메뉴 건너뛰기




Volumn 3, Issue 6, 1996, Pages 433-445

Hydrolytic antibodies: Variations on a theme

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC ANTIBODY;

EID: 0030155251     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(96)90091-5     Document Type: Review
Times cited : (96)

References (58)
  • 1
    • 0000138520 scopus 로고
    • Proteolytic enzymes
    • (Colowick, S.P. & Kaplan, N.O., eds), Academic Press, Inc., New York
    • Perlmann, G.E. & Lorand, L., eds (1970). Proteolytic enzymes. In Methods in Enzymology. (Colowick, S.P. & Kaplan, N.O., eds), Academic Press, Inc., New York.
    • (1970) Methods in Enzymology
    • Perlmann, G.E.1    Lorand, L.2
  • 2
    • 0000138520 scopus 로고
    • Proteolytic enzymes: Part B
    • (Colowick, S.P. & Kaplan, N.O., eds), Academic Press, Inc., New York
    • Lorand, L., ed. (1976). Proteolytic enzymes: Part B. In Methods in Enzymology. (Colowick, S.P. & Kaplan, N.O., eds), Academic Press, Inc., New York.
    • (1976) Methods in Enzymology
    • Lorand, L.1
  • 3
    • 0019744312 scopus 로고
    • Proteolytic enzymes: Part C
    • (Colowick, S.P. & Kaplan, N.O., eds), Academic Press, Inc., New York
    • Lorand, L., ed. (1981). Proteolytic enzymes: Part C. In Methods in Enzymology. (Colowick, S.P. & Kaplan, N.O., eds), Academic Press, Inc., New York.
    • (1981) Methods in Enzymology
    • Lorand, L.1
  • 5
    • 0025730616 scopus 로고
    • At the crossroads of chemistry and immunology: Catalytic antibodies
    • Lerner, R.A., Benkovic, S.J. & Schultz, P.G. (1991). At the crossroads of chemistry and immunology: catalytic antibodies. Science 252, 659-667.
    • (1991) Science , vol.252 , pp. 659-667
    • Lerner, R.A.1    Benkovic, S.J.2    Schultz, P.G.3
  • 6
    • 0028817877 scopus 로고
    • From molecular diversity to catalysis: Lessons from the immune system
    • Schultz, P.G. & Lerner, R.A. (1995). From molecular diversity to catalysis: lessons from the immune system. Science 269, 1835-1842.
    • (1995) Science , vol.269 , pp. 1835-1842
    • Schultz, P.G.1    Lerner, R.A.2
  • 7
    • 0001299493 scopus 로고
    • A phosphonamidate dipeptide analogue as an inhibitor of carboxypeptidase A
    • Jacobsen, N.E. & Bartlett, P.A. (1981). A phosphonamidate dipeptide analogue as an inhibitor of carboxypeptidase A. J. Am. Chem. Soc. 103, 654-657.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 654-657
    • Jacobsen, N.E.1    Bartlett, P.A.2
  • 9
    • 0021113924 scopus 로고
    • Phosphonamidates as transition-state analogue inhibitors of thermolysin
    • Bartlett, P.A. & Marlowe, C.K. (1983). Phosphonamidates as transition-state analogue inhibitors of thermolysin. Biochemistry 22, 4618-4624.
    • (1983) Biochemistry , vol.22 , pp. 4618-4624
    • Bartlett, P.A.1    Marlowe, C.K.2
  • 10
    • 0026100862 scopus 로고
    • Peptidic phosphonylating agents as irreversible inhibitors of serine proteases and models of the tetrahedral intermediates
    • Sampson, N.S. & Bartlett, P.A. (1991). Peptidic phosphonylating agents as irreversible inhibitors of serine proteases and models of the tetrahedral intermediates. Biochemistry 30, 2255-2263.
    • (1991) Biochemistry , vol.30 , pp. 2255-2263
    • Sampson, N.S.1    Bartlett, P.A.2
  • 12
    • 0027980056 scopus 로고
    • Differences in the biochemical properties of esterolytic antibodies correlate with structural diversity
    • Zemel, R., Schindler, D.G., Tawfik, D.S., Eshhar, Z. & Green, B.S. (1994). Differences in the biochemical properties of esterolytic antibodies correlate with structural diversity. Mol. Immunol. 31, 127-137.
    • (1994) Mol. Immunol. , vol.31 , pp. 127-137
    • Zemel, R.1    Schindler, D.G.2    Tawfik, D.S.3    Eshhar, Z.4    Green, B.S.5
  • 13
    • 0029610074 scopus 로고
    • Crystal structure of the complex of a catalytic antibody Fab fragment with a transition-state analog: Structural similarities in esterase-like catalytic antibodies
    • Charbonnier, J.-B., et al., & Knossow, M. (1995). Crystal structure of the complex of a catalytic antibody Fab fragment with a transition-state analog: structural similarities in esterase-like catalytic antibodies. Proc. Natl. Acad. Sci. USA 92, 11721-11725.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11721-11725
    • Charbonnier, J.-B.1    Knossow, M.2
  • 14
    • 0028773154 scopus 로고
    • Crystal structure of a catalytic antibody Fab with esterase-like activity
    • Golinelli-Pimpaneau, B., et al., & Knossow, M. (1994). Crystal structure of a catalytic antibody Fab with esterase-like activity. Structure 2, 175-183.
    • (1994) Structure , vol.2 , pp. 175-183
    • Golinelli-Pimpaneau, B.1    Knossow, M.2
  • 17
  • 18
    • 0028011543 scopus 로고
    • Kinetic and mechanistic characterization of an efficient hydrolytic antibody: Evidence for the formation of an acyl intermediate
    • Guo, J., Huang, W. & Scanlan, T.S. (1994). Kinetic and mechanistic characterization of an efficient hydrolytic antibody: evidence for the formation of an acyl intermediate. J. Am. Chem. Soc. 116, 6062-6069.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 6062-6069
    • Guo, J.1    Huang, W.2    Scanlan, T.S.3
  • 19
    • 0028027058 scopus 로고
    • Crystal structure of a catalytic antibody with a serine protease active site
    • Zhou, G.W., Guo, J., Huang, W., Fletterick, R.J. & Scanlan, T.S. (1994). Crystal structure of a catalytic antibody with a serine protease active site. Science 265, 1059-1064.
    • (1994) Science , vol.265 , pp. 1059-1064
    • Zhou, G.W.1    Guo, J.2    Huang, W.3    Fletterick, R.J.4    Scanlan, T.S.5
  • 20
    • 0023513107 scopus 로고
    • Development of the primary antibody repertoire
    • Alt, F.W., Blackwell, T.K. & Yancopoulos, G.D. (1987). Development of the primary antibody repertoire. Science 238, 1079-1087.
    • (1987) Science , vol.238 , pp. 1079-1087
    • Alt, F.W.1    Blackwell, T.K.2    Yancopoulos, G.D.3
  • 21
    • 0023510298 scopus 로고
    • Evolutionary and somatic selection of the antibody repertoire in the mouse
    • Rajewsky, K., Förster, I. & Cumano, A. (1987). Evolutionary and somatic selection of the antibody repertoire in the mouse. Science 238, 1088-1094.
    • (1987) Science , vol.238 , pp. 1088-1094
    • Rajewsky, K.1    Förster, I.2    Cumano, A.3
  • 22
    • 0025242063 scopus 로고
    • Arginine 127 stabilizes the transition state in carboxypeptidase A
    • Phillips, M.A., Fletterick, R. & Rutter, W.J. (1990). Arginine 127 stabilizes the transition state in carboxypeptidase A. J. Biol. Chem. 265, 20692-20698.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20692-20698
    • Phillips, M.A.1    Fletterick, R.2    Rutter, W.J.3
  • 23
    • 0026581791 scopus 로고
    • Transition-state characterization: A new approach combining inhibitor analogues and variation in enzyme structure
    • Phillips, M.A., Kaplan, A.P., Rutter, W.J. & Bartlett, P.A. (1992). Transition-state characterization: a new approach combining inhibitor analogues and variation in enzyme structure. Biochemistry 31, 959-963.
    • (1992) Biochemistry , vol.31 , pp. 959-963
    • Phillips, M.A.1    Kaplan, A.P.2    Rutter, W.J.3    Bartlett, P.A.4
  • 24
    • 0029991227 scopus 로고    scopus 로고
    • The immunological evolution of catalysis
    • Patten, P.A., et al., & Schultz, P.G. (1996). The immunological evolution of catalysis. Science 271, 1086-1091.
    • (1996) Science , vol.271 , pp. 1086-1091
    • Patten, P.A.1    Schultz, P.G.2
  • 25
    • 0028955273 scopus 로고
    • Mechanistically different catalytic antibodies obtained from immunization with a single transition-state analog
    • Guo, J., Huang, W., Zhou, G.W., Fletterick, R.J. & Scanlan, T.S. (1995). Mechanistically different catalytic antibodies obtained from immunization with a single transition-state analog. Proc. Natl. Acad. Sci. USA 92, 1694-1698.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1694-1698
    • Guo, J.1    Huang, W.2    Zhou, G.W.3    Fletterick, R.J.4    Scanlan, T.S.5
  • 26
    • 0027407935 scopus 로고
    • A genetic approach to the generation of antibodies with enhanced catalytic activities
    • Lesley, S.A., Patten, P.A. & Schultz, P.G. (1993). A genetic approach to the generation of antibodies with enhanced catalytic activities. Proc. Natl. Acad Sci. USA 90, 1160-1165.
    • (1993) Proc. Natl. Acad Sci. USA , vol.90 , pp. 1160-1165
    • Lesley, S.A.1    Patten, P.A.2    Schultz, P.G.3
  • 27
    • 0025688224 scopus 로고
    • The enzymic nature of antibody catalysis: Development of multistep kinetic processing
    • Benkovic, S.J., Adams, J.A. & Borders, C.L., Jr. (1990). The enzymic nature of antibody catalysis: development of multistep kinetic processing. Science 250, 1135-1139.
    • (1990) Science , vol.250 , pp. 1135-1139
    • Benkovic, S.J.1    Adams, J.A.2    Borders Jr., C.L.3
  • 28
    • 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. (1988). Induction of an antibody that catalyzes the hydrolysis of an amide bond. Science 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
  • 29
    • 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, RA & Benkovic, S.J. (1992). Substituent effects on an antibody-catalyzed hydrolysis of phenyl esters: further evidence for an acyl-antibody intermediate. J. Am. Chem. Soc. 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
  • 30
    • 0028013654 scopus 로고
    • Catalytic antibody model and mutagenesis implicate arginine in transition-state stabilization
    • Roberts, V.A., Stewart, J., Benkovic, SJ. & Getzoff, E.D. (1994). Catalytic antibody model and mutagenesis implicate arginine in transition-state stabilization. J. Mol. Biol. 235, 1098-1116.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1098-1116
    • Roberts, V.A.1    Stewart, J.2    Benkovic, S.J.3    Getzoff, E.D.4
  • 31
    • 0028222096 scopus 로고
    • Site-directed mutagenesis of a catalytic antibody: An arginine and a histidine residue play key roles
    • Stewart, J.D., Roberts, V.A., Thomas, N.R., Getzoff, E.D. & Benkovic, S.J. (1994). Site-directed mutagenesis of a catalytic antibody: an arginine and a histidine residue play key roles. Biochemistry 33, 1994-2003.
    • (1994) Biochemistry , vol.33 , pp. 1994-2003
    • Stewart, J.D.1    Roberts, V.A.2    Thomas, N.R.3    Getzoff, E.D.4    Benkovic, S.J.5
  • 33
    • 0028898288 scopus 로고
    • Detection of a catalytic antibody species acylated at the active site by electrospray mass spectrometry
    • Krebs, J.F., Siuzdak, G. & Dyson, H.J. (1995). Detection of a catalytic antibody species acylated at the active site by electrospray mass spectrometry. Biochemistry 34, 720-723.
    • (1995) Biochemistry , vol.34 , pp. 720-723
    • Krebs, J.F.1    Siuzdak, G.2    Dyson, H.J.3
  • 34
    • 0025736815 scopus 로고
    • Construction and characterization of a single-chain catalytic antibody
    • Gibbs, R.A., et al., & Benkovic, S.J. (1991). Construction and characterization of a single-chain catalytic antibody. Proc. Natl. Acad. Sci. USA 88, 4001-4004.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4001-4004
    • Gibbs, R.A.1    Benkovic, S.J.2
  • 35
    • 0025808084 scopus 로고
    • Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 2. Structural basis of hapten binding and idiotypy
    • Strong, R.K., Petsko, G.A., Sharon, J. & Margolies, M.N. (1991). Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 2. Structural basis of hapten binding and idiotypy. Biochemistry 30, 3749-3757.
    • (1991) Biochemistry , vol.30 , pp. 3749-3757
    • Strong, R.K.1    Petsko, G.A.2    Sharon, J.3    Margolies, M.N.4
  • 36
    • 0021711720 scopus 로고
    • Somatic mutation and the maturation of immune response to 2-phenyl oxazolone
    • Griffiths, G.M., Berek, C., Kaartinen, M. & Milstein, C. (1984). Somatic mutation and the maturation of immune response to 2-phenyl oxazolone. Nature 312, 271-275.
    • (1984) Nature , vol.312 , pp. 271-275
    • Griffiths, G.M.1    Berek, C.2    Kaartinen, M.3    Milstein, C.4
  • 37
    • 0025119206 scopus 로고
    • Three-dimensional structure determination of an anti-2-phenyloxazolone antibody: The role of somatic mutation and heavy/light chain pairing in the maturation of an immune response
    • Alzari, P.M., et al., & Milstein, C. (1990). Three-dimensional structure determination of an anti-2-phenyloxazolone antibody: the role of somatic mutation and heavy/light chain pairing in the maturation of an immune response. EMBO J. 9, 3807-3814.
    • (1990) EMBO J. , vol.9 , pp. 3807-3814
    • Alzari, P.M.1    Milstein, C.2
  • 38
    • 0022032207 scopus 로고
    • On the specificity of antibody/antigen interactions: Phosphocholine binding to McPC603 and the correlation of three-dimensional structure and sequence data
    • Padlan, E.A., Cohen, G.H. & Davies, D.R. (1985). On the specificity of antibody/antigen interactions: phosphocholine binding to McPC603 and the correlation of three-dimensional structure and sequence data. Ann. Inst. Pasteur Immunol. 136C, 271-276.
    • (1985) Ann. Inst. Pasteur Immunol. , vol.136 C , pp. 271-276
    • Padlan, E.A.1    Cohen, G.H.2    Davies, D.R.3
  • 39
    • 0025799756 scopus 로고
    • Structural and kinetic studies of the Fab fragment of a monoclonal anti-spin label antibody by nuclear magnetic resonance
    • Theriault, T.P., Leahy, D.J., Levitt, M. & McConnell, H.M. (1991). Structural and kinetic studies of the Fab fragment of a monoclonal anti-spin label antibody by nuclear magnetic resonance. J. Mol. Biol. 221, 257-270.
    • (1991) J. Mol. Biol. , vol.221 , pp. 257-270
    • Theriault, T.P.1    Leahy, D.J.2    Levitt, M.3    McConnell, H.M.4
  • 41
    • 0024280501 scopus 로고
    • Dissecting the catalytic triad of a serine protease
    • Carter, P. & Wells, J.A. (1988). Dissecting the catalytic triad of a serine protease. Nature 332, 564-568.
    • (1988) Nature , vol.332 , pp. 564-568
    • Carter, P.1    Wells, J.A.2
  • 42
    • 0023783073 scopus 로고
    • Subtilisin - An enzyme designed to be engineered
    • Wells, J.A. & Estell, D.A. (1988). Subtilisin - an enzyme designed to be engineered. Trends Biochem. Sci. 13, 291-297.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 291-297
    • Wells, J.A.1    Estell, D.A.2
  • 43
    • 0025938822 scopus 로고
    • Comparison of the structures of three carboxypeptidase A-phosphonate complexes determined by X-ray crystallography
    • Kim, H. & Lipscomb, W.N. (1991). Comparison of the structures of three carboxypeptidase A-phosphonate complexes determined by X-ray crystallography. Biochemistry 30, 8171-8180.
    • (1991) Biochemistry , vol.30 , pp. 8171-8180
    • Kim, H.1    Lipscomb, W.N.2
  • 44
    • 0023121559 scopus 로고
    • Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond
    • Tronrud, D.E., Holden, H.M. & Matthews, B.W. (1987). Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond. Science 235, 571-574.
    • (1987) Science , vol.235 , pp. 571-574
    • Tronrud, D.E.1    Holden, H.M.2    Matthews, B.W.3
  • 45
    • 0026093195 scopus 로고
    • Crystal structures of alpha-lytic protease complexes with irreversibly bound phosphonate esters
    • Bone, R., Sampson, N.S., Bartlett, P.A. & Agard, D.A. (1991). Crystal structures of alpha-lytic protease complexes with irreversibly bound phosphonate esters, Biochemistry 30, 2263-2272.
    • (1991) Biochemistry , vol.30 , pp. 2263-2272
    • Bone, R.1    Sampson, N.S.2    Bartlett, P.A.3    Agard, D.A.4
  • 47
    • 0026563253 scopus 로고
    • Semisynthetic combinatorial antibody libraries: A chemical solution to the diversity problem
    • Barbas, C.F., III, Bain, J.D., Hoekstra, D.M. & Lerner, R.A. (1992). Semisynthetic combinatorial antibody libraries: a chemical solution to the diversity problem. Proc. Natl. Acad. Sci. USA 89, 4457-4461.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4457-4461
    • Barbas III, C.F.1    Bain, J.D.2    Hoekstra, D.M.3    Lerner, R.A.4
  • 48
    • 0027759586 scopus 로고
    • Selection of human anti-hapten antibodies from semisynthetic libraries
    • Barbas, C.F., III, Amberg, W., Simoncsits, A., Jones, T.M. & Lerner, R.A. (1993). Selection of human anti-hapten antibodies from semisynthetic libraries. Gene 137, 57-62.
    • (1993) Gene , vol.137 , pp. 57-62
    • Barbas III, C.F.1    Amberg, W.2    Simoncsits, A.3    Jones, T.M.4    Lerner, R.A.5
  • 49
    • 0030133645 scopus 로고    scopus 로고
    • Glubodies: Randomized libraries of glutathione transferase enzymes
    • Napolitano, E.W., et al., & Tainer, J.A. (1996). Glubodies: randomized libraries of glutathione transferase enzymes. Chemistry & Biology 3, 359-367.
    • (1996) Chemistry & Biology , vol.3 , pp. 359-367
    • Napolitano, E.W.1    Tainer, J.A.2
  • 50
    • 0028788510 scopus 로고
    • Catalytic antibodies generated via homologous and heterologous immunization
    • Tsumuraya, T., Suga, H., Meguro, S., Tsunakawa, A. & Masamune, S. (1995). Catalytic antibodies generated via homologous and heterologous immunization. J. Am. Chem. Soc. 117, 11390-11396.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11390-11396
    • Tsumuraya, T.1    Suga, H.2    Meguro, S.3    Tsunakawa, A.4    Masamune, S.5
  • 51
    • 0029590066 scopus 로고
    • Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes
    • Wagner, J., Lerner, R.A. & Barbas, C.F., III (1995). Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes. Science 270, 1797-1800.
    • (1995) Science , vol.270 , pp. 1797-1800
    • Wagner, J.1    Lerner, R.A.2    Barbas III, C.F.3
  • 52
    • 0025596912 scopus 로고
    • Peroxidase activity of an antibody-heme complex
    • Cochran, A.G. & Schultz, P.G. (1990). Peroxidase activity of an antibody-heme complex. J. Am. Chem. Soc. 112, 9414-9415.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9414-9415
    • Cochran, A.G.1    Schultz, P.G.2
  • 54
    • 0025071847 scopus 로고
    • Metalloantibodies
    • Iverson, B.L., et al., & Lerner, R.A. (1990). Metalloantibodies. Science 249, 659-662.
    • (1990) Science , vol.249 , pp. 659-662
    • Iverson, B.L.1    Lerner, R.A.2
  • 55
    • 0029018511 scopus 로고
    • Transition-state stabilization as a measure of the efficiency of antibody catalysis
    • Stewart, J.D. & Benkovic, S.J. (1995). Transition-state stabilization as a measure of the efficiency of antibody catalysis. Nature 375, 388-391.
    • (1995) Nature , vol.375 , pp. 388-391
    • Stewart, J.D.1    Benkovic, S.J.2
  • 56
    • 0025941729 scopus 로고
    • In vivo catalysis of a metabolically essential reaction by an antibody
    • Tang, Y., Hicks, J.B. & Hilvert, D. (1991). In vivo catalysis of a metabolically essential reaction by an antibody. Proc. Natl. Sci. USA 88, 8784-8786.
    • (1991) Proc. Natl. Sci. USA , vol.88 , pp. 8784-8786
    • Tang, Y.1    Hicks, J.B.2    Hilvert, D.3
  • 57
    • 0028068780 scopus 로고
    • Selection of catalytic antibodies for a biosynthetic reaction from a combinatorial cDNA library by complementation of an auxotrophic Escherichia coli: Antibodies for orotate decarboxylation
    • Smiley, J.A. & Benkovic, S.J. (1994). Selection of catalytic antibodies for a biosynthetic reaction from a combinatorial cDNA library by complementation of an auxotrophic Escherichia coli: antibodies for orotate decarboxylation. Proc. Natl. Acad. Sci. USA 91, 8319-8323.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8319-8323
    • Smiley, J.A.1    Benkovic, S.J.2
  • 58
    • 0023660979 scopus 로고
    • Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution
    • Sheriff, S., Hendrickson, W.A. & Smith, J.L (1987). Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution. J. Mol. Biol. 197, 273-296.
    • (1987) J. Mol. Biol. , vol.197 , pp. 273-296
    • Sheriff, S.1    Hendrickson, W.A.2    Smith, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.