메뉴 건너뛰기




Volumn 7, Issue 9, 2011, Pages 631-638

Mechanistic evidence for a front-side, SNi-type reaction in a retaining glycosyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

BRONSTED ACID; GLYCOSYLTRANSFERASE; NUCLEOPHILE; OXOCARBENIUM ION; OXYGEN; TREHALOSE; TREHALOSE 6 PHOSPHATE SYNTHETASE; UNCLASSIFIED DRUG;

EID: 84860389788     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.628     Document Type: Article
Times cited : (136)

References (50)
  • 2
    • 0024165727 scopus 로고
    • Analysis of the galactosyltranferase reaction by positional isotope exchange and secondary deuterium isotope effects
    • DOI 10.1016/0003-9861(88)90007-0
    • Kim, S.C., Singh, A.N. & Raushel, F.M. Analysis of the galactosyltransferase reaction by positional isotope exchange and secondary deuterium isotope efects. Arch. Biochem. Biophys. 267, 54-59 (1988). (Pubitemid 19001011)
    • (1988) Archives of Biochemistry and Biophysics , vol.267 , Issue.1 , pp. 54-59
    • Kim, S.C.1    Singh, A.N.2    Raushel, F.M.3
  • 3
    • 0032488595 scopus 로고    scopus 로고
    • Isotope trapping and kinetic isotope effect studies of rat liver α- (2→6)-sialyltransferase
    • DOI 10.1021/bi971624t
    • Bruner, M. & Horenstein, B.A. Isotope trapping and kinetic isotope efect studies of rat liver α-(2-6)-sialyltransferase. Biochemistry 37, 289-297 (1998). (Pubitemid 28049132)
    • (1998) Biochemistry , vol.37 , Issue.1 , pp. 289-297
    • Bruner, M.1    Horenstein, B.A.2
  • 4
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • DOI 10.1038/35090602
    • Vocadlo, D.J., Davies, G.J., Laine, R. & Withers, S.G. Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature 412, 835-838 (2001). (Pubitemid 32801467)
    • (2001) Nature , vol.412 , Issue.6849 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 6
    • 79953884100 scopus 로고    scopus 로고
    • Trapping and characterization of covalent intermediates of mutant retaining glycosyltransferases
    • Soya, N., Fang, Y., Palcic, M.M. & Klassen, J.S. Trapping and characterization of covalent intermediates of mutant retaining glycosyltransferases. Glycobiology 21, 547-552 (2011).
    • (2011) Glycobiology , vol.21 , pp. 547-552
    • Soya, N.1    Fang, Y.2    Palcic, M.M.3    Klassen, J.S.4
  • 7
    • 33845584643 scopus 로고    scopus 로고
    • Chemical rescue of α3-galactosyltransferase. Implications in the mechanism of retaining glycosyltransferases
    • DOI 10.1021/ja0659931
    • Monegal, A. & Planas, A. Chemical rescue of α3- galactosyltransferase. implications in the mechanism of retaining glycosyltransferase. J. Am. Chem. Soc. 128, 16030-16031 (2006). (Pubitemid 44936584)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.50 , pp. 16030-16031
    • Monegal, A.1    Planas, A.2
  • 8
    • 0037161293 scopus 로고    scopus 로고
    • Mechanistic studies of a retaining α-galactosyltransferase from Neisseria meningitidis
    • DOI 10.1021/bi012031s
    • Ly, H.D., Lougheed, B., Wakarchuk, W.W. & Withers, S.G. Mechanistic studies of a retaining α-galactosyltransferase from Neisseria meningitidis. Biochemistry 41, 5075-5085 (2002). (Pubitemid 34411661)
    • (2002) Biochemistry , vol.41 , Issue.16 , pp. 5075-5085
    • Ly, H.D.1    Lougheed, B.2    Wakarchuk, W.W.3    Withers, S.G.4
  • 9
    • 0036909547 scopus 로고    scopus 로고
    • Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA
    • DOI 10.1016/S1074-5521(02)00292-2, PII S1074552102002922
    • Gibson, R.P., Turkenburg, J.P., Charnock, S.J., Lloyd, R. & Davies, G.J. Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA. Chem. Biol. 9, 1337-1346 (2002). (Pubitemid 36010690)
    • (2002) Chemistry and Biology , vol.9 , Issue.12 , pp. 1337-1346
    • Gibson, R.P.1    Turkenburg, J.P.2    Charnock, S.J.3    Lloyd, R.4    Davies, G.J.5
  • 10
    • 0035151023 scopus 로고    scopus 로고
    • Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs
    • DOI 10.1038/84168
    • Persson, K. et al. Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor analogs. Nat. Struct. Biol. 8, 166-175 (2001). (Pubitemid 32116071)
    • (2001) Nature Structural Biology , vol.8 , Issue.2 , pp. 166-175
    • Persson, K.1    Ly, H.D.2    Dieckelmann, M.3    Wakarchuk, W.W.4    Withers, S.G.5    Strynadka, N.C.J.6
  • 11
    • 0035865381 scopus 로고    scopus 로고
    • Bovine α1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases
    • DOI 10.1093/emboj/20.4.638
    • Gastinel, L.N. et al. Bovine α-1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferase. EMBO J. 20, 638-649 (2001). (Pubitemid 32167629)
    • (2001) EMBO Journal , vol.20 , Issue.4 , pp. 638-649
    • Gastinel, L.N.1    Bignon, C.2    Misra, A.K.3    Hindsgaul, O.4    Shaper, J.H.5    Joziasse, D.H.6
  • 13
    • 33750974777 scopus 로고    scopus 로고
    • Insights into the Synthesis of Lipopolysaccharide and Antibiotics through the Structures of Two Retaining Glycosyltransferases from Family GT4
    • DOI 10.1016/j.chembiol.2006.09.005, PII S1074552106003371
    • Martinez-Fleites, C. et al. Insights into the synthesis of lipopolysaccharide and antibiotics through the structures of two retaining glycosyltransferases from family GT4. Chem. Biol. 13, 1143-1152 (2006). (Pubitemid 44750727)
    • (2006) Chemistry and Biology , vol.13 , Issue.11 , pp. 1143-1152
    • Martinez-Fleites, C.1    Proctor, M.2    Roberts, S.3    Bolam, D.N.4    Gilbert, H.J.5    Davies, G.J.6
  • 14
    • 34248657555 scopus 로고    scopus 로고
    • Conformational Changes Induced by Binding UDP-2F-galactose to α-1,3 Galactosyltransferase- Implications for Catalysis
    • DOI 10.1016/j.jmb.2007.04.012, PII S0022283607004780
    • Jamaluddin, H., Tumbale, P., Withers, S.G., Acharya, K.R. & Brew, K. Conformational changes induced by binding UDP-2F-galactose to alpha-1,3-galactosyltransferase-implications for catalysis. J. Mol. Biol. 369, 1270-1281 (2007). (Pubitemid 46770770)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.5 , pp. 1270-1281
    • Jamaluddin, H.1    Tumbale, P.2    Withers, S.G.3    Acharya, K.R.4    Brew, K.5
  • 15
    • 47049105152 scopus 로고    scopus 로고
    • Structural and enzymatic analysis of MshA from Corynebacterium glutamicum
    • Vetting, M.W., Frantom, P.A. & Blanchard, J.S. Structural and enzymatic analysis of MshA from Corynebacterium glutamicum. J. Biol. Chem. 283, 15834-15844 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 15834-15844
    • Vetting, M.W.1    Frantom, P.A.2    Blanchard, J.S.3
  • 16
    • 37049151007 scopus 로고
    • 257. Reaction kinetics and the Walden inversion. Part VI. Relation of steric orientation to mechanism in substitutions involving halogen atoms and simple or substituted hydroxyl groups
    • Cowdrey, W.A., Hughes, E.D., Ingold, C.K., Masterman, S. & Scott, A.D. 257. Reaction kinetics and the Walden inversion. Part VI. Relation of steric orientation to mechanism in substitutions involving halogen atoms and simple or substituted hydroxyl groups. J. Chem. Soc. 1252-1271 (1937).
    • (1937) J. Chem. Soc. , pp. 1252-1271
    • Cowdrey, W.A.1    Hughes, E.D.2    Ingold, C.K.3    Masterman, S.4    Scott, A.D.5
  • 17
    • 0001403866 scopus 로고
    • Solvolysis of D-glucopyranosyl derivatives in mixtures of ethanol and 2, 2,2-trifuoroethanol
    • Sinnott, M.L. & Jencks, W. P. Solvolysis of D-glucopyranosyl derivatives in mixtures of ethanol and 2,2,2-trifuoroethanol. J. Am. Chem. Soc. 102, 2026-2032 (1980).
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 2026-2032
    • Sinnott, M.L.1    Jencks, W.P.2
  • 19
    • 0035893762 scopus 로고    scopus 로고
    • α-retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: Mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors
    • DOI 10.1042/0264-6021:3600727
    • Nidetzky, B. & Eis, C. α-Retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors. Biochem. J. 360, 727-736 (2001). (Pubitemid 34020280)
    • (2001) Biochemical Journal , vol.360 , Issue.3 , pp. 727-736
    • Nidetzky, B.1    Els, C.2
  • 20
    • 33746882419 scopus 로고    scopus 로고
    • Structure-function relationships for Schizophyllum commune trehalose phosphorylase and their implications for the catalytic mechanism of family GT-4 glycosyltransferases
    • DOI 10.1042/BJ20060029
    • Goedl, C., Griessler, R., Schwarz, A. & Nidetzky, B. Structure-function relationships for Schizophyllum commune trehalose phosphorylase and their implications for the catalytic mechanism of family GT-4 glycosyltransferase. Biochem. J. 397, 491-500 (2006). (Pubitemid 44187507)
    • (2006) Biochemical Journal , vol.397 , Issue.3 , pp. 491-500
    • Goedl, C.1    Griessler, R.2    Schwarz, A.3    Nidetzky, B.4
  • 21
    • 70350538953 scopus 로고    scopus 로고
    • Sucrose phosphorylase harboring a redesigned, glycosyltransferase-like active site exhibits retaining glucosyl transfer in the absence of a covalent intermediate
    • Goedl, C. & Nidetzky, B. Sucrose phosphorylase harboring a redesigned, glycosyltransferase-like active site exhibits retaining glucosyl transfer in the absence of a covalent intermediate. ChemBioChem 10, 2333-2337 (2009).
    • (2009) ChemBioChem , vol.10 , pp. 2333-2337
    • Goedl, C.1    Nidetzky, B.2
  • 22
    • 76349106696 scopus 로고    scopus 로고
    • Mechanistic insight into enzymatic glycosyl transfer with retention of confguration through analysis of glycomimetic inhibitors
    • Errey, J.C. et al. Mechanistic insight into enzymatic glycosyl transfer with retention of confguration through analysis of glycomimetic inhibitors. Angew. Chem. Int. Ed. Engl. 49, 1234-1237 (2010).
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 1234-1237
    • Errey, J.C.1
  • 23
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • DOI 10.1016/S0022-2836(03)00307-3
    • Coutinho, P.M., Deleury, E., Davies, G.J. & Henrissat, B. An evolving hierarchical family classifcation for glycosyltransferases. J. Mol. Biol. 328, 307-317 (2003). (Pubitemid 36407576)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.2 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 24
    • 84961977626 scopus 로고    scopus 로고
    • Te analysis of enzymic free energy relationships using kinetic and computational models
    • Greig, I.R. Te analysis of enzymic free energy relationships using kinetic and computational models. Chem. Soc. Rev. 39, 2272-2301 (2010).
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 2272-2301
    • Greig, I.R.1
  • 25
    • 0000468730 scopus 로고    scopus 로고
    • Binding energy and catalysis: The implications for transition-state analogs and catalytic antibodies
    • Mader, M.M. & Bartlett, P.A. Binding energy and catalysis: the implications for transition-state analogs and catalytic antibodies. Chem. Rev. 97, 1281-1302 (1997).
    • (1997) Chem. Rev. , vol.97 , pp. 1281-1302
    • Mader, M.M.1    Bartlett, P.A.2
  • 28
    • 33644635257 scopus 로고    scopus 로고
    • Toward a detailed understanding of base excision repair enzymes: Transition state and mechanistic analyses of N-glycoside hydrolysis and N-glycosyl transfer
    • Berti, P.J. & McCann, J.A.B. Toward a detailed understanding of base excision repair enzymes: transition state and mechanistic analyses of N-glycoside hydrolysis and N-glycosyl transfer. Chem. Rev. 106, 506-555 (2006).
    • (2006) Chem. Rev. , vol.106 , pp. 506-555
    • Berti, P.J.1    McCann, J.A.B.2
  • 29
    • 0019874674 scopus 로고
    • Minimal kinetic mechanism and general equation for deuterium isotope efects on enzymic reactions: Uncertaintly in detecting a rate-limiting step
    • Northrop, D.B. Minimal kinetic mechanism and general equation for deuterium isotope efects on enzymic reactions: uncertaintly in detecting a rate-limiting step. Biochemistry 20, 4056-4061 (1981).
    • (1981) Biochemistry , vol.20 , pp. 4056-4061
    • Northrop, D.B.1
  • 30
    • 0034700259 scopus 로고    scopus 로고
    • Kinetic isotope efects studies of the reaction catalyzed by uracil DNA glycosylase: Evidence for an oxocarbenium ion-uracil anion intermediate
    • Werner, R.M. & Stivers, J.T. Kinetic isotope efects studies of the reaction catalyzed by uracil DNA glycosylase: evidence for an oxocarbenium ion-uracil anion intermediate. Biochemistry 39, 14054-14064 (2000).
    • (2000) Biochemistry , vol.39 , pp. 14054-14064
    • Werner, R.M.1    Stivers, J.T.2
  • 31
    • 39749128713 scopus 로고    scopus 로고
    • Transition state structure of E. coli tRNA-specific adenosine deaminase
    • DOI 10.1021/ja078008x
    • Luo, M. & Schramm, V.L. Transition state structure of E. coli tRNA-specifc adenosine deaminase. J. Am. Chem. Soc. 130, 2649-2655 (2008). (Pubitemid 351304780)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.8 , pp. 2649-2655
    • Luo, M.1    Schramm, V.L.2
  • 32
    • 9744244276 scopus 로고    scopus 로고
    • The use of isotope effects to determine enzyme mechanisms
    • DOI 10.1016/j.abb.2004.08.027, PII S0003986104004965
    • Cleland, W. W. Te use of isotope efects to determine enzyme mechanisms. Arch. Biochem. Biophys. 433, 2-12 (2005). (Pubitemid 39586578)
    • (2005) Archives of Biochemistry and Biophysics , vol.433 , Issue.1 , pp. 2-12
    • Cleland, W.W.1
  • 33
    • 1642302768 scopus 로고    scopus 로고
    • 13C Kinetic Isotope Effects Measured at Natural Abundance by NMR Spectroscopy
    • DOI 10.1021/ja0394028
    • 13C kinetic isotope efects measured at natural abundance by NMR spectroscopy. J. Am. Chem. Soc. 126, 3769-3776 (2004). (Pubitemid 38391870)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.12 , pp. 3769-3776
    • Lee, J.K.1    Bain, A.D.2    Berti, P.J.3
  • 34
    • 0001562923 scopus 로고    scopus 로고
    • Transition state looseness and α-secondary kinetic isotope effects
    • DOI 10.1021/ja962733i, PII S0002786396027333
    • Glad, S.S. & Jensen, F. Transition state looseness and α-secondary kinetic isotope efects. J. Am. Chem. Soc. 119, 227-232 (1997). (Pubitemid 27064504)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.1 , pp. 227-232
    • Glad, S.S.1    Jensen, F.2
  • 35
    • 0001433447 scopus 로고
    • Hyperconjugation and the angular dependence of β-deuterium isotope efects
    • Sunko, D.E., Szele, I. & Hehre, W.J. Hyperconjugation and the angular dependence of β-deuterium isotope efects. J. Am. Chem. Soc. 99, 5000-5005 (1977).
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 5000-5005
    • Sunko, D.E.1    Szele, I.2    Hehre, W.J.3
  • 36
    • 33845185675 scopus 로고
    • IUPAC recommendations for the representation of reaction mechanisms
    • Guthrie, R.D. & Jencks, W.P. IUPAC recommendations for the representation of reaction mechanisms. Acc. Chem. Res. 22, 343-349 (1989).
    • (1989) Acc. Chem. Res. , vol.22 , pp. 343-349
    • Guthrie, R.D.1    Jencks, W.P.2
  • 37
    • 0030722604 scopus 로고    scopus 로고
    • Glucosidase-catalyzed hydrolysis of α-D-glucopyranosyl pyridinium salts: Kinetic evidence for nucleophilic involvement at the glucosidation transition state
    • DOI 10.1021/ja963733l
    • Huang, X., Tanaka, K.S.E. & Bennet, A.J. Glucosidase-catalyzed hydrolysis of α-D-glucopyranosyl pyridinium salts: kinetic evidence for nucleophilic involvement at the glucosidation transition state. J. Am. Chem. Soc. 119, 11147-11154 (1997). (Pubitemid 27520932)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.46 , pp. 11147-11154
    • Huang, X.1    Tanaka, K.S.E.2    Bennet, A.J.3
  • 38
    • 77952543565 scopus 로고    scopus 로고
    • A direct NMR method for the measurement of competitive kinetic isotope efects
    • Chan, J., Lewis, A.R., Gilbert, M., Karwaski, M.-F. & Bennet, A.J. A direct NMR method for the measurement of competitive kinetic isotope efects. Nat. Chem. Biol. 6, 405-407 (2010).
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 405-407
    • Chan, J.1    Lewis, A.R.2    Gilbert, M.3    Karwaski, M.-F.4    Bennet, A.J.5
  • 39
    • 0019889069 scopus 로고
    • Oxygen-18 leaving group kinetic isotope efects on the hydrolysis of nitrophenyl glycosides. 2. Lysozyme and beta-glucosidase: Acid and alkaline hydrolysis
    • Rosenberg, S. & Kirsch, J.F. Oxygen-18 leaving group kinetic isotope efects on the hydrolysis of nitrophenyl glycosides. 2. Lysozyme and beta-glucosidase: acid and alkaline hydrolysis. Biochemistry 20, 3196-3204 (1981).
    • (1981) Biochemistry , vol.20 , pp. 3196-3204
    • Rosenberg, S.1    Kirsch, J.F.2
  • 40
    • 0001358095 scopus 로고
    • Complete kinetic isotope efect description of transition states for acid-catalyzed hydrolyses of methyl alpha-and beta-glucopyranosides
    • Bennet, A.J. & Sinnott, M.L. Complete kinetic isotope efect description of transition states for acid-catalyzed hydrolyses of methyl alpha-and beta-glucopyranosides. J. Am. Chem. Soc. 108, 7287-7294 (1986).
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 7287-7294
    • Bennet, A.J.1    Sinnott, M.L.2
  • 41
    • 0035823824 scopus 로고    scopus 로고
    • A kinetic isotope effect study on the hydrolysis reactions of methyl xylopyranosides and methyl 5-thioxylopyranosides: Oxygen versus sulfur stabilization of carbenium ions
    • DOI 10.1021/ja011232g
    • Indurugalla, D. & Bennet, A.J. A kinetic isotope efect study on the hydrolysis reactions of methyl xylopyranosides and methyl 5-thioxylopyranosides: oxygen versus sulfur stabilization of carbeniumions. J. Am. Chem. Soc. 123, 10889-10898 (2001). (Pubitemid 33042001)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.44 , pp. 10889-10898
    • Indurugalla, D.1    Bennet, A.J.2
  • 43
    • 0000957274 scopus 로고    scopus 로고
    • Synthetic utility of yeast hexokinase. Substrate specifcity, cofactor regeneration, and product isolation
    • Chenault, H.K., Mandes, R.F. & Hornberger, K.R. Synthetic utility of yeast hexokinase. Substrate specifcity, cofactor regeneration, and product isolation. J. Org. Chem. 62, 331-336 (1997). (Pubitemid 127494197)
    • (1997) Journal of Organic Chemistry , vol.62 , Issue.2 , pp. 331-336
    • Chenault, K.1    Mandes, R.F.2    Hornberger, K.R.3
  • 46
    • 72949107086 scopus 로고    scopus 로고
    • Glycosidase inhibition: Assessing mimicry of the transition state
    • Gloster, T.M. & Davies, G.J. Glycosidase inhibition: assessing mimicry of the transition state. Org. Biomol. Chem. 8, 305-320 (2010).
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 305-320
    • Gloster, T.M.1    Davies, G.J.2
  • 47
    • 11944256494 scopus 로고
    • Catalytic mechanism of enzymic glycosyl transfer
    • Sinnott, M.L. Catalytic mechanism of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202 (1990).
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 49
    • 0019289005 scopus 로고
    • Purification, properties, kinetics, and mechanism of β-N- acetylglucosamidase from Aspergillus niger
    • Jones, C.S. & Kosman, D.J. Purifcation, properties, kinetics, and mechanism of β-N-acetylglucosaminidase from Aspergillus niger. J. Biol. Chem. 255, 11861-11869 (1980). (Pubitemid 11132202)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.24 , pp. 11861-11869
    • Jones, C.S.1    Kosman, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.