메뉴 건너뛰기




Volumn 27, Issue 1, 2014, Pages 113-121

Catalytic efficiency of designed catalytic proteins

Author keywords

[No Author keywords available]

Indexed keywords

ESTER; PROTEIN; CATALYTIC PROTEIN; ORGANOPHOSPHATE; UNCLASSIFIED DRUG;

EID: 84904466057     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2014.06.006     Document Type: Review
Times cited : (98)

References (40)
  • 1
  • 2
    • 77956745716 scopus 로고
    • Catalysis by micelles, membranes and other aqueous aggregates as models of enzyme action
    • Kunitake T., Shinkai S. Catalysis by micelles, membranes and other aqueous aggregates as models of enzyme action. Adv Phys Org Chem 1981, 17:435-487.
    • (1981) Adv Phys Org Chem , vol.17 , pp. 435-487
    • Kunitake, T.1    Shinkai, S.2
  • 3
    • 1842582944 scopus 로고    scopus 로고
    • Biomimetic reactions catalyzed by cyclodextrins and their derivatives
    • Breslow R., Dong S.D. Biomimetic reactions catalyzed by cyclodextrins and their derivatives. Chem Rev 1998, 98:1997-2012.
    • (1998) Chem Rev , vol.98 , pp. 1997-2012
    • Breslow, R.1    Dong, S.D.2
  • 4
    • 84990085627 scopus 로고    scopus 로고
    • The design of molecular hosts, guest and their complexes
    • Cram D.J. The design of molecular hosts, guest and their complexes. Angew Chem Int Ed Engl 2003, 27:1009-1020.
    • (2003) Angew Chem Int Ed Engl , vol.27 , pp. 1009-1020
    • Cram, D.J.1
  • 5
    • 0033791659 scopus 로고    scopus 로고
    • Critical analysis of antibody catalysis
    • Hilvert D. Critical analysis of antibody catalysis. Annu Rev Biochem 2000, 69:751-793.
    • (2000) Annu Rev Biochem , vol.69 , pp. 751-793
    • Hilvert, D.1
  • 6
    • 77949860707 scopus 로고    scopus 로고
    • Designing artificial enzymes by intuition and computation
    • Nanda V., Koder R.L. Designing artificial enzymes by intuition and computation. Nat Chem 2010, 2:15-24.
    • (2010) Nat Chem , vol.2 , pp. 15-24
    • Nanda, V.1    Koder, R.L.2
  • 8
    • 65249171530 scopus 로고    scopus 로고
    • Design of protein-interaction specificity gives selective βZIP-binding peptides
    • Grigoryan G., Reinke A.W., Keating A.E. Design of protein-interaction specificity gives selective βZIP-binding peptides. Nature 2009, 458:859-864.
    • (2009) Nature , vol.458 , pp. 859-864
    • Grigoryan, G.1    Reinke, A.W.2    Keating, A.E.3
  • 9
    • 33947086265 scopus 로고
    • Physical organic chemistry of benzisoxazoles. II. Linearity of the Bronsted free energy relationship for the base-catalyzed decomposition of benzisoxazoles
    • Kemp D.S., Casey M.L. Physical organic chemistry of benzisoxazoles. II. Linearity of the Bronsted free energy relationship for the base-catalyzed decomposition of benzisoxazoles. J Am Chem Soc 1973, 95:6670-6680.
    • (1973) J Am Chem Soc , vol.95 , pp. 6670-6680
    • Kemp, D.S.1    Casey, M.L.2
  • 10
    • 0029793086 scopus 로고    scopus 로고
    • Off-the-shelf proteins that rival tailor-made antibodies as catalysts
    • Hollfelder F., Kirby A.J., Tawfik D.S. Off-the-shelf proteins that rival tailor-made antibodies as catalysts. Nature 1996, 383:60-63.
    • (1996) Nature , vol.383 , pp. 60-63
    • Hollfelder, F.1    Kirby, A.J.2    Tawfik, D.S.3
  • 12
    • 84863000087 scopus 로고    scopus 로고
    • Bridging the gaps in design methodologies by evolutionary optimization of the stability and proficiency of designed Kemp eliminase KE59
    • Khersonsky O., Kiss G., Röthlisberger D., Dym O., Albeck S., Houk K.N., Baker D., Tawfik D.S. Bridging the gaps in design methodologies by evolutionary optimization of the stability and proficiency of designed Kemp eliminase KE59. Proc Natl Acad Sci U S A 2012, 109:10358-10363.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 10358-10363
    • Khersonsky, O.1    Kiss, G.2    Röthlisberger, D.3    Dym, O.4    Albeck, S.5    Houk, K.N.6    Baker, D.7    Tawfik, D.S.8
  • 13
    • 0028869408 scopus 로고
    • Large rate accelerations in antibody catalysis by strategic use of haptenic charge
    • Thorn S.N., Daniels R.G., Auditor M.-T.M., Hilvert D. Large rate accelerations in antibody catalysis by strategic use of haptenic charge. Nature 1995, 373:228-230.
    • (1995) Nature , vol.373 , pp. 228-230
    • Thorn, S.N.1    Daniels, R.G.2    Auditor, M.-T.M.3    Hilvert, D.4
  • 14
    • 73249139757 scopus 로고    scopus 로고
    • An aspartate and a water molecule mediate efficient acid-base catalysis in a talored antibody pocket
    • Debler E.W., Muller R., Hilvert D., Wilson I.A. An aspartate and a water molecule mediate efficient acid-base catalysis in a talored antibody pocket. Proc Natl Acad Sci U S A 2009, 106:18539-18544.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 18539-18544
    • Debler, E.W.1    Muller, R.2    Hilvert, D.3    Wilson, I.A.4
  • 15
    • 0030798274 scopus 로고    scopus 로고
    • Catalysis of the Kemp elimination by antibodies elicitied against a cationic hapten
    • Genre-Grandpierre A., Tellier C. Catalysis of the Kemp elimination by antibodies elicitied against a cationic hapten. Bioorg Med Chem Lett 1997, 7:2497-2502.
    • (1997) Bioorg Med Chem Lett , vol.7 , pp. 2497-2502
    • Genre-Grandpierre, A.1    Tellier, C.2
  • 18
    • 84904513451 scopus 로고    scopus 로고
    • Design of catalytically amplified sensors for small molecules
    • Makhlynets O.V., Korendovych I.V. Design of catalytically amplified sensors for small molecules. Biomolecules 2014, 4:402-418.
    • (2014) Biomolecules , vol.4 , pp. 402-418
    • Makhlynets, O.V.1    Korendovych, I.V.2
  • 20
    • 84867093396 scopus 로고    scopus 로고
    • Engineering a model protein cavity to catalyze the Kemp elimination
    • Merski M., Shoichet B.K. Engineering a model protein cavity to catalyze the Kemp elimination. Proc Natl Acad Sci U S A 2012, 109:16179-16183.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 16179-16183
    • Merski, M.1    Shoichet, B.K.2
  • 21
    • 0032253961 scopus 로고    scopus 로고
    • Theozymes and compuzymes: theoretical models for biological catalysis
    • Tantillo D.J., Chen J., Houk K.N. Theozymes and compuzymes: theoretical models for biological catalysis. Curr Opin Chem Biol 1998, 2:743-750.
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 743-750
    • Tantillo, D.J.1    Chen, J.2    Houk, K.N.3
  • 23
    • 77649271939 scopus 로고    scopus 로고
    • Evolutionary optimization of computationally designed enzymes: Kemp eliminases of the KE07 series
    • Khersonsky O., Rothlisberger D., Dym O., Albeck S., Jackson C.J., Baker D., Tawfik D.S. Evolutionary optimization of computationally designed enzymes: Kemp eliminases of the KE07 series. J Mol Biol 2010, 396:1025-1042.
    • (2010) J Mol Biol , vol.396 , pp. 1025-1042
    • Khersonsky, O.1    Rothlisberger, D.2    Dym, O.3    Albeck, S.4    Jackson, C.J.5    Baker, D.6    Tawfik, D.S.7
  • 27
    • 33947322034 scopus 로고
    • Nonlinear structure-reactivity correlations. Reactivity of nucleophilic reagents toward esters
    • Jencks W.P., Gilchrist M. Nonlinear structure-reactivity correlations. Reactivity of nucleophilic reagents toward esters. J Am Chem Soc 1968, 90:2622-2637.
    • (1968) J Am Chem Soc , vol.90 , pp. 2622-2637
    • Jencks, W.P.1    Gilchrist, M.2
  • 28
    • 0014217102 scopus 로고
    • Esterase activities of human carbonic anhydrases B and C
    • Verpoorte J.A., Mehta S., Edsall J.T. Esterase activities of human carbonic anhydrases B and C. J Biol Chem 1967, 242:4221-4229.
    • (1967) J Biol Chem , vol.242 , pp. 4221-4229
    • Verpoorte, J.A.1    Mehta, S.2    Edsall, J.T.3
  • 29
    • 0033514981 scopus 로고    scopus 로고
    • Rate-determining step of Escherichia coli alkaline phosphatase altered by the removal of a positive charge at the active center
    • Sun L., Martin D.C., Kantrowitz E.R. Rate-determining step of Escherichia coli alkaline phosphatase altered by the removal of a positive charge at the active center. Biochemistry 1999, 38:2842-2848.
    • (1999) Biochemistry , vol.38 , pp. 2842-2848
    • Sun, L.1    Martin, D.C.2    Kantrowitz, E.R.3
  • 30
    • 0001468012 scopus 로고
    • Substituent effects on an antibody-catalyzed hydrolysis of phenyl-esters: further evidence for an acyl-antibody intermediate
    • Gibbs R.A., Benkovic P.A., Janda K.D., Lerner R.A., Benkovic S.J. Substituent effects on an antibody-catalyzed hydrolysis of phenyl-esters: further evidence for an acyl-antibody intermediate. J Am Chem Soc 1992, 114:3528-3534.
    • (1992) J Am Chem Soc , vol.114 , pp. 3528-3534
    • Gibbs, R.A.1    Benkovic, P.A.2    Janda, K.D.3    Lerner, R.A.4    Benkovic, S.J.5
  • 31
    • 0023759322 scopus 로고
    • Induction of an antibody that catalyzes the hydrolysis of an amide bond
    • Janda K.D., Schloeder D., Benkovic S.J., Lerner R.A. Induction of an antibody that catalyzes the hydrolysis of an amide bond. Science 1988, 241:1188-1191.
    • (1988) Science , vol.241 , pp. 1188-1191
    • Janda, K.D.1    Schloeder, D.2    Benkovic, S.J.3    Lerner, R.A.4
  • 32
    • 0031587461 scopus 로고    scopus 로고
    • Catalysis of hydrolysis and transesterification reactions of p-nitrophenyl esters by a designed helix-loop-helix dimer
    • Broo K.S., Brive L., Ahlberg P., Baltzer L. Catalysis of hydrolysis and transesterification reactions of p-nitrophenyl esters by a designed helix-loop-helix dimer. J Am Chem Soc 1997, 119:11362-11372.
    • (1997) J Am Chem Soc , vol.119 , pp. 11362-11372
    • Broo, K.S.1    Brive, L.2    Ahlberg, P.3    Baltzer, L.4
  • 33
    • 0034674345 scopus 로고    scopus 로고
    • a of reactive esters sets the stage for cooperativity in nucleophilic and general-acid catalysis
    • a of reactive esters sets the stage for cooperativity in nucleophilic and general-acid catalysis. Chemistry 2000, 6:2214-2220.
    • (2000) Chemistry , vol.6 , pp. 2214-2220
    • Nilsson, J.1    Baltzer, L.2
  • 34
    • 0035807809 scopus 로고    scopus 로고
    • Enzyme-like proteins by computational design
    • Bolon D.N., Mayo S. Enzyme-like proteins by computational design. Proc Natl Acad Sci U S A 2001, 98:14274-14279.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14274-14279
    • Bolon, D.N.1    Mayo, S.2
  • 35
    • 0842270116 scopus 로고    scopus 로고
    • Enzyme-like proteins from an unselected library of designed amino acid sequences
    • Wei Y., Hecht M.H. Enzyme-like proteins from an unselected library of designed amino acid sequences. Protein Eng Des Sel 2004, 17:67-75.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 67-75
    • Wei, Y.1    Hecht, M.H.2
  • 38
    • 84860773275 scopus 로고    scopus 로고
    • Catalysis by a de novo zinc-mediated protein interface: implications for natural enzyme evolution and rational enzyme engineering
    • Der B.S., Edwards D.R., Kuhlman B. Catalysis by a de novo zinc-mediated protein interface: implications for natural enzyme evolution and rational enzyme engineering. Biochemistry 2012, 51:3933-3940.
    • (2012) Biochemistry , vol.51 , pp. 3933-3940
    • Der, B.S.1    Edwards, D.R.2    Kuhlman, B.3
  • 39
    • 84856397386 scopus 로고    scopus 로고
    • Hydrolytic catalysis and structural stabilization in a designed metalloprotein
    • Zastrow M.L., Peacock A.F.A., Stuckey J.A., Pecoraro V.L. Hydrolytic catalysis and structural stabilization in a designed metalloprotein. Nat Chem 2012, 4:118-123.
    • (2012) Nat Chem , vol.4 , pp. 118-123
    • Zastrow, M.L.1    Peacock, A.F.A.2    Stuckey, J.A.3    Pecoraro, V.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.