메뉴 건너뛰기




Volumn 8, Issue 2, 1999, Pages 410-417

Breaking the low barrier hydrogen bond in a serine protease

Author keywords

Conformational change; Organic co solvents; Protein crystallography; Subtilisin

Indexed keywords

HYDROGEN; SERINE PROTEINASE; SOLVENT; SUBTILISIN;

EID: 0032966653     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.2.410     Document Type: Article
Times cited : (32)

References (36)
  • 1
    • 0025757012 scopus 로고
    • Engineering subtilisin and its substrates for efficient ligation of peptide bonds in aqueous solution
    • Abrahmsen L, Tom J, Bumier J, Butcher KA, Kossiakoff A, Wells JA. 1991. Engineering subtilisin and its substrates for efficient ligation of peptide bonds in aqueous solution. Biochemistry 30:4151-4159.
    • (1991) Biochemistry , vol.30 , pp. 4151-4159
    • Abrahmsen, L.1    Tom, J.2    Bumier, J.3    Butcher, K.A.4    Kossiakoff, A.5    Wells, J.A.6
  • 2
    • 0030723218 scopus 로고    scopus 로고
    • A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment
    • Ash EL, Sudmeier JL, DeFabo EC, Bachovchin WW. 1997. A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment. Science 278:1128-1132.
    • (1997) Science , vol.278 , pp. 1128-1132
    • Ash, E.L.1    Sudmeier, J.L.2    DeFabo, E.C.3    Bachovchin, W.W.4
  • 3
    • 33947094423 scopus 로고
    • Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of alpha-lytic protease. Implications for the charge-relay mechanism of peptide bond cleavage by serine proteases
    • Bachovchin WW, Roberts JD. 1978. Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of alpha-lytic protease. Implications for the charge-relay mechanism of peptide bond cleavage by serine proteases. J Am Chem Soc 100:8041-8047.
    • (1978) J Am Chem Soc , vol.100 , pp. 8041-8047
    • Bachovchin, W.W.1    Roberts, J.D.2
  • 4
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger AT, Kuriyan J, Karplus M. 1987. Crystallographic R factor refinement by molecular dynamics. Science 235:458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 5
    • 0017836261 scopus 로고
    • On the mechanism of action of methyl chymotrypsin
    • Byers LD, Koshland DE Jr. 1978. On the mechanism of action of methyl chymotrypsin. Bioorg Chem 7:15-33.
    • (1978) Bioorg Chem , vol.7 , pp. 15-33
    • Byers, L.D.1    Koshland D.E., Jr.2
  • 6
    • 0023384982 scopus 로고
    • Engineering enzyme specificity by "substrate-assisted catalysis."
    • Carter P, Wells JA. 1987. Engineering enzyme specificity by "substrate-assisted catalysis." Science 237:394-399.
    • (1987) Science , vol.237 , pp. 394-399
    • Carter, P.1    Wells, J.A.2
  • 7
    • 0015994917 scopus 로고
    • pH dependence of chymotrypsin catalysis
    • Fersht AR, Renard M. 1974. pH dependence of chymotrypsin catalysis. Biochemistry 13:1416-1426.
    • (1974) Biochemistry , vol.13 , pp. 1416-1426
    • Fersht, A.R.1    Renard, M.2
  • 8
    • 0017226279 scopus 로고
    • Low-resolution structure of the glycogen phosphorylase a monomer and comparison with phosphorylase b
    • Fletterick RJ, Sygusch J, Murray N, Madsen NB, Johnson LN. 1976. Low-resolution structure of the glycogen phosphorylase a monomer and comparison with phosphorylase b. J Mol Biol 103:1-13.
    • (1976) J Mol Biol , vol.103 , pp. 1-13
    • Fletterick, R.J.1    Sygusch, J.2    Murray, N.3    Madsen, N.B.4    Johnson, L.N.5
  • 9
    • 0028040716 scopus 로고
    • A low-barrier hydrogen bond in the catalytic triad of serine proteases
    • Frey PA, Whitt SA, Tobin JB. 1994. A low-barrier hydrogen bond in the catalytic triad of serine proteases. Science 264:1927-1930.
    • (1994) Science , vol.264 , pp. 1927-1930
    • Frey, P.A.1    Whitt, S.A.2    Tobin, J.B.3
  • 10
    • 0026655149 scopus 로고
    • Organic solvent changes the chymotrypsin specificity with respect to nucleophiles
    • Gololobov MY, Voyushina TL, Stepanov VM, Adlercreutz P. 1992. Organic solvent changes the chymotrypsin specificity with respect to nucleophiles. FEBS Lett 307:309-312.
    • (1992) FEBS Lett , vol.307 , pp. 309-312
    • Gololobov, M.Y.1    Voyushina, T.L.2    Stepanov, V.M.3    Adlercreutz, P.4
  • 11
    • 10544255345 scopus 로고    scopus 로고
    • A low-barrier hydrogen bond in subtilisin: 1H and 15N NMR studies with peptidyl trifluoromethyl ketones
    • Halkides CJ, Wu YQ, Murray CJ. 1996. A low-barrier hydrogen bond in subtilisin: 1H and 15N NMR studies with peptidyl trifluoromethyl ketones. Biochemistry 35:15941-15948.
    • (1996) Biochemistry , vol.35 , pp. 15941-15948
    • Halkides, C.J.1    Wu, Y.Q.2    Murray, C.J.3
  • 12
    • 0015103388 scopus 로고
    • Catalytic activity of alpha-chymotrypsin in which histidine 57 has been methylated
    • Henderson R. 1971. Catalytic activity of alpha-chymotrypsin in which histidine 57 has been methylated. Biochem J 124:13-18.
    • (1971) Biochem J , vol.124 , pp. 13-18
    • Henderson, R.1
  • 13
    • 84945096204 scopus 로고
    • Model bias in macromolecular crystal structures
    • Hodel A, Kim S-H, Brünger AT. 1992. Model bias in macromolecular crystal structures. Acta Crystallogr A 48:851-858.
    • (1992) Acta Crystallogr A , vol.48 , pp. 851-858
    • Hodel, A.1    Kim, S.-H.2    Brünger, A.T.3
  • 14
    • 0018278636 scopus 로고
    • Synthesis of peptide bonds by proteinases. Addition of organic cosolvents shifts peptide bond equilibria toward synthesis
    • Homandberg GA, Mattis JA, Laskowski M Jr. 1978. Synthesis of peptide bonds by proteinases. Addition of organic cosolvents shifts peptide bond equilibria toward synthesis. Biochemistry 17:5220-5227.
    • (1978) Biochemistry , vol.17 , pp. 5220-5227
    • Homandberg, G.A.1    Mattis, J.A.2    Laskowski M., Jr.3
  • 15
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 16
    • 0029897902 scopus 로고    scopus 로고
    • A weak calcium binding site in subtilisin BPN′ has a dramatic effect on protein stability
    • Kidd RD, Yennawar HP, Sears P, Wong C-H, Farber GK. 1996. A weak calcium binding site in subtilisin BPN′ has a dramatic effect on protein stability. J Am Chem Soc 118:1645-1650.
    • (1996) J Am Chem Soc , vol.118 , pp. 1645-1650
    • Kidd, R.D.1    Yennawar, H.P.2    Sears, P.3    Wong, C.-H.4    Farber, G.K.5
  • 17
    • 0025101851 scopus 로고
    • Chymotrypsin suspended in organic solvents with salt hydrates is a good catalyst for peptide synthesis from mainly undissolved reactants
    • Kuhl P, Halling PJ, Jakubke H-D. 1990. Chymotrypsin suspended in organic solvents with salt hydrates is a good catalyst for peptide synthesis from mainly undissolved reactants. Tetrahedron Lett 31:5213-5216.
    • (1990) Tetrahedron Lett , vol.31 , pp. 5213-5216
    • Kuhl, P.1    Halling, P.J.2    Jakubke, H.-D.3
  • 18
    • 0018141241 scopus 로고
    • Hydrogen bonds in serine proteinases and their complexes with protein proteinase inhibitors. Proton nuclear magnetic resonance studies
    • Markley JL. 1978. Hydrogen bonds in serine proteinases and their complexes with protein proteinase inhibitors. Proton nuclear magnetic resonance studies. Biochemistry 17:4648-4656.
    • (1978) Biochemistry , vol.17 , pp. 4648-4656
    • Markley, J.L.1
  • 21
    • 0024962392 scopus 로고
    • Large increases in general stability for subtilisin BPN′ through incremental changes in the free energy of unfolding
    • Pantoliano MW, Whitlow M, Wood JF, Dodd SW, Hardman KD, Rollence ML, Bryan PN. 1989. Large increases in general stability for subtilisin BPN′ through incremental changes in the free energy of unfolding. Biochemistry 28:7205-7213.
    • (1989) Biochemistry , vol.28 , pp. 7205-7213
    • Pantoliano, M.W.1    Whitlow, M.2    Wood, J.F.3    Dodd, S.W.4    Hardman, K.D.5    Rollence, M.L.6    Bryan, P.N.7
  • 23
    • 0022307510 scopus 로고
    • Diffraction methods for biological macromolecules. Flow cell construction and use
    • Petsko GA. 1985. Diffraction methods for biological macromolecules. Flow cell construction and use. Methods Enzymol 114:141-146.
    • (1985) Methods Enzymol , vol.114 , pp. 141-146
    • Petsko, G.A.1
  • 24
    • 0028000937 scopus 로고
    • Engineering subtilisin for peptide coupling: Studies on the effects of counterions and site-specific modifications on the stability and specificity of the enzyme
    • Sears P, Schuster M, Wang P, Witte K, Wong C-H. 1994. Engineering subtilisin for peptide coupling: Studies on the effects of counterions and site-specific modifications on the stability and specificity of the enzyme. J Am Chem Soc 116:6521-6530.
    • (1994) J Am Chem Soc , vol.116 , pp. 6521-6530
    • Sears, P.1    Schuster, M.2    Wang, P.3    Witte, K.4    Wong, C.-H.5
  • 25
    • 0025363640 scopus 로고
    • The synthesis of a D-amino acid ester in an organic media with alpha-chymotrypsin modified by a bio-imprinting procedure
    • Stahl M, Mansson MO, Mosbach K. 1990. The synthesis of a D-amino acid ester in an organic media with alpha-chymotrypsin modified by a bio-imprinting procedure. Biotechnol Lett 12:161-166.
    • (1990) Biotechnol Lett , vol.12 , pp. 161-166
    • Stahl, M.1    Mansson, M.O.2    Mosbach, K.3
  • 26
    • 85022237431 scopus 로고
    • Inversion of enzyme enantioselectivity mediated by the solvent
    • Tawaki S, Klibanov AM. 1992. Inversion of enzyme enantioselectivity mediated by the solvent. J Am Chem Soc 114:1882-1884.
    • (1992) J Am Chem Soc , vol.114 , pp. 1882-1884
    • Tawaki, S.1    Klibanov, A.M.2
  • 27
    • 0029069320 scopus 로고
    • Low-barrier hydrogen bonding in molecular complexes analogous to histidine and aspartate in the catalytic triad of serine proteases
    • Tobin JB, Whitt SA, Cassidy CS, Frey PA. 1995. Low-barrier hydrogen bonding in molecular complexes analogous to histidine and aspartate in the catalytic triad of serine proteases. Biochemistry 34:6919-6924.
    • (1995) Biochemistry , vol.34 , pp. 6919-6924
    • Tobin, J.B.1    Whitt, S.A.2    Cassidy, C.S.3    Frey, P.A.4
  • 28
    • 0023783073 scopus 로고
    • Subtilisin - An enzyme designed to be engineered
    • Wells JA, Estell DA. 1988. Subtilisin - An enzyme designed to be engineered. TIBS 13:291-297.
    • (1988) TIBS , vol.13 , pp. 291-297
    • Wells, J.A.1    Estell, D.A.2
  • 29
    • 0025082964 scopus 로고
    • Enzymes as synthetic catalysts, mechanistic and active-site considerations of natural and modified chymotrypsin
    • West JB, Hennen WJ, Lalonde JL, Bibbs JA, Zhong Z, Meyer EF Jr, Wong C-H. 1990. Enzymes as synthetic catalysts, mechanistic and active-site considerations of natural and modified chymotrypsin. J Am Chem Soc 112:5313-5320.
    • (1990) J Am Chem Soc , vol.112 , pp. 5313-5320
    • West, J.B.1    Hennen, W.J.2    Lalonde, J.L.3    Bibbs, J.A.4    Zhong, Z.5    Meyer E.F., Jr.6    Wong, C.-H.7
  • 30
    • 0024382916 scopus 로고
    • Enzymatic catalysts in organic synthesis
    • Wong C-H. 1989. Enzymatic catalysts in organic synthesis. Science 244:1145-1152.
    • (1989) Science , vol.244 , pp. 1145-1152
    • Wong, C.-H.1
  • 32
    • 0000321692 scopus 로고
    • Enzyme-catalyzed processes in organic solvents
    • Zaks A, Klibanov AM. 1985. Enzyme-catalyzed processes in organic solvents. Proc Natl Acad Sci USA 82:3192-3196.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 3192-3196
    • Zaks, A.1    Klibanov, A.M.2
  • 33
    • 0000836283 scopus 로고
    • Substrate specificity of enzymes in organic solvents vs. water is reversed
    • Zaks A, Klibanov AM. 1986. Substrate specificity of enzymes in organic solvents vs. water is reversed. J Am Chem Soc 108:2767-2768.
    • (1986) J Am Chem Soc , vol.108 , pp. 2767-2768
    • Zaks, A.1    Klibanov, A.M.2
  • 34
    • 0024278258 scopus 로고
    • Enzymatic catalysis in nonaqueous solvents
    • Zaks A, Klibanov AM. 1988. Enzymatic catalysis in nonaqueous solvents. J Biol Chem 263:3194-3201.
    • (1988) J Biol Chem , vol.263 , pp. 3194-3201
    • Zaks, A.1    Klibanov, A.M.2
  • 35
    • 0025970164 scopus 로고
    • Engineering subtilisin for reaction in dimethylformamide
    • Zhong Z, Bibbs JA, Yuan W, Wong C-H. 1991a. Engineering subtilisin for reaction in dimethylformamide. J Am Chem Soc 113:683-684.
    • (1991) J Am Chem Soc , vol.113 , pp. 683-684
    • Zhong, Z.1    Bibbs, J.A.2    Yuan, W.3    Wong, C.-H.4
  • 36
    • 0001287339 scopus 로고
    • Active-site-directed modification of subtilisin
    • Zhong Z, Bibbs JA, Yuan W, Wong C-H. 1991b. Active-site-directed modification of subtilisin. J Am Chem Soc 113:2259-2263.
    • (1991) J Am Chem Soc , vol.113 , pp. 2259-2263
    • Zhong, Z.1    Bibbs, J.A.2    Yuan, W.3    Wong, C.-H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.