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Volumn 13, Issue 7, 2003, Pages 1321-1324

Investigation of an antibody-ligase. Evidence for strain-induced catalysis

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; HAPTEN; LIGASE; THIOESTER;

EID: 0037424712     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-894X(03)00123-9     Document Type: Article
Times cited : (2)

References (20)
  • 2
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    • p-Nitrobenzyl esters were not viable substrates, with catalysis being either too ineffectual to detect reliably or absent altogether, suggesting that more activated acyl donors were required. Conveniently chromogenic p-nitrobenzyl esters were chosen because of their residual structural similarity to the hapten and, at the same time, higher reactivity than p-nitrobenzyl derivatives:
    • p-Nitrobenzyl esters were not viable substrates, with catalysis being either too ineffectual to detect reliably or absent altogether, suggesting that more activated acyl donors were required. Conveniently chromogenic p-nitrobenzyl esters were chosen because of their residual structural similarity to the hapten and, at the same time, higher reactivity than p-nitrobenzyl derivatives: Hirschmann R., Taylor C.M., Benkovic P.A., Taylor S.D., Yager K.M., Sprengler P.A., Smith A.B. III, Benkovic S.J. Science. 265:1994;234.
    • (1994) Science , vol.265 , pp. 234
    • Hirschmann, R.1    Taylor, C.M.2    Benkovic, P.A.3    Taylor, S.D.4    Yager, K.M.5    Sprengler, P.A.6    Smith A.B. III7    Benkovic, S.J.8
  • 3
    • 85031208093 scopus 로고    scopus 로고
    • note
    • The peptide bond formation was completely inhibited by addition of an amount of hapten 1 equal to twice the antibody concentration.
  • 5
    • 0031053443 scopus 로고    scopus 로고
    • Tawfik et al. subsequently reported p-nitrophenyl hydrolytic antibodies elicited by a p-nitrobenzyl phosphonate hapten:
    • Tawfik et al. subsequently reported p-nitrophenyl hydrolytic antibodies elicited by a p-nitrobenzyl phosphonate hapten: Tawfik D.S., Lindner A.B., Chap R., Eshhar Z., Green B.S. Eur. J. Biochem. 244:1997;619.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 619
    • Tawfik, D.S.1    Lindner, A.B.2    Chap, R.3    Eshhar, Z.4    Green, B.S.5
  • 7
    • 0028829779 scopus 로고
    • In contrast, enzyme-derived ligase, sublitigase, is incapable of cyclizing linear peptide precursors, containing less than 12 amino acids:
    • In contrast, enzyme-derived ligase, sublitigase, is incapable of cyclizing linear peptide precursors, containing less than 12 amino acids: Jackson D.Y., Burnier J.P., Wells J.A. J. Am. Chem. Soc. 117:1995;819.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 819
    • Jackson, D.Y.1    Burnier, J.P.2    Wells, J.A.3
  • 8
    • 0028290693 scopus 로고
    • Schultz et al. subsequently disclosed generation of an abzyme-ligase:
    • Schultz et al. subsequently disclosed generation of an abzyme-ligase: Jacobsen J.R., Schultz P.S. Proc. Natl. Acad. Sci. USA. 91:1994;5888.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5888
    • Jacobsen, J.R.1    Schultz, P.S.2
  • 12
    • 85031200522 scopus 로고    scopus 로고
    • note
    • Both the desired and diasteriomeric dipeptide standards were prepared for the kinetic assay.
  • 14
    • 85031202179 scopus 로고    scopus 로고
    • note
    • The residual activity data was consistent with reversible inhibition.
  • 20
    • 0004214524 scopus 로고
    • London: Longmans, Green and Co
    • Haldane J.B.S. Enzymes. 1930;Longmans, Green and Co, London.
    • (1930) Enzymes
    • Haldane, J.B.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.