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Volumn 44, Issue , 2016, Pages 51-60

Carbohydrate active enzymes in medicine and biotechnology: The reaction mechanism of retaining glycosyltransferases

Author keywords

Ab initio molecular dynamics; Enzyme catalysis; Glycosyltransferases; Metadynamics; Quantum mechanics molecular mechanics; Retention of configuration.

Indexed keywords

GLYCOSIDE; GLYCOSYLTRANSFERASE;

EID: 84957900542     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20150177     Document Type: Article
Times cited : (48)

References (59)
  • 1
    • 0035937499 scopus 로고    scopus 로고
    • Chemical glycobiology
    • CrossRef PubMed
    • Bertozzi, C.R. and Kiessling, L.L. (2001) Chemical glycobiology. Science 291, 2357-2364 CrossRef PubMed
    • (2001) Science , vol.291 , pp. 2357-2364
    • Bertozzi, C.R.1    Kiessling, L.L.2
  • 2
    • 84867747900 scopus 로고    scopus 로고
    • Recent structures, evolution and mechanisms of glycosyltransferases
    • CrossRef PubMed
    • Breton, C., Fournel-Gigleux, S. and Palcic, M.M. (2012) Recent structures, evolution and mechanisms of glycosyltransferases. Curr. Opin. Struct. Biol. 22, 540-549 CrossRef PubMed
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 540-549
    • Breton, C.1    Fournel-Gigleux, S.2    Palcic, M.M.3
  • 3
    • 27844587415 scopus 로고    scopus 로고
    • Sweetening. Natural products via glycorandomization
    • CrossRef PubMed
    • Griffith, B.R., Langenhan, J.M. and Thorson, J.S. (2005) 'Sweetening' natural products via glycorandomization. Curr. Opin. Biotechnol. 16, 622-630 CrossRef PubMed
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 622-630
    • Griffith, B.R.1    Langenhan, J.M.2    Thorson, J.S.3
  • 4
    • 33748302743 scopus 로고    scopus 로고
    • Exploiting the reversibility of natural product glycosyltransferase-catalyzed reactions
    • CrossRef PubMed
    • Zhang, C., Griffith, B.R., Fu, Q., Albermann, C., Fu, X., Lee, I.K., Li, L. and Thorson, J.S. (2006) Exploiting the reversibility of natural product glycosyltransferase-catalyzed reactions. Science 313, 1291-1294 CrossRef PubMed
    • (2006) Science , vol.313 , pp. 1291-1294
    • Zhang, C.1    Griffith, B.R.2    Fu, Q.3    Albermann, C.4    Fu, X.5    Lee, I.K.6    Li, L.7    Thorson, J.S.8
  • 5
    • 79953328716 scopus 로고    scopus 로고
    • Glycosyltransferases as biocatalysts
    • CrossRef PubMed
    • Palcic, M.M. (2011) Glycosyltransferases as biocatalysts. Curr. Opin. Chem. Biol. 15, 226-233 CrossRef PubMed
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 226-233
    • Palcic, M.M.1
  • 6
    • 84859982558 scopus 로고    scopus 로고
    • A glycosyltransferase inhibitor from a molecular fragment library simultaneously interferes with metal ion and substrate binding
    • CrossRef PubMed
    • Jorgensen, R., Grimm, L.L., Sindhuwinata, N., Peters, T. and Palcic, M.M. (2012) A glycosyltransferase inhibitor from a molecular fragment library simultaneously interferes with metal ion and substrate binding. Angew. Chem. Int. Ed. Engl. 51, 4171-4175 CrossRef PubMed
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 4171-4175
    • Jorgensen, R.1    Grimm, L.L.2    Sindhuwinata, N.3    Peters, T.4    Palcic, M.M.5
  • 7
    • 49449087287 scopus 로고    scopus 로고
    • Glycosyltransferases: Structures, functions, and mechanisms
    • CrossRef PubMed
    • Lairson, L.L., Henrissat, B., Davies, G.J. and Withers, S.G. (2008) Glycosyltransferases: structures, functions, and mechanisms. Annu. Rev. Biochem. 77, 521-555 CrossRef PubMed
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 521-555
    • Lairson, L.L.1    Henrissat, B.2    Davies, G.J.3    Withers, S.G.4
  • 8
    • 53849121583 scopus 로고    scopus 로고
    • Mechanistic insights into glycosidase chemistry
    • CrossRef PubMed
    • Vocadlo, D.J. and Davies, G.J. (2008) Mechanistic insights into glycosidase chemistry. Curr. Opin. Chem. Biol. 12, 539-555 CrossRef PubMed
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 539-555
    • Vocadlo, D.J.1    Davies, G.J.2
  • 10
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • CrossRef PubMed
    • Vocadlo, D.J., Davies, G.J., Laine, R. and Withers, S.G. (2001) Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature 412, 835-838 CrossRef PubMed
    • (2001) Nature , vol.412 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 11
    • 14644390850 scopus 로고    scopus 로고
    • A theoretical DFT investigation of the lysozyme mechanism: Computational evidence for a covalent intermediate pathway
    • CrossRef PubMed
    • Bottoni, A., Miscione, G.P. and De Vivo, M. (2005) A theoretical DFT investigation of the lysozyme mechanism: computational evidence for a covalent intermediate pathway. Proteins 59, 118-130 CrossRef PubMed
    • (2005) Proteins , vol.59 , pp. 118-130
    • Bottoni, A.1    Miscione, G.P.2    De Vivo, M.3
  • 12
    • 52449116184 scopus 로고    scopus 로고
    • QM/MM simulations predict a covalent intermediate in the hen egg white lysozyme reaction with its natural substrate
    • CrossRef
    • Bowman, A.L., Grant, I.M. and Mulholland, A.J. (2008) QM/MM simulations predict a covalent intermediate in the hen egg white lysozyme reaction with its natural substrate. Chem. Commun. 4425-4427 CrossRef
    • (2008) Chem. Commun. , pp. 4425-4427
    • Bowman, A.L.1    Grant, I.M.2    Mulholland, A.J.3
  • 13
    • 83755162490 scopus 로고    scopus 로고
    • Catalytic Itinerary in1,31,4-beta-glucanase unraveled by QM/MM metadynamics. Charge is not yet fully developed at the oxocarbenium ion-like transition state
    • CrossRef PubMed
    • Biarnés, X., Ardèvol, A., Iglesias-Fernández, J., Planas, A. and Rovira, C. (2011) Catalytic itinerary in 1,3-1,4-beta-glucanase unraveled by QM/MM metadynamics. Charge is not yet fully developed at the oxocarbenium ion-like transition state. J. Am. Chem. Soc. 133, 20301-20309 CrossRef PubMed
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 20301-20309
    • Biarnés, X.1    Ardèvol, A.2    Iglesias-Fernández, J.3    Planas, A.4    Rovira, C.5
  • 14
    • 3142615417 scopus 로고    scopus 로고
    • Intermediate trapping on a mutant retaining alpha-galactosyltransferase identifies an unexpected aspartate residue
    • CrossRef PubMed
    • Lairson, L.L., Chiu, C.P., Ly, H.D., He, S., Wakarchuk, W.W., Strynadka, N.C. and Withers, S.G. (2004) Intermediate trapping on a mutant retaining alpha-galactosyltransferase identifies an unexpected aspartate residue. J. Biol. Chem. 279, 28339-28344 CrossRef PubMed
    • (2004) J. Biol. Chem. , vol.279 , pp. 28339-28344
    • Lairson, L.L.1    Chiu, C.P.2    Ly, H.D.3    He, S.4    Wakarchuk, W.W.5    Strynadka, N.C.6    Withers, S.G.7
  • 15
    • 79953884100 scopus 로고    scopus 로고
    • Trapping and characterization of covalent intermediates of mutant retaining glycosyltransferases
    • CrossRef PubMed
    • Soya, N., Fang, Y., Palcic, M.M. and Klassen, J.S. (2011) Trapping and characterization of covalent intermediates of mutant retaining glycosyltransferases. Glycobiology 21, 547-552 CrossRef PubMed
    • (2011) Glycobiology , vol.21 , pp. 547-552
    • Soya, N.1    Fang, Y.2    Palcic, M.M.3    Klassen, J.S.4
  • 16
    • 33845584643 scopus 로고    scopus 로고
    • Chemical rescue of alpha3-galactosyltransferase. Implications in the Mechanism of Retaining Glycosyltransferases
    • CrossRef PubMed
    • Monegal, A. and Planas, A. (2006) Chemical rescue of alpha3-galactosyltransferase. Implications in the mechanism of retaining glycosyltransferases. J. Am. Chem. Soc. 128, 16030-16031 CrossRef PubMed
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 16030-16031
    • Monegal, A.1    Planas, A.2
  • 17
    • 11944256494 scopus 로고
    • Catalytic mechanism of enzymic glycosyl transfer
    • CrossRef
    • Sinnott, M.L. (1990) Catalytic mechanism of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202 CrossRef
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 18
    • 0005589257 scopus 로고
    • The kinetics and stereochemistry of the decomposition of secondary alkyl chlorosulfites
    • CrossRef
    • Lewis, E.S. and Boozer, C.E. (1952) The kinetics and stereochemistry of the decomposition of secondary alkyl chlorosulfites. J. Am. Chem. Soc. 74, 308-311 CrossRef
    • (1952) J. Am. Chem. Soc. , vol.74 , pp. 308-311
    • Lewis, E.S.1    Boozer, C.E.2
  • 19
    • 0001403866 scopus 로고
    • Solvolysis of D-glucopyranosyl Derivatives in Mixtures of Ethanol and 2,2,2-trifluoroethenol
    • CrossRef
    • Sinnott, M.L. and Jencks, W.P. (1980) Solvolysis of D-glucopyranosyl derivatives in mixtures of ethanol and 2,2,2-trifluoroethenol. J. Am. Chem. Soc. 102, 2026-2032 CrossRef
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 2026-2032
    • Sinnott, M.L.1    Jencks, W.P.2
  • 20
    • 84855926382 scopus 로고    scopus 로고
    • A stepwise solvent-promoted SNi reaction of alpha-D-glucopyranosyl fluoride: Mechanistic implications for retaining glycosyltransferases
    • CrossRef PubMed
    • Chan, J., Tang, A. and Bennet, A.J. (2012) A stepwise solvent-promoted SNi reaction of alpha-D-glucopyranosyl fluoride: mechanistic implications for retaining glycosyltransferases. J. Am. Chem. Soc. 134, 1212-1220 CrossRef PubMed
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 1212-1220
    • Chan, J.1    Tang, A.2    Bennet, A.J.3
  • 21
    • 0035151023 scopus 로고    scopus 로고
    • Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs
    • CrossRef PubMed
    • Persson, K., Ly, H.D., Dieckelmann, M., Wakarchuk, W.W., Withers, S.G. and Strynadka, N.C. (2001) Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs. Nat. Struct. Biol. 8, 166-175 CrossRef PubMed
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 166-175
    • Persson, K.1    Ly, H.D.2    Dieckelmann, M.3    Wakarchuk, W.W.4    Withers, S.G.5    Strynadka, N.C.6
  • 22
    • 1542268957 scopus 로고    scopus 로고
    • Molecular modeling insights into the catalytic mechanism of the retaining galactosyltransferase LgtC
    • CrossRef PubMed
    • Tvaroska, I. (2004) Molecular modeling insights into the catalytic mechanism of the retaining galactosyltransferase LgtC. Carbohydr. Res. 339, 1007-1014 CrossRef PubMed
    • (2004) Carbohydr. Res. , vol.339 , pp. 1007-1014
    • Tvaroska, I.1
  • 23
    • 0037461172 scopus 로고    scopus 로고
    • On the reaction pathways and determination of transition-state structures for retaining alpha-galactosyltransferases
    • CrossRef PubMed
    • Andre, I., Tvaroska, I. and Carver, J.P. (2003) On the reaction pathways and determination of transition-state structures for retaining alpha-galactosyltransferases. Carbohydr. Res. 338, 865-877 CrossRef PubMed
    • (2003) Carbohydr. Res. , vol.338 , pp. 865-877
    • Andre, I.1    Tvaroska, I.2    Carver, J.P.3
  • 24
    • 84934312417 scopus 로고    scopus 로고
    • Mixed quantum mechanical/molecular mechanical molecular dynamics simulations of biological systems in ground and electronically excited states
    • Brunk, E. and Rothlisberger, U. (2015) Mixed quantum mechanical/molecular mechanical molecular dynamics simulations of biological systems in ground and electronically excited states. Chem. Rev., doi: 10.1021/cr500628b
    • (2015) Chem. Rev.
    • Brunk, E.1    Rothlisberger, U.2
  • 25
    • 4243943295 scopus 로고    scopus 로고
    • Generalized gradient approximation made simple
    • CrossRef PubMed
    • Perdew, J.P., Burke, K. and Ernzerhof, M. (1996) Generalized gradient approximation made simple. Phys. Rev. Lett. 77, 3865-3868 CrossRef PubMed
    • (1996) Phys. Rev. Lett. , vol.77 , pp. 3865-3868
    • Perdew, J.P.1    Burke, K.2    Ernzerhof, M.3
  • 26
    • 84933073715 scopus 로고    scopus 로고
    • Reaction mechanisms in carbohydrate-active enzymes: Glycoside hydrolases and glycosyltransferases. Insights from Ab Initio Quantum Mechanics/molecular Mechanics Dynamic Simulations
    • CrossRef PubMed
    • Ardevol, A. and Rovira, C. (2015) Reaction mechanisms in carbohydrate-active enzymes: glycoside hydrolases and glycosyltransferases. Insights from ab Initio quantum mechanics/molecular mechanics dynamic simulations. J. Am. Chem. Soc. 137, 7528-7547 CrossRef PubMed
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 7528-7547
    • Ardevol, A.1    Rovira, C.2
  • 27
    • 0036790894 scopus 로고    scopus 로고
    • Escaping free-energy minima
    • CrossRef PubMed
    • Laio, A. and Parrinello, M. (2002) Escaping free-energy minima. Proc. Natl. Acad. Sci. U.S.A. 99, 12562-12566 CrossRef PubMed
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12562-12566
    • Laio, A.1    Parrinello, M.2
  • 28
    • 84923103951 scopus 로고    scopus 로고
    • Perspectives on electrostatics and conformational motions in enzyme catalysis
    • CrossRef PubMed
    • Hanoian, P., Liu, C.T., Hammes-Schiffer, S. and Benkovic, S. (2015) Perspectives on electrostatics and conformational motions in enzyme catalysis. Acc. Chem. Res. 48, 482-489 CrossRef PubMed
    • (2015) Acc. Chem. Res. , vol.48 , pp. 482-489
    • Hanoian, P.1    Liu, C.T.2    Hammes-Schiffer, S.3    Benkovic, S.4
  • 29
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • CrossRef PubMed
    • Henzler-Wildman, K. and Kern, D. (2007) Dynamic personalities of proteins. Nature 450, 964-972 CrossRef PubMed
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 30
    • 36849039429 scopus 로고    scopus 로고
    • A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
    • CrossRef PubMed
    • Henzler-Wildman, K.A., Lei, M., Thai, V., Kerns, S.J., Karplus, M. and Kern, D. (2007) A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 450, 913-916 CrossRef PubMed
    • (2007) Nature , vol.450 , pp. 913-916
    • Henzler-Wildman, K.A.1    Lei, M.2    Thai, V.3    Kerns, S.J.4    Karplus, M.5    Kern, D.6
  • 31
    • 4243606192 scopus 로고
    • Unified approach for molecular dynamics and density-functional theory
    • CrossRef PubMed
    • Car, R. and Parrinello, M. (1985) Unified approach for molecular dynamics and density-functional theory. Phys. Rev. Lett. 55, 2471-2474 CrossRef PubMed
    • (1985) Phys. Rev. Lett. , vol.55 , pp. 2471-2474
    • Car, R.1    Parrinello, M.2
  • 32
    • 84875760613 scopus 로고    scopus 로고
    • Metadynamics. WIres comput
    • CrossRef
    • Barducci, A., Bonomi, M. and Parrinello, M. (2011) Metadynamics. WIREs Comput. Mol. Sci. 1, 826-843 CrossRef
    • (2011) Mol. Sci. , vol.1 , pp. 826-843
    • Barducci, A.1    Bonomi, M.2    Parrinello, M.3
  • 33
    • 33644772083 scopus 로고    scopus 로고
    • Equilibrium free energies from nonequilibrium metadynamics
    • CrossRef PubMed
    • Bussi, G., Laio, A. and Parrinello, M. (2006) Equilibrium free energies from nonequilibrium metadynamics. Phys. Rev. Lett. 96, 090601 CrossRef PubMed
    • (2006) Phys. Rev. Lett. , vol.96 , pp. 090601
    • Bussi, G.1    Laio, A.2    Parrinello, M.3
  • 34
    • 84902817448 scopus 로고    scopus 로고
    • Well-tempered metadynamics converges asymptotically
    • CrossRef PubMed
    • Dama, J.F., Parrinello, M. and Voth, G.A. (2014) Well-tempered metadynamics converges asymptotically. Phys. Rev. Lett. 112, 240602 CrossRef PubMed
    • (2014) Phys. Rev. Lett. , vol.112 , pp. 240602
    • Dama, J.F.1    Parrinello, M.2    Voth, G.A.3
  • 35
    • 70349598928 scopus 로고    scopus 로고
    • Transition path sampling and other advanced simulation techniques for rare events
    • Holm, C. and Kremer, K. Springer, Berlin Heidelberg CrossRef
    • Dellago, C. and Bolhuis, P. (2009) Transition path sampling and other advanced simulation techniques for rare events. In Advanced Computer Simulation Approaches for Soft Matter Sciences III (Holm, C. and Kremer, K., eds), pp. 167-233, Springer, Berlin Heidelberg CrossRef
    • (2009) Advanced Computer Simulation Approaches for Soft Matter Sciences3 , pp. 167-233
    • Dellago, C.1    Bolhuis, P.2
  • 36
    • 80855133537 scopus 로고    scopus 로고
    • The molecular mechanism of enzymatic glycosyl transfer with retention of configuration: Evidence for a short-lived oxocarbenium-like species
    • CrossRef PubMed
    • Ardèvol, A. and Rovira, C. (2011) The molecular mechanism of enzymatic glycosyl transfer with retention of configuration: evidence for a short-lived oxocarbenium-like species. Angew. Chem. Int. Ed. Engl. 50, 10897-10901 CrossRef PubMed
    • (2011) Angew. Chem. Int. Ed. Engl. , vol.50 , pp. 10897-10901
    • Ardèvol, A.1    Rovira, C.2
  • 38
    • 84887175860 scopus 로고    scopus 로고
    • Formation of a covalent glycosyl-enzyme species in a retaining glycosyltransferase
    • CrossRef PubMed
    • Rojas-Cervellera, V., Ardèvol, A., Boero, M., Planas, A. and Rovira, C. (2013) Formation of a covalent glycosyl-enzyme species in a retaining glycosyltransferase. Chemistry 19, 14018-14023 CrossRef PubMed
    • (2013) Chemistry , vol.19 , pp. 14018-14023
    • Rojas-Cervellera, V.1    Ardèvol, A.2    Boero, M.3    Planas, A.4    Rovira, C.5
  • 40
    • 0345826092 scopus 로고    scopus 로고
    • The donor subsite of trehalose-6-phosphate synthase: Binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution
    • CrossRef PubMed
    • Gibson, R.P., Tarling, C.A., Roberts, S., Withers, S.G. and Davies, G.J. (2004) The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution. J. Biol. Chem. 279, 1950-1955 CrossRef PubMed
    • (2004) J. Biol. Chem. , vol.279 , pp. 1950-1955
    • Gibson, R.P.1    Tarling, C.A.2    Roberts, S.3    Withers, S.G.4    Davies, G.J.5
  • 41
    • 84860389788 scopus 로고    scopus 로고
    • Mechanistic evidence for a front-side, SNi-type reaction in a retaining glycosyltransferase
    • CrossRef PubMed
    • Lee, S.S., Hong, S.Y., Errey, J.C., Izumi, A., Davies, G.J. and Davis, B.G. (2011) Mechanistic evidence for a front-side, SNi-type reaction in a retaining glycosyltransferase. Nat. Chem. Biol. 7, 631-638 CrossRef PubMed
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 631-638
    • Lee, S.S.1    Hong, S.Y.2    Errey, J.C.3    Izumi, A.4    Davies, G.J.5    Davis, B.G.6
  • 42
    • 0012023519 scopus 로고    scopus 로고
    • Characterization of a bifunctional enzyme fusion of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase of Escherichia coli
    • CrossRef PubMed
    • Seo, H.S., Koo, Y.J., Lim, J.Y., Song, J.T., Kim, C.H., Kim, J.K., Lee, J.S. and Choi, Y.D. (2000) Characterization of a bifunctional enzyme fusion of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase of Escherichia coli. Appl. Environ. Microbiol. 66, 2484-2490 CrossRef PubMed
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2484-2490
    • Seo, H.S.1    Koo, Y.J.2    Lim, J.Y.3    Song, J.T.4    Kim, C.H.5    Kim, J.K.6    Lee, J.S.7    Choi, Y.D.8
  • 43
    • 84901675902 scopus 로고    scopus 로고
    • A theoretical study on the catalytic mechanism of the retaining alpha-1,2-mannosyltransferase Kre2p/Mnt1p: The impact of different metal ions on catalysis
    • CrossRef PubMed
    • Bobovska, A., Tvaroska, I. and Kona, J. (2014) A theoretical study on the catalytic mechanism of the retaining alpha-1,2-mannosyltransferase Kre2p/Mnt1p: the impact of different metal ions on catalysis. Org. Biomol. Chem. 12, 4201-4210 CrossRef PubMed
    • (2014) Org. Biomol. Chem. , vol.12 , pp. 4201-4210
    • Bobovska, A.1    Tvaroska, I.2    Kona, J.3
  • 45
    • 84858218497 scopus 로고    scopus 로고
    • Retaining glycosyltransferase mechanism studied by QM/MM methods: Lipopolysaccharyl-alpha-1,4-galactosyltransferase C transfers alpha-galactose via an oxocarbenium ion-like transition state
    • CrossRef PubMed
    • Gomez, H., Polyak, I., Thiel, W., Lluch, J.M. and Masgrau, L. (2012) Retaining glycosyltransferase mechanism studied by QM/MM methods: lipopolysaccharyl-alpha-1,4-galactosyltransferase C transfers alpha-galactose via an oxocarbenium ion-like transition state. J. Am. Chem. Soc. 134, 4743-4752 CrossRef PubMed
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 4743-4752
    • Gomez, H.1    Polyak, I.2    Thiel, W.3    Lluch, J.M.4    Masgrau, L.5
  • 46
    • 84881007618 scopus 로고    scopus 로고
    • Geometric attributes of retaining glycosyltransferase enzymes favor an orthogonal mechanism
    • CrossRef PubMed
    • Schuman, B., Evans, S.V. and Fyles, T.M. (2013) Geometric attributes of retaining glycosyltransferase enzymes favor an orthogonal mechanism. PLoS One 8, e71077 CrossRef PubMed
    • (2013) PLoS One , vol.8 , pp. E71077
    • Schuman, B.1    Evans, S.V.2    Fyles, T.M.3
  • 47
    • 0008522066 scopus 로고
    • Reinvestigation of the SNi reaction. The ionization of chlorosulfites
    • CrossRef
    • Schreiner, P.R., Schleyer, P.V.R. and Hill, R.K. (1993) Reinvestigation of the SNi reaction. The ionization of chlorosulfites. J. Org. Chem. 58, 2822-2829 CrossRef
    • (1993) J. Org. Chem. , vol.58 , pp. 2822-2829
    • Schreiner, P.R.1    Schleyer, P.V.R.2    Hill, R.K.3
  • 48
    • 84860365843 scopus 로고    scopus 로고
    • Control of mucin-type O-glycosylation: A classification of the polypeptide GalNAc-transferase gene family
    • CrossRef PubMed
    • Bennett, E.P., Mandel, U., Clausen, H., Gerken, T.A., Fritz, T.A. and Tabak, L.A. (2012) Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family. Glycobiology 22, 736-756 CrossRef PubMed
    • (2012) Glycobiology , vol.22 , pp. 736-756
    • Bennett, E.P.1    Mandel, U.2    Clausen, H.3    Gerken, T.A.4    Fritz, T.A.5    Tabak, L.A.6
  • 50
    • 84898075763 scopus 로고    scopus 로고
    • A computational and experimental study of O-glycosylation. Catalysis by human UDP-GalNAc polypeptide:GalNAc transferase-T2
    • CrossRef PubMed
    • Gomez, H., Rojas, R., Patel, D., Tabak, L.A., Lluch, J.M. and Masgrau, L. (2014) A computational and experimental study of O-glycosylation. Catalysis by human UDP-GalNAc polypeptide:GalNAc transferase-T2. Org. Biomol. Chem. 12, 2645-2655 CrossRef PubMed
    • (2014) Org. Biomol. Chem. , vol.12 , pp. 2645-2655
    • Gomez, H.1    Rojas, R.2    Patel, D.3    Tabak, L.A.4    Lluch, J.M.5    Masgrau, L.6
  • 51
    • 84929493591 scopus 로고    scopus 로고
    • Stepwise catalytic mechanism via short-lived intermediate inferred from combined QM/MM MERP and PES calculations on retaining glycosyltransferase ppGalNAcT2
    • CrossRef PubMed
    • Trnka, T., Kozmon, S., Tvaroska, I. and Koca, J. (2015) Stepwise catalytic mechanism via short-lived intermediate inferred from combined QM/MM MERP and PES calculations on retaining glycosyltransferase ppGalNAcT2. PLoS Comput. Biol. 11, e1004061 CrossRef PubMed
    • (2015) PLoS Comput. Biol. , vol.11 , pp. e1004061
    • Trnka, T.1    Kozmon, S.2    Tvaroska, I.3    Koca, J.4
  • 52
    • 34248657555 scopus 로고    scopus 로고
    • Conformational changes induced by binding UDP-2F-galactose to alpha-1,3 galactosyltransferase- implications for catalysis
    • CrossRef PubMed
    • Jamaluddin, H., Tumbale, P., Withers, S.G., Acharya, K.R. and Brew, K. (2007) Conformational changes induced by binding UDP-2F-galactose to alpha-1,3 galactosyltransferase- implications for catalysis. J. Mol. Biol. 369, 1270-1281 CrossRef PubMed
    • (2007) J. Mol. Biol. , vol.369 , pp. 1270-1281
    • Jamaluddin, H.1    Tumbale, P.2    Withers, S.G.3    Acharya, K.R.4    Brew, K.5
  • 53
    • 0037008717 scopus 로고    scopus 로고
    • Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase, alpha-1,3-galactosyltransferase
    • CrossRef PubMed
    • Boix, E., Zhang, Y., Swaminathan, G.J., Brew, K. and Acharya, K.R. (2002) Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase, alpha-1,3-galactosyltransferase. J. Biol. Chem. 277, 28310-28318 CrossRef PubMed
    • (2002) J. Biol. Chem. , vol.277 , pp. 28310-28318
    • Boix, E.1    Zhang, Y.2    Swaminathan, G.J.3    Brew, K.4    Acharya, K.R.5
  • 55
    • 84860298921 scopus 로고    scopus 로고
    • Conformational analyses of the reaction coordinate of glycosidases
    • CrossRef PubMed
    • Davies, G.J., Planas, A. and Rovira, C. (2012) Conformational analyses of the reaction coordinate of glycosidases. Acc. Chem. Res. 45, 308-316 CrossRef PubMed
    • (2012) Acc. Chem. Res. , vol.45 , pp. 308-316
    • Davies, G.J.1    Planas, A.2    Rovira, C.3
  • 56
    • 84877299428 scopus 로고    scopus 로고
    • Substrate-assisted and nucleophilically assisted catalysis in bovine alpha1,3-galactosyltransferase. Mechanistic Implications for Retaining Glycosyltransferases
    • CrossRef PubMed
    • Gomez, H., Lluch, J.M. and Masgrau, L. (2013) Substrate-assisted and nucleophilically assisted catalysis in bovine alpha1,3-galactosyltransferase. Mechanistic implications for retaining glycosyltransferases. J. Am. Chem. Soc. 135, 7053-7063 CrossRef PubMed
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 7053-7063
    • Gomez, H.1    Lluch, J.M.2    Masgrau, L.3
  • 57
    • 84924942777 scopus 로고    scopus 로고
    • Theoretical study of enzymatic catalysis explains why the trapped covalent intermediate in the E303C mutant of glycosyltransferase GTB was not detected in the wild-type enzyme
    • CrossRef PubMed
    • Bobovska, A., Tvaroska, I. and Kona, J. (2015) Theoretical study of enzymatic catalysis explains why the trapped covalent intermediate in the E303C mutant of glycosyltransferase GTB was not detected in the wild-type enzyme. Glycobiology 25, 3-7 CrossRef PubMed
    • (2015) Glycobiology , vol.25 , pp. 3-7
    • Bobovska, A.1    Tvaroska, I.2    Kona, J.3
  • 58
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • CrossRef PubMed
    • Humphrey, W., Dalke, A. and Schulten, K. (1996) VMD: visual molecular dynamics. J. Mol. Graph. 14, 33-38 CrossRef PubMed
    • (1996) J. Mol. Graph. , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 59
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges. The resp model
    • CrossRef
    • Bayly, C.I., Cieplak, P., Cornell, W.D. and Kollman, P.A. (1993) A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges. The RESP model. J. Phys. Chem. 97, 10269-10280 CrossRef
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4


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