메뉴 건너뛰기




Volumn 401, Issue 3, 2007, Pages 721-726

Evidence that the mechanism of antibody-catalysed hydrolysis of arylcarbamates can be determined by the structure of the immunogen used to elicit the catalytic antibody

Author keywords

Antibody; Catalytic antibody; Hydrolysis; Mechanism

Indexed keywords

ANTIBODIES; CATALYSIS; HYDROLYSIS; IMMUNOLOGY; REACTION KINETICS; SUBSTITUTION REACTIONS; SUBSTRATES;

EID: 33846876098     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20060551     Document Type: Article
Times cited : (6)

References (26)
  • 1
    • 33947547892 scopus 로고
    • Molecular architecture and biological reactions
    • Pauling, L. (1946) Molecular architecture and biological reactions. Chem. Eng. News. 24, 1375-1377
    • (1946) Chem. Eng. News , vol.24 , pp. 1375-1377
    • Pauling, L.1
  • 4
    • 0033791659 scopus 로고    scopus 로고
    • Critical analysis of antibody catalysis
    • Hilvert, D. (2000) Critical analysis of antibody catalysis. Ann. Rev. Biochem. 69, 751-793
    • (2000) Ann. Rev. Biochem , vol.69 , pp. 751-793
    • Hilvert, D.1
  • 5
    • 0000468730 scopus 로고    scopus 로고
    • Binding energy and catalysis: The implications for transition-state analogs and catalytic antibodies
    • Mader, M. M. and Bartlett, P. A. (1997) Binding energy and catalysis: the implications for transition-state analogs and catalytic antibodies. Chem. Rev. 97, 1281-1301
    • (1997) Chem. Rev , vol.97 , pp. 1281-1301
    • Mader, M.M.1    Bartlett, P.A.2
  • 8
    • 9144238827 scopus 로고    scopus 로고
    • Improvement in hydrolytic antibody activity by change in haptenic structure from phosphate to phosphonate with retention of a common leaving-group determinant: Evidence for the 'flexibility' hypothesis
    • Gul, S., Sonkaria, S., Pinitglang, S., Florez-Alvarez, J., Hussain, S., Thomas, E. W., Ostler, E. L., Gallacher, G., Resmini, M. and Brocklehurst, K. (2003) Improvement in hydrolytic antibody activity by change in haptenic structure from phosphate to phosphonate with retention of a common leaving-group determinant: evidence for the 'flexibility' hypothesis. Biochem. J. 376, 813-821
    • (2003) Biochem. J , vol.376 , pp. 813-821
    • Gul, S.1    Sonkaria, S.2    Pinitglang, S.3    Florez-Alvarez, J.4    Hussain, S.5    Thomas, E.W.6    Ostler, E.L.7    Gallacher, G.8    Resmini, M.9    Brocklehurst, K.10
  • 9
    • 3142729079 scopus 로고    scopus 로고
    • Evidence for 'lock and key' character in an antiphosphonate hydrolytic antibody catalytic site augmented by non-reaction centre recognition: Variation in substrate selectivity between an anti-phosphonate antibody, an anti-phosphate antibody and two hydrolytic enzymes
    • Sonkaria, S., Boucher, G., Florez-Alvarez, J., Said, B., Hussain, S., Ostler, E. L., Gul, S., Thomas, E. W., Resmini, M., Gallacher, G. and Brocklehurst, K. (2004) Evidence for 'lock and key' character in an antiphosphonate hydrolytic antibody catalytic site augmented by non-reaction centre recognition: variation in substrate selectivity between an anti-phosphonate antibody, an anti-phosphate antibody and two hydrolytic enzymes. Biochem. J. 381, 125-310
    • (2004) Biochem. J , vol.381 , pp. 125-310
    • Sonkaria, S.1    Boucher, G.2    Florez-Alvarez, J.3    Said, B.4    Hussain, S.5    Ostler, E.L.6    Gul, S.7    Thomas, E.W.8    Resmini, M.9    Gallacher, G.10    Brocklehurst, K.11
  • 12
    • 37049142425 scopus 로고
    • Alkaline hydrolysis of substituted phenyl N-phenylcarbamates, Structure-reactivity relationships consistent with an E1cB mechanism
    • Williams, A. (1972) Alkaline hydrolysis of substituted phenyl N-phenylcarbamates, Structure-reactivity relationships consistent with an E1cB mechanism. J. Chem. Soc. Perkin Trans. 2, 808-812
    • (1972) J. Chem. Soc. Perkin Trans , vol.2 , pp. 808-812
    • Williams, A.1
  • 13
    • 37049132783 scopus 로고
    • Elimination-addition mechanism for the hydrolysis of carbamates, Trapping of an isocyanate intermediate by an o-amino-group
    • Hegarty, A. F. and Frost, L. N. (1973) Elimination-addition mechanism for the hydrolysis of carbamates, Trapping of an isocyanate intermediate by an o-amino-group. J. Chem. Soc. Perkin Trans. 2, 1719-1728
    • (1973) J. Chem. Soc. Perkin Trans , vol.2 , pp. 1719-1728
    • Hegarty, A.F.1    Frost, L.N.2
  • 15
    • 0000606860 scopus 로고
    • The influence of the leaving tendency of the phenoxy group on the ammonolysis and hydrolysis of substituted phenyl acetates
    • Bruice, T. C. and Mayahi, M. F. (1960) The influence of the leaving tendency of the phenoxy group on the ammonolysis and hydrolysis of substituted phenyl acetates. J. Am. Chem. Soc. 82, 3067-3071
    • (1960) J. Am. Chem. Soc , vol.82 , pp. 3067-3071
    • Bruice, T.C.1    Mayahi, M.F.2
  • 16
    • 0034652121 scopus 로고    scopus 로고
    • A general kinetic approach to investigation of active-site availability in macromolecular catalysis
    • Resmini, M., Gul, S., Carter., S., Sonkaria, S., Topham, C. M., Gallacher, G. and Brocklehurst, K. (2000) A general kinetic approach to investigation of active-site availability in macromolecular catalysis. Biochem. J. 346, 117-125
    • (2000) Biochem. J , vol.346 , pp. 117-125
    • Resmini, M.1    Gul, S.2    Carter, S.3    Sonkaria, S.4    Topham, C.M.5    Gallacher, G.6    Brocklehurst, K.7
  • 17
    • 0034853355 scopus 로고    scopus 로고
    • Kinetic and titration methods for determination of active site contents of enzyme and catalytic antibody preparations
    • Brocklehurst, K., Resmini, M. and Topham, C. M. (2001) Kinetic and titration methods for determination of active site contents of enzyme and catalytic antibody preparations. Methods 24, 153-167
    • (2001) Methods , vol.24 , pp. 153-167
    • Brocklehurst, K.1    Resmini, M.2    Topham, C.M.3
  • 18
    • 0034697408 scopus 로고    scopus 로고
    • The kinetic basis of a general method for the investigation of active site content of enzymes and catalytic antibodies: First order behaviour under single turnover and cycling conditions
    • Topham, C. M., Gul, S., Resmini, M., Sonkaria, S., Gallacher, G. and Brocklehurst, K. (2000) The kinetic basis of a general method for the investigation of active site content of enzymes and catalytic antibodies: first order behaviour under single turnover and cycling conditions. J. Theor. Biol. 204, 239-256
    • (2000) J. Theor. Biol , vol.204 , pp. 239-256
    • Topham, C.M.1    Gul, S.2    Resmini, M.3    Sonkaria, S.4    Gallacher, G.5    Brocklehurst, K.6
  • 19
    • 0033999087 scopus 로고    scopus 로고
    • An investigation of antibody acyl hydrolysis catalysis using a large set of related haptens
    • Odenbaugh, A. L., Helms, E. D. and Iverson, B. L. (2000) An investigation of antibody acyl hydrolysis catalysis using a large set of related haptens. Bioorg. Med. Chem. 8, 413-426
    • (2000) Bioorg. Med. Chem , vol.8 , pp. 413-426
    • Odenbaugh, A.L.1    Helms, E.D.2    Iverson, B.L.3
  • 21
    • 0030761840 scopus 로고    scopus 로고
    • Polyclonal catalytic antibody for hetero-cycloaddition of hepta-1,3-diene with ethyl glyoxylate an approach to the synthesis of 2-nonulosonic acid analogs
    • Hu, Y. J., Ji, Y. Y., Wu, Y. L., Yang, B. H. and Yeh, M. (1997) Polyclonal catalytic antibody for hetero-cycloaddition of hepta-1,3-diene with ethyl glyoxylate an approach to the synthesis of 2-nonulosonic acid analogs. Biorg. Med. Chem. Lett. 7, 1601-1606
    • (1997) Biorg. Med. Chem. Lett , vol.7 , pp. 1601-1606
    • Hu, Y.J.1    Ji, Y.Y.2    Wu, Y.L.3    Yang, B.H.4    Yeh, M.5
  • 23
    • 0030983982 scopus 로고    scopus 로고
    • Characterization of the hydrolytic activity of a polyclonal catalytic antibody preparation by pH-dependence and chemical modification studies: Evidence for Tyr and Arg side chains as hydrogen bond donors
    • Resmini, M., Vigna, R., Simms, C., Barber, J., Hagi-Pavli, E. P., Watts, A., Verma, C., Gallacher, G. and Brocklehurst, K. (1997) Characterization of the hydrolytic activity of a polyclonal catalytic antibody preparation by pH-dependence and chemical modification studies: evidence for Tyr and Arg side chains as hydrogen bond donors. Biochem. J. 326 279-287
    • (1997) Biochem. J , vol.326 , pp. 279-287
    • Resmini, M.1    Vigna, R.2    Simms, C.3    Barber, J.4    Hagi-Pavli, E.P.5    Watts, A.6    Verma, C.7    Gallacher, G.8    Brocklehurst, K.9
  • 25
    • 0028918401 scopus 로고
    • A proficient enzyme
    • Radzicka, A. and Wolfenden, R. (1995) A proficient enzyme. Science 267, 90-93
    • (1995) Science , vol.267 , pp. 90-93
    • Radzicka, A.1    Wolfenden, R.2
  • 26
    • 33947303518 scopus 로고
    • Multiple structure reactivity correlations. Alkaline hydrolyses of acyl and aryl substituted benzoates
    • Kirsch, J. F., Clewell, W. and Simon, A. (1968) Multiple structure reactivity correlations. Alkaline hydrolyses of acyl and aryl substituted benzoates. J. Org. Chem. 33, 127-132
    • (1968) J. Org. Chem , vol.33 , pp. 127-132
    • Kirsch, J.F.1    Clewell, W.2    Simon, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.