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Volumn 277, Issue 9, 2010, Pages 2171-2179

Highly site-selective stability increases by glycosylation of dihydrofolate reductase

Author keywords

Enzyme; Glycosylation; Kinetics; Mutagenesis; Stability

Indexed keywords

CYSTEINE; DIHYDROFOLATE REDUCTASE; GLUCOSE; IODOACETAMIDE; LACTOSE; MALTOTRIOSE; N ACETYLGLUCOSAMINE; SUGAR;

EID: 77951209387     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07634.x     Document Type: Article
Times cited : (12)

References (51)
  • 1
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: Toward understanding the function of sugars
    • Dwek RA (1996) Glycobiology: toward understanding the function of sugars. Chem Rev 96, 683 720.
    • (1996) Chem Rev , vol.96 , pp. 683-720
    • Dwek, R.A.1
  • 3
    • 0036462604 scopus 로고    scopus 로고
    • Synthesis of glycoproteins
    • Davis BG (2002) Synthesis of glycoproteins. Chem Rev 102, 579 601.
    • (2002) Chem Rev , vol.102 , pp. 579-601
    • Davis, B.G.1
  • 4
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro RG (2002) Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 12, 43R 56R.
    • (2002) Glycobiology , vol.12
    • Spiro, R.G.1
  • 5
    • 70349113034 scopus 로고    scopus 로고
    • Determination of glycosylation sites and site-specific heterogeneity in glycoproteins
    • An HJ, Froehlich JW Lebrilla CB (2009) Determination of glycosylation sites and site-specific heterogeneity in glycoproteins. Curr Opin Chem Biol 13, 421 426.
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 421-426
    • An, H.J.1    Froehlich, J.W.2    Lebrilla, C.B.3
  • 7
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki A (1993) Biological roles of oligosaccharides - all of the theories are correct. Glycobiology 3, 97 130. (Pubitemid 23132602)
    • (1993) Glycobiology , vol.3 , Issue.2 , pp. 97-130
    • Varki, A.1
  • 9
    • 0030065240 scopus 로고    scopus 로고
    • Stabilization of proteins by glycosylation examined by NMR analysis of a fucosylated proteinase inhibitor
    • DOI 10.1038/nsb0196-45
    • Mer G, Hietter H Lefevre JF (1996) Stabilization of proteins by glycosylation examined by NMR analysis of a fucosylated proteinase inhibitor. Nat Struct Biol 3, 45 53. (Pubitemid 26023910)
    • (1996) Nature Structural Biology , vol.3 , Issue.1 , pp. 45-53
    • Mer, G.1    Hietter, H.2    Lefevre, J.-F.3
  • 10
    • 0031025267 scopus 로고    scopus 로고
    • Effects of protein glycosylation on catalysis: Changes in hydrogen tunneling and enthalpy of activation in the glucose oxidase reaction
    • DOI 10.1021/bi962492r
    • Kohen A, Jonsson T Klinman JP (1997) Effects of protein glycosylation on catalysis: changes in hydrogen tunneling and enthalpy of activation in the glucose oxidase reaction. Biochemistry 36, 2603 2611. (Pubitemid 27106654)
    • (1997) Biochemistry , vol.36 , Issue.9 , pp. 2603-2611
    • Kohen, A.1    Jonsson, T.2    Klinman, J.P.3
  • 11
    • 0042266719 scopus 로고    scopus 로고
    • A genetic approach to mammalian glycan function
    • Lowe JB Marth JD (2003) A genetic approach to mammalian glycan function. Annu Rev Biochem 72, 643 691.
    • (2003) Annu Rev Biochem , vol.72 , pp. 643-691
    • Lowe, J.B.1    Marth, J.D.2
  • 12
    • 33750468309 scopus 로고    scopus 로고
    • Protein glycosylation, conserved from yeast to man: A model organism helps elucidate congenital human diseases
    • DOI 10.1002/anie.200601645
    • Lehle L, Strahl S Tanner W (2006) Protein glycosylation, conserved from yeast to man: a model organism helps elucidate congenital human diseases. Angew Chem Int Ed 45, 6802 6818. (Pubitemid 44654465)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.41 , pp. 6802-6818
    • Lehle, L.1    Strahl, S.2    Tanner, W.3
  • 13
    • 35248882544 scopus 로고    scopus 로고
    • Modulation of protein biophysical properties by chemical glycosylation: Biochemical insights and biomedical implications
    • DOI 10.1007/s00018-007-6551-y
    • Sola RJ, Rodriguez-Martinez JA Griebenow K (2007) Modulation of protein biophysical properties by chemical glycosylation: biochemical insights and biomedical implications. Cell Mol Life Sci 64, 2133 2152. (Pubitemid 350092414)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.16 , pp. 2133-2152
    • Sola, R.J.1    Rodriguez-Martinez, J.A.2    Griebenow, K.3
  • 14
    • 23644442411 scopus 로고    scopus 로고
    • Increased thermal stability of site-selectively glycosylated dihydrofolate reductase
    • Swanwick RS, Daines AM, Tey LH, Flitsch SL Allemann RK (2005) Increased thermal stability of site-selectively glycosylated dihydrofolate reductase. ChemBioChem 6, 1338 1340.
    • (2005) ChemBioChem , vol.6 , pp. 1338-1340
    • Swanwick, R.S.1    Daines, A.M.2    Tey, L.H.3    Flitsch, S.L.4    Allemann, R.K.5
  • 15
    • 0030665701 scopus 로고    scopus 로고
    • Effect of chemical glycosylation of Rnase A on the protein stability and surface histidines accessibility in immobilized metal ion affinity electrophoresis (IMAGE) system
    • Baek WO Vijayalakshmi MA (1997) Effect of chemical glycosylation of Rnase A on the protein stability and surface histidines accessibility in immobilized metal ion affinity electrophoresis (IMAGE) system. Biochim Biophys Acta 1336, 394 402.
    • (1997) Biochim Biophys Acta , vol.1336 , pp. 394-402
    • Baek, W.O.1    Vijayalakshmi, M.A.2
  • 16
    • 0034769575 scopus 로고    scopus 로고
    • Stability enhancement of Escherichia coli penicillin G acylase by glycosylation with yeast mannan
    • DOI 10.1042/BA20010037
    • Masarova J, Mislovicova D, Gemeiner P Michalkova E (2001) Stability enhancement of Escherichia coli penicillin G acylase by glycosylation with yeast mannan. Biotechnol Appl Biochem 34, 127 133. (Pubitemid 32977944)
    • (2001) Biotechnology and Applied Biochemistry , vol.34 , Issue.2 , pp. 127-133
    • Masarova, J.1    Mislovicova, D.2    Gemeiner, P.3    Michalkova, E.4
  • 17
    • 1542615145 scopus 로고    scopus 로고
    • Glycoforms of β-Lactoglobulin with Improved Thermostability and Preserved Structural Packing
    • DOI 10.1002/bit.20030
    • Broersen K, Voragen AGJ, Hamer RJ de Jongh HHJ (2004) Glycoforms of beta-lactoglobulin with improved thermostability and preserved structural packing. Biotechnol Bioeng 86, 78 87. (Pubitemid 38339394)
    • (2004) Biotechnology and Bioengineering , vol.86 , Issue.1 , pp. 78-87
    • Broersen, K.1    Voragen, A.G.J.2    Hamer, R.J.3    De Jongh, H.H.J.4
  • 18
    • 0029904281 scopus 로고    scopus 로고
    • Influence of the carbohydrate moiety on the stability of glycoproteins
    • DOI 10.1021/bi9517704
    • Wang CQ, Eufemi M, Turano C Giartosio A (1996) Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry 35, 7299 7307. (Pubitemid 26189798)
    • (1996) Biochemistry , vol.35 , Issue.23 , pp. 7299-7307
    • Wang, C.1    Eufemi, M.2    Turano, C.3    Giartosio, A.4
  • 20
    • 0031008063 scopus 로고    scopus 로고
    • Effect of glycosylation on the stability of alpha(1)-antitrypsin toward urea denaturation and thermal deactivation
    • Kwon KS Yu MH (1997) Effect of glycosylation on the stability of alpha(1)-antitrypsin toward urea denaturation and thermal deactivation. Biochim Biophys Acta 1335, 265 272.
    • (1997) Biochim Biophys Acta , vol.1335 , pp. 265-272
    • Kwon, K.S.1    Yu, M.H.2
  • 21
    • 0031013887 scopus 로고    scopus 로고
    • Mechanism of the stabilization of ribonuclease A by sorbitol: Preferential hydration is greater for the denatured than for the native protein
    • Xie GF Timasheff SN (1997) Mechanism of the stabilization of ribonuclease A by sorbitol: preferential hydration is greater for the denatured than for the native protein. Protein Sci 6, 211 221.
    • (1997) Protein Sci , vol.6 , pp. 211-221
    • Xie, G.F.1    Timasheff, S.N.2
  • 22
    • 0030973690 scopus 로고    scopus 로고
    • The thermodynamic mechanism of protein stabilization by trehalose
    • Xie GF Timasheff SN (1997) The thermodynamic mechanism of protein stabilization by trehalose. Biophys Chem 64, 25 43.
    • (1997) Biophys Chem , vol.64 , pp. 25-43
    • Xie, G.F.1    Timasheff, S.N.2
  • 23
    • 0023659990 scopus 로고
    • Stabilization of phosphofructokinase with sugars during freeze-drying - Characterization of enhanced protection in the presence of divalent-cations
    • Carpenter JF, Crowe LM Crowe JH (1987) Stabilization of phosphofructokinase with sugars during freeze-drying - characterization of enhanced protection in the presence of divalent-cations. Biochim Biophys Acta 923, 109 115.
    • (1987) Biochim Biophys Acta , vol.923 , pp. 109-115
    • Carpenter, J.F.1    Crowe, L.M.2    Crowe, J.H.3
  • 24
    • 0348053809 scopus 로고
    • Preservation of membranes in anhydrobiotic organisms - The role of trehalose
    • Crowe JH, Crowe LM Chapman D (1984) Preservation of membranes in anhydrobiotic organisms - the role of trehalose. Science 223, 701 703.
    • (1984) Science , vol.223 , pp. 701-703
    • Crowe, J.H.1    Crowe, L.M.2    Chapman, D.3
  • 25
    • 0031736892 scopus 로고    scopus 로고
    • Promotion of polypeptide folding by interactions with Asn-glycans
    • Kimura N, Uchida M, Nishimura S Yamaguchi H (1998) Promotion of polypeptide folding by interactions with Asn-glycans. J Biochem 124, 857 862. (Pubitemid 28488168)
    • (1998) Journal of Biochemistry , vol.124 , Issue.4 , pp. 857-862
    • Kimura, N.1    Uchida, M.2    Nishimura, S.3    Yamaguchi, H.4
  • 26
    • 33846005807 scopus 로고    scopus 로고
    • Attributes of glycosylation in the establishment of the unfolding pathway of soybean agglutinin
    • DOI 10.1529/biophysj.106.092668
    • Sinha S Surolia A (2007) Attributes of glycosylation in the establishment of the unfolding pathway of soybean agglutinin. Biophys J 92, 208 216. (Pubitemid 46048429)
    • (2007) Biophysical Journal , vol.92 , Issue.1 , pp. 208-216
    • Sinha, S.1    Surolia, A.2
  • 27
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water - How do solvents affect these processes
    • Timasheff SN (1993) The control of protein stability and association by weak interactions with water - how do solvents affect these processes. Annu Rev Biophys Biomol Struct 22, 67 97.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 28
    • 67649860671 scopus 로고    scopus 로고
    • Combined approaches to the synthesis and study of glycoproteins
    • Bernardes GJL, Castagner B Seeberger PH (2009) Combined approaches to the synthesis and study of glycoproteins. ACS Chem Biol 4, 703 713.
    • (2009) ACS Chem Biol , vol.4 , pp. 703-713
    • Bernardes, G.J.L.1    Castagner, B.2    Seeberger, P.H.3
  • 29
    • 70350509098 scopus 로고    scopus 로고
    • A new ligation strategy for peptide and protein glycosylation: Photoinduced thiol-ene coupling
    • Dondoni A, Massi A, Nanni P Roda A (2009) A new ligation strategy for peptide and protein glycosylation: photoinduced thiol-ene coupling. Chem Eur J 15, 11444 11449.
    • (2009) Chem Eur J , vol.15 , pp. 11444-11449
    • Dondoni, A.1    Massi, A.2    Nanni, P.3    Roda, A.4
  • 31
    • 0141565183 scopus 로고    scopus 로고
    • Site-specific glycosylation of an aglycosylated human IgG1-Fc antibody protein generates neoglycoproteins with enhanced function
    • DOI 10.1016/j.chembiol.2003.08.006
    • Watt GM, Lund J, Levens M, Kolli VSK, Jefferis R Boons GJ (2003) Site-specific glycosylation of an aglycosylated human IgG1-Fc antibody protein generates neoglycoproteins with enhanced function. Chem Biol 10, 807 814. (Pubitemid 37171899)
    • (2003) Chemistry and Biology , vol.10 , Issue.9 , pp. 807-814
    • Watt, G.M.1    Lund, J.2    Levens, M.3    Kolli, V.S.K.4    Jefferis, R.5    Boons, G.-J.6
  • 32
    • 0035057706 scopus 로고    scopus 로고
    • Selective in vitro glycosylation of recombinant proteins: Semi-synthesis of novel homogeneous glycoforms of human erythropoietin
    • DOI 10.1016/S1074-5521(00)90065-6, PII S107455210000065X
    • Macmillan D, Bill RM, Sage KA, Fern D Flitsch SL (2001) Selective in vitro glycosylation of recombinant proteins: semi-synthesis of novel homogeneous glycoforms of human erythropoietin. Chem Biol 8, 133 145. (Pubitemid 32300208)
    • (2001) Chemistry and Biology , vol.8 , Issue.2 , pp. 133-145
    • Macmillan, D.1    Bill, R.M.2    Sage, K.A.3    Fern, D.4    Flitsch, S.L.5
  • 34
    • 0025998876 scopus 로고
    • A novel method for the specific glycosylation of proteins
    • Davis NJ Flitsch SL (1991) A novel method for the specific glycosylation of proteins. Tetrahedron Lett 32, 6793 6796.
    • (1991) Tetrahedron Lett , vol.32 , pp. 6793-6796
    • Davis, N.J.1    Flitsch, S.L.2
  • 36
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • DOI 10.1021/bi962337c
    • Sawaya MR Kraut J (1997) Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry 36, 586 603. (Pubitemid 27057006)
    • (1997) Biochemistry , vol.36 , Issue.3 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 37
    • 0028952263 scopus 로고
    • A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from Escherichia coli
    • Iwakura M, Jones BE, Luo JB Matthews CR (1995) A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from Escherichia coli. J Biochem 117, 480 488.
    • (1995) J Biochem , vol.117 , pp. 480-488
    • Iwakura, M.1    Jones, B.E.2    Luo, J.B.3    Matthews, C.R.4
  • 38
    • 0016292941 scopus 로고
    • Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin
    • Greene RF Pace CN (1974) Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin. J Biol Chem 249, 5388 5393.
    • (1974) J Biol Chem , vol.249 , pp. 5388-5393
    • Greene, R.F.1    Pace, C.N.2
  • 39
    • 76149110500 scopus 로고    scopus 로고
    • Solvent effects on catalysis by Escherichia coli dihydrofolate reductase
    • Loveridge EJ, Tey LH Allemann RK (2010) Solvent effects on catalysis by Escherichia coli dihydrofolate reductase. J Am Chem Soc 132, 1137 1143.
    • (2010) J Am Chem Soc , vol.132 , pp. 1137-1143
    • Loveridge, E.J.1    Tey, L.H.2    Allemann, R.K.3
  • 40
    • 1842531419 scopus 로고    scopus 로고
    • Pivotal role of Gly 121 in dihydrofolate reductase from Escherichia coli: The altered structure of a mutant enzyme may form the basis of its diminished catalytic performance
    • Swanwick RS, Shrimpton PJ Allemann RK (2004) Pivotal role of Gly 121 in dihydrofolate reductase from Escherichia coli: the altered structure of a mutant enzyme may form the basis of its diminished catalytic performance. Biochemistry 43, 4119 4127.
    • (2004) Biochemistry , vol.43 , pp. 4119-4127
    • Swanwick, R.S.1    Shrimpton, P.J.2    Allemann, R.K.3
  • 41
    • 0037083390 scopus 로고    scopus 로고
    • Thermal unfolding molecular dynamics simulation of Escherichia coli dihydrofolate reductase: Thermal stability of protein domains and unfolding pathway
    • DOI 10.1002/prot.10040
    • Sham YY, Ma BY, Tsai CJ Nussinov R (2002) Thermal unfolding molecular dynamics simulation of Escherichia coli dihydrofolate reductase: thermal stability of protein domains and unfolding pathway. Proteins 46, 308 320. (Pubitemid 34150751)
    • (2002) Proteins: Structure, Function and Genetics , vol.46 , Issue.3 , pp. 308-320
    • Sham, Y.Y.1    Ma, B.2    Tsai, C.-J.3    Nussinov, R.4
  • 42
    • 0025373255 scopus 로고
    • Refolding of Escherichia coli dihydrofolate reductase: Sequential formation of substrate binding sites
    • DOI 10.1073/pnas.87.12.4413
    • Frieden C (1990) Refolding of Escherichia coli dihydrofolate-reductase - sequential formation of substrate binding sites. Proc Natl Acad Sci USA 87, 4413 4416. (Pubitemid 20204110)
    • (1990) Proceedings of the National Academy of Sciences of the United States of America , vol.87 , Issue.12 , pp. 4413-4416
    • Frieden, C.1
  • 43
    • 0026005997 scopus 로고    scopus 로고
    • Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
    • Kuwajima K, Garvey EP, Finn BE, Matthews CR Sugai S (2002) Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry 30, 7693 7703.
    • (2002) Biochemistry , vol.30 , pp. 7693-7703
    • Kuwajima, K.1    Garvey, E.P.2    Finn, B.E.3    Matthews, C.R.4    Sugai, S.5
  • 44
    • 0027315969 scopus 로고    scopus 로고
    • A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model
    • Jennings PA, Finn BE, Jones BE Matthews CR (2002) A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model. Biochemistry 32, 3783 3789.
    • (2002) Biochemistry , vol.32 , pp. 3783-3789
    • Jennings, P.A.1    Finn, B.E.2    Jones, B.E.3    Matthews, C.R.4
  • 45
    • 0028925815 scopus 로고    scopus 로고
    • Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy
    • Jones BE, Beechem JM Matthews CR (2002) Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy. Biochemistry 34, 1867 1877.
    • (2002) Biochemistry , vol.34 , pp. 1867-1877
    • Jones, B.E.1    Beechem, J.M.2    Matthews, C.R.3
  • 46
    • 29344466944 scopus 로고    scopus 로고
    • Conformation coupled enzyme catalysis: Single-molecule and transient kinetics investigation of dihydrofolate reductase
    • Antikainen NM, Smiley RD, Benkovic SJ Hammes GG (2005) Conformation coupled enzyme catalysis: single-molecule and transient kinetics investigation of dihydrofolate reductase. Biochemistry 44, 16835 16843.
    • (2005) Biochemistry , vol.44 , pp. 16835-16843
    • Antikainen, N.M.1    Smiley, R.D.2    Benkovic, S.J.3    Hammes, G.G.4
  • 48
    • 11144328151 scopus 로고    scopus 로고
    • Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle
    • DOI 10.1021/bi048119y
    • Venkitakrishnan RP, Zaborowski E, McElheny D, Benkovic SJ, Dyson HJ Wright PE (2004) Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle. Biochemistry 43, 16046 16055. (Pubitemid 40041018)
    • (2004) Biochemistry , vol.43 , Issue.51 , pp. 16046-16055
    • Venkitakrishnan, R.P.1    Zaborowski, E.2    McElheny, D.3    Benkovic, S.J.4    Dyson, H.J.5    Wright, P.E.6
  • 49
    • 0027998347 scopus 로고
    • Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: Important roles of a flexible loop in the stability and function
    • Gekko K, Kunori Y, Takeuchi H, Ichihara S Kodama M (1994) Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: important role of a flexible loop in the stability and function. J Biochem 116, 34 41. (Pubitemid 24230779)
    • (1994) Journal of Biochemistry , vol.116 , Issue.1 , pp. 34-41
    • Gekko, K.1    Kunori, Y.2    Takeuchi, H.3    Ichihara, S.4    Kodama, M.5
  • 50
    • 0031443372 scopus 로고    scopus 로고
    • Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant
    • Cameron CE Benkovic SJ (1997) Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant. Biochemistry 36, 15792 15800.
    • (1997) Biochemistry , vol.36 , pp. 15792-15800
    • Cameron, C.E.1    Benkovic, S.J.2
  • 51
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • Fierke CA, Johnson KA Benkovic SJ (1987) Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. Biochemistry 26, 4085 4092.
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3


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