, Jia Y, Wang W, Li Y, Lu S, Jin JM, Tang SY (2016) Engineering a carbohydrate-processing transglycosidase into glycosyltransferase for natural product glycodiversification. Sci Rep. doi:10.1038/srep21051
    • (2016) Sci Rep
    • Liang, C.1    Zhang, Y.2    Jia, Y.3    Wang, W.4    Li, Y.5    Lu, S.6    Jin, J.M.7    Tang, S.Y.8
  • 15
  • 17
    • 0023161238 scopus 로고
    • Dextransucrase: a glucosyltransferase from Streptococcus sanguis
    • COI: 1:CAS:528:DyaL2sXlvFeltbY%3D, PID: 3037240
    • Mayer RM (1987) Dextransucrase: a glucosyltransferase from Streptococcus sanguis. Methods Enzymol 138:649–661
    • (1987) Methods Enzymol , vol.138 , pp. 649-661
    • Mayer, R.M.1
  • 18
    • 84911887172 scopus 로고    scopus 로고
    • Residue Leu940 has a crucial role in the linkage and reaction specificity of the glucansucrase GTF180 of the probiotic bacterium Lactobacillus reuteri 180
    • COI: 1:CAS:528:DC%2BC2cXhvFKkt7rO, PID: 25288798
    • Meng X, Dobruchowska JM, Pijning T, Lopez CA, Kamerling JP, Dijkhuizen L (2014) Residue Leu940 has a crucial role in the linkage and reaction specificity of the glucansucrase GTF180 of the probiotic bacterium Lactobacillus reuteri 180. J Biol Chem 289:32773–32782
    • (2014) J Biol Chem , vol.289 , pp. 32773-32782
    • Meng, X.1    Dobruchowska, J.M.2    Pijning, T.3    Lopez, C.A.4    Kamerling, J.P.5    Dijkhuizen, L.6
  • 19
    • 84955589463 scopus 로고    scopus 로고
    • Synthesis of new hyper-branched α-glucans from sucrose by Lactobacillus reuteri 180 glucansucrase mutants
    • COI: 1:CAS:528:DC%2BC2MXitVGitbvE
    • Meng X, Dobruchowska JM, Pijning T, Gerwig GJ, Dijkhuizen L (2016) Synthesis of new hyper-branched α-glucans from sucrose by Lactobacillus reuteri 180 glucansucrase mutants. J Agr Food Chem 64:433–442
    • (2016) J Agr Food Chem , vol.64 , pp. 433-442
    • Meng, X.1    Dobruchowska, J.M.2    Pijning, T.3    Gerwig, G.J.4    Dijkhuizen, L.5
  • 20
    • 84949633712 scopus 로고    scopus 로고
    • Characterization of the functional roles of amino acid residues in acceptor binding subsite +1 in the active site of the glucansucrase GTF180 enzyme of Lactobacillus reuteri 180
    • COI: 1:CAS:528:DC%2BC2MXitVShsr7I, PID: 26507662
    • Meng X, Pijning T, Dobruchowska JM, Gerwig GJ, Dijkhuizen L (2015) Characterization of the functional roles of amino acid residues in acceptor binding subsite +1 in the active site of the glucansucrase GTF180 enzyme of Lactobacillus reuteri 180. J Biol Chem 290:30131–30141
    • (2015) J Biol Chem , vol.290 , pp. 30131-30141
    • Meng, X.1    Pijning, T.2    Dobruchowska, J.M.3    Gerwig, G.J.4    Dijkhuizen, L.5
  • 21
    • 0034694205 scopus 로고    scopus 로고
    • Transglycosylation by Streptococcus mutans GS-5 glucosyltransferase-D: Acceptor specificity and engineering of reaction conditions
    • COI: 1:CAS:528:DC%2BD3cXnsl2mtbo%3D, PID: 11005918
    • Meulenbeld GH, Hartmans S (2000) Transglycosylation by Streptococcus mutans GS-5 glucosyltransferase-D: Acceptor specificity and engineering of reaction conditions. Biotechnol Bioeng 70:363–369
    • (2000) Biotechnol Bioeng , vol.70 , pp. 363-369
    • Meulenbeld, G.H.1    Hartmans, S.2
  • 22
    • 0032896501 scopus 로고    scopus 로고
    • Glucansucrases: mechanism of action and structure-function relationships
    • COI: 1:CAS:528:DyaK1MXivF2ju78%3D, PID: 10234842
    • Monchois V, Willemot RM, Monsan P (1999) Glucansucrases: mechanism of action and structure-function relationships. FEMS Microbiol Rev 23:131–151
    • (1999) FEMS Microbiol Rev , vol.23 , pp. 131-151
    • Monchois, V.1    Willemot, R.M.2    Monsan, P.3
  • 23
    • 77952899716 scopus 로고    scopus 로고
    • Transglucosidases as efficient tools for oligosaccharide and glucoconjugate synthesis
    • COI: 1:CAS:528:DC%2BC3cXntVSlurg%3D, PID: 20362489
    • Monsan P, Remaud-Siméon M, André I (2010) Transglucosidases as efficient tools for oligosaccharide and glucoconjugate synthesis. Curr Opin Microbiol 13:293–300
    • (2010) Curr Opin Microbiol , vol.13 , pp. 293-300
    • Monsan, P.1    Remaud-Siméon, M.2    André, I.3
  • 24
    • 84878731998 scopus 로고    scopus 로고
    • Synthesis of hexyl α-glucoside and α-polyglucosides by a novel Microbacterium isolate
    • COI: 1:CAS:528:DC%2BC3sXosVejur0%3D, PID: 23579729
    • Ojha S, Mishra S, Kapoor S, Chand S (2013) Synthesis of hexyl α-glucoside and α-polyglucosides by a novel Microbacterium isolate. Appl Microbiol Biotechnol 97:5293–5301
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 5293-5301
    • Ojha, S.1    Mishra, S.2    Kapoor, S.3    Chand, S.4
  • 25
    • 45749158699 scopus 로고    scopus 로고
    • Biochemical and crystallographic characterization of a glucansucrase from Lactobacillus reuteri 180
    • COI: 1:CAS:528:DC%2BD1cXisFOmu7g%3D
    • Pijning T, Vujicic-Zagar A, Kralj S, Eeuwema W, Dijkhuizen L, Dijkstra BW (2008) Biochemical and crystallographic characterization of a glucansucrase from Lactobacillus reuteri 180. Biocat Biotrans 26:12–17
    • (2008) Biocat Biotrans , vol.26 , pp. 12-17
    • Pijning, T.1    Vujicic-Zagar, A.2    Kralj, S.3    Eeuwema, W.4    Dijkhuizen, L.5    Dijkstra, B.W.6
  • 26
    • 22144445294 scopus 로고    scopus 로고
    • Enzymatic synthesis and anti-coagulant effect of salicin analogs by using the Leuconostoc mesenteroides glucansucrase acceptor reaction
    • COI: 1:CAS:528:DC%2BD2MXjtFyktrY%3D, PID: 15831245
    • Seo ES, Lee JH, Park JY, Kim D, Han HJ, Robyt JF (2005) Enzymatic synthesis and anti-coagulant effect of salicin analogs by using the Leuconostoc mesenteroides glucansucrase acceptor reaction. J Biotechnol 117:31–38
    • (2005) J Biotechnol , vol.117 , pp. 31-38
    • Seo, E.S.1    Lee, J.H.2    Park, J.Y.3    Kim, D.4    Han, H.J.5    Robyt, J.F.6
  • 27
    • 84965047080 scopus 로고    scopus 로고
    • Glucosylation of catechol with the GTFA glucansucrase enzyme from Lactobacillus reuteri and sucrose as donor substrate
    • te Poele EM, Grijpstra P, Van Leeuwen SS, Dijkhuizen L (2016) Glucosylation of catechol with the GTFA glucansucrase enzyme from Lactobacillus reuteri and sucrose as donor substrate. Bioconjug Chem http://www.ncbi.nlm.nih.gov/pubmed/26898769.
    • (2016) Bioconjug Chem
    • te Poele, E.M.1    Grijpstra, P.2    Van Leeuwen, S.S.3    Dijkhuizen, L.4
  • 29
    • 0033046740 scopus 로고    scopus 로고
    • Biochemical and structural characterization of the glucan and fructan exopolysaccharides synthesized by the Lactobacillus reuteri wild-type strain and by mutant strains
    • PID: 10388696
    • Van Geel-Schutten GH, Faber E, Smit E, Bonting K, Smith M, Ten Brink B, Kamerling J, Vliegenthart J, Dijkhuizen L (1999) Biochemical and structural characterization of the glucan and fructan exopolysaccharides synthesized by the Lactobacillus reuteri wild-type strain and by mutant strains. Appl Environ Microbiol 65:3008–3014
    • (1999) Appl Environ Microbiol , vol.65 , pp. 3008-3014
    • Van Geel-Schutten, G.H.1    Faber, E.2    Smit, E.3    Bonting, K.4    Smith, M.5    Ten Brink, B.6    Kamerling, J.7    Vliegenthart, J.8    Dijkhuizen, L.9
  • 31
    • 78650734599 scopus 로고    scopus 로고
    • Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes
    • COI: 1:CAS:528:DC%2BC3cXhs1WisL%2FF, PID: 21118988
    • Vujicic-Zagar A, Pijning T, Kralj S, Lopez CA, Eeuwema W, Dijkhuizen L, Dijkstra BW (2010) Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes. Proc Natl Acad Sci USA 107:21406–21411
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 21406-21411
    • Vujicic-Zagar, A.1    Pijning, T.2    Kralj, S.3    Lopez, C.A.4    Eeuwema, W.5    Dijkhuizen, L.6    Dijkstra, B.W.7
  • 32
    • 0025349048 scopus 로고
    • Formation of a stable L-ascorbic acid α-glucoside by mammalian α-glucosidase-catalyzed transglucosylation
    • COI: 1:CAS:528:DyaK3cXlvVOjt74%3D, PID: 2200520
    • Yamamoto I, Muto N, Nagata E, Nakamura T, Suzuki Y (1990) Formation of a stable L-ascorbic acid α-glucoside by mammalian α-glucosidase-catalyzed transglucosylation. Biochim Biophys Acta 1035:44–50
    • (1990) Biochim Biophys Acta , vol.1035 , pp. 44-50
    • Yamamoto, I.1    Muto, N.2    Nagata, E.3    Nakamura, T.4    Suzuki, Y.5
  • 33
    • 0037195956 scopus 로고    scopus 로고
    • Synthesis of acarbose analogues by transglycosylation reactions of Leuconostoc mesenteroides B-512FMC and B-742CB dextransucrases
    • COI: 1:CAS:528:DC%2BD38XpsFejsrY%3D
    • Yoon SH, Robyt JF (2002) Synthesis of acarbose analogues by transglycosylation reactions of Leuconostoc mesenteroides B-512FMC and B-742CB dextransucrases. Carb Res 337:2427–2435
    • (2002) Carb Res , vol.337 , pp. 2427-2435
    • Yoon, S.H.1    Robyt, J.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.