메뉴 건너뛰기




Volumn 1, Issue , 2011, Pages 47-79

Mechanism and Catalytic Promiscuity: Emerging Mechanistic Principles for Identification and Manipulation of Catalytically Promiscuous Enzymes

Author keywords

Active site; Catalytic promiscuity; Enzyme mechanism; Protein superfamily; Rate acceleration

Indexed keywords


EID: 84884639085     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527634026.ch3     Document Type: Chapter
Times cited : (6)

References (126)
  • 1
    • 0033117461 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • O'Brien, P.J. and Herschlag, D. (1999) Catalytic promiscuity and the evolution of new enzymatic activities . Chemistry and Biology,6, R91-105 .
    • (1999) Chemistry and Biology , vol.6
    • O'Brien, P.J.1    Herschlag, D.2
  • 2
    • 10044248344 scopus 로고    scopus 로고
    • Catalytic promiscuity in biocatalysis: using old enzymes to form new bonds and follow new pathways
    • Bornscheuer, U.T., and Kazlauskas, R.J. (2004) Catalytic promiscuity in biocatalysis: using old enzymes to form new bonds and follow new pathways . Angewandte Chemie-International Edition in English,43,6032-40 .
    • (2004) Angewandte Chemie-International Edition in English , vol.43 , pp. 6032-6040
    • Bornscheuer, U.T.1    Kazlauskas, R.J.2
  • 3
    • 0037396292 scopus 로고    scopus 로고
    • Enzymes with extra talents: moonlighting functions and catalytic promiscuity
    • Copley, S.D. (2003) Enzymes with extra talents: moonlighting functions and catalytic promiscuity . Current Opinion in Chemical Biology,7,265-72 .
    • (2003) Current Opinion in Chemical Biology , vol.7 , pp. 265-272
    • Copley, S.D.1
  • 5
    • 34247131307 scopus 로고    scopus 로고
    • Enzyme promiscuity: mechanism and applications
    • Hult, K., and Berglund, P. (2007) Enzyme promiscuity: mechanism and applications . Trends in Biotechnology,25,231-8 .
    • (2007) Trends in Biotechnology , vol.25 , pp. 231-238
    • Hult, K.1    Berglund, P.2
  • 8
    • 33845864966 scopus 로고    scopus 로고
    • Robustness-epistasis link shapes the fi tness landscape of a randomly drifting protein
    • Bershtein, S., Segal, M., Bekerman, R., Tokuriki, N., and Tawfik, D.S. (2006) Robustness-epistasis link shapes the fi tness landscape of a randomly drifting protein . Nature,444,929-32 .
    • (2006) Nature , vol.444 , pp. 929-932
    • Bershtein, S.1    Segal, M.2    Bekerman, R.3    Tokuriki, N.4    Tawfik, D.S.5
  • 9
    • 24344494387 scopus 로고    scopus 로고
    • Evolutionary potential of (beta/ alpha)8-barrels: in vitro enhancement of a ' new'reaction in the enolase superfamily
    • Vick, J.E., Schmidt, D.M., and Gerlt, J.A. (2005) Evolutionary potential of (beta/ alpha)8-barrels: in vitro enhancement of a ' new'reaction in the enolase superfamily . Biochemistry,44,11722-9 .
    • (2005) Biochemistry , vol.44 , pp. 11722-1179
    • Vick, J.E.1    Schmidt, D.M.2    Gerlt, J.A.3
  • 10
    • 25444456889 scopus 로고    scopus 로고
    • Shared promiscuous activities and evolutionary features in various members of the amidohydrolase superfamily
    • Roodveldt, C., and Tawfik, D.S. (2005) Shared promiscuous activities and evolutionary features in various members of the amidohydrolase superfamily . Biochemistry,44,12728-36 .
    • (2005) Biochemistry , vol.44 , pp. 12728-12736
    • Roodveldt, C.1    Tawfik, D.S.2
  • 12
    • 4644358158 scopus 로고    scopus 로고
    • Evolution of enzymatic activity in the tautomerase superfamily: mechanistic and structural studies of the 1,3-dichloropropene catabolic enzymes
    • Poelarends, G.J., and Whitman, C.P. (2004) Evolution of enzymatic activity in the tautomerase superfamily: mechanistic and structural studies of the 1,3-dichloropropene catabolic enzymes . Bioorganic Chemistry,32,376-92 .
    • (2004) Bioorganic Chemistry , vol.32 , pp. 376-392
    • Poelarends, G.J.1    Whitman, C.P.2
  • 13
    • 16844379112 scopus 로고    scopus 로고
    • Directed evolution of the promiscuous esterase activity of carbonic anhydrase II
    • Gould, S.M., and Tawfik, D.S. (2005) Directed evolution of the promiscuous esterase activity of carbonic anhydrase II . Biochemistry,44,5444-52 .
    • (2005) Biochemistry , vol.44 , pp. 5444-5452
    • Gould, S.M.1    Tawfik, D.S.2
  • 15
    • 0347362473 scopus 로고    scopus 로고
    • Escherichia coli mutators present an enhanced risk for emergence of antibiotic resistance during urinary tract infections
    • Miller, K., O'Neill, A.J., and Chopra, I. (2004) Escherichia coli mutators present an enhanced risk for emergence of antibiotic resistance during urinary tract infections . Antimicrobial Agents and Chemotherapy,48,23-9 .
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , pp. 23-29
    • Miller, K.1    O'Neill, A.J.2    Chopra, I.3
  • 16
    • 0034674175 scopus 로고    scopus 로고
    • Estimating the number of protein folds and families from complete genome data
    • Wolf, Y.I., Grishin, N.V., and Koonin, E.V. (2000) Estimating the number of protein folds and families from complete genome data . Journal of Molecular Biology,299,897-905 .
    • (2000) Journal of Molecular Biology , vol.299 , pp. 897-905
    • Wolf, Y.I.1    Grishin, N.V.2    Koonin, E.V.3
  • 17
    • 0035896377 scopus 로고    scopus 로고
    • The TIM-barrel fold: a versatile framework for effi cient enzymes
    • Wierenga, R.K. (2001) The TIM-barrel fold: a versatile framework for effi cient enzymes . FEBS Letters,492,193-8 .
    • (2001) FEBS Letters , vol.492 , pp. 193-18
    • Wierenga, R.K.1
  • 18
    • 4143074011 scopus 로고    scopus 로고
    • Estimating the prevalence of protein sequences adopting functional enzyme folds
    • Axe, D.D. (2004) Estimating the prevalence of protein sequences adopting functional enzyme folds . Journal of Molecular Biology,341,1295-315 .
    • (2004) Journal of Molecular Biology , vol.341 , pp. 1295-1315
    • Axe, D.D.1
  • 20
    • 0028961335 scopus 로고
    • SCOP: a structural classifi cation of proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T., and Chothia, C. (1995) SCOP: a structural classifi cation of proteins database for the investigation of sequences and structures . Journal of Molecular Biology,247,536-40 .
    • (1995) Journal of Molecular Biology , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 25
    • 0034058625 scopus 로고    scopus 로고
    • The CATH Dictionary of Homologous Superfamilies (DHS): a consensus approach for identifying distant structural homologues
    • Bray, J.E., Todd, A.E., Pearl, F.M., Thornton, J.M., and Orengo, C.A. (2000) The CATH Dictionary of Homologous Superfamilies (DHS): a consensus approach for identifying distant structural homologues . Protein Engineering,13,153-65 .
    • (2000) Protein Engineering , vol.13 , pp. 153-165
    • Bray, J.E.1    Todd, A.E.2    Pearl, F.M.3    Thornton, J.M.4    Orengo, C.A.5
  • 26
    • 13444272079 scopus 로고    scopus 로고
    • The CATH Domain Structure Database and related resources Gene3D and DHS provide comprehensive domain family information for genome analysis
    • Pearl, F., Todd, A., Sillitoe, I., Dibley, M., Redfern, O., Lewis, T., Bennett, C., Marsden, R., Grant, A., Lee, D. et al . (2005) The CATH Domain Structure Database and related resources Gene3D and DHS provide comprehensive domain family information for genome analysis . Nucleic Acids Research,33, D247-51 .
    • (2005) Nucleic Acids Research , vol.33
    • Pearl, F.1    Todd, A.2    Sillitoe, I.3    Dibley, M.4    Redfern, O.5    Lewis, T.6    Bennett, C.7    Marsden, R.8    Grant, A.9    Lee, D.10
  • 27
    • 0036087169 scopus 로고    scopus 로고
    • SUPERFAMILY: HMMs representing all proteins of known structure. SCOP sequence searches. alignments and genome assignments
    • Gough, J., and Chothia, C. (2002) SUPERFAMILY: HMMs representing all proteins of known structure. SCOP sequence searches, alignments and genome assignments . Nucleic Acids Research,30,268-72 .
    • (2002) Nucleic Acids Research , vol.30 , pp. 268-272
    • Gough, J.1    Chothia, C.2
  • 30
    • 33747517236 scopus 로고    scopus 로고
    • Structural and functional comparisons of nucleotide pyrophosphatase/phosphodiesterase and alkaline phosphatase: implications formechanism and evolution
    • Zalatan, J.G., Fenn, T.D., Brunger, A.T., and Herschlag, D. (2006) Structural and functional comparisons of nucleotide pyrophosphatase/phosphodiesterase and alkaline phosphatase: implications formechanism and evolution . Biochemistry,45,9788-803 .
    • (2006) Biochemistry , vol.45 , pp. 9788-9803
    • Zalatan, J.G.1    Fenn, T.D.2    Brunger, A.T.3    Herschlag, D.4
  • 31
    • 0032477286 scopus 로고    scopus 로고
    • Sulphatase activity of E. coli alkaline phosphatase demonstrates a functional link to arylsulfatases. an evolutionary related enzyme family
    • O'Brien, P.J., and Herschlag, D. (1998) Sulphatase activity of E. coli alkaline phosphatase demonstrates a functional link to arylsulfatases, an evolutionary related enzyme family . Journal of the American Chemical Society,120,12369-70 .
    • (1998) Journal of the American Chemical Society , vol.120 , pp. 12369-12370
    • O'Brien, P.J.1    Herschlag, D.2
  • 32
    • 0344012191 scopus 로고    scopus 로고
    • The 4-oxalocrotonate tautomerase-and YwhB-catalyzed hydration of 3E-haloacrylates: implications for the evolution of new enzymatic activities
    • Wang, S.C., Johnson, W.H. Jr and Whitman, C.P. (2003) The 4-oxalocrotonate tautomerase-and YwhB-catalyzed hydration of 3E-haloacrylates: implications for the evolution of new enzymatic activities . Journal of the American Chemical Society,125,14282-3 .
    • (2003) Journal of the American Chemical Society , vol.125 , pp. 14282-14283
    • Wang, S.C.1    Johnson Jr., W.H.2    Whitman, C.P.3
  • 33
    • 0032461412 scopus 로고    scopus 로고
    • A superfamily of metalloenzymes unifi es phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases
    • Galperin, M.Y., Bairoch, A., and Koonin, E.V. (1998) A superfamily of metalloenzymes unifi es phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases . Protein Engineering,7,1829-35 .
    • (1998) Protein Engineering , vol.7 , pp. 1829-1835
    • Galperin, M.Y.1    Bairoch, A.2    Koonin, E.V.3
  • 34
    • 17844384785 scopus 로고    scopus 로고
    • Structural and catalytic diversity within the amidohydrolase superfamily
    • Seibert, C.M., and Raushel, F.M. (2005) Structural and catalytic diversity within the amidohydrolase superfamily . Biochemistry,44,6383-91 .
    • (2005) Biochemistry , vol.44 , pp. 6383-63891
    • Seibert, C.M.1    Raushel, F.M.2
  • 38
    • 0034923923 scopus 로고    scopus 로고
    • Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies
    • Gerlt, J.A., and Babbitt, P.C. (2001) Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies . Annual Review of Biochemistry,70,209-46 .
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 209-246
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 39
    • 0017272554 scopus 로고
    • Enzyme recruitment in evolution of new function
    • Jensen, R.A. (1976) Enzyme recruitment in evolution of new function . Annual Review of Biochemistry,30,409-25 .
    • (1976) Annual Review of Biochemistry , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 40
    • 0141483333 scopus 로고    scopus 로고
    • Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase
    • Lamble, H.J., Heyer, N.I., Bull, S.D., Hough, D.W., and Danson, M.J. (2003) Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase . The Journal of Biological Chemistry,278,34066-72 .
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 34066-34072
    • Lamble, H.J.1    Heyer, N.I.2    Bull, S.D.3    Hough, D.W.4    Danson, M.J.5
  • 42
    • 28844468051 scopus 로고    scopus 로고
    • Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the archaeon Sulfolobus solfataricus
    • Lamble, H.J., Theodossis, A., Milburn, C.C., Taylor, G.L., Bull, S.D., Hough, D. W., and Danson, M.J. (2005) Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the archaeon Sulfolobus solfataricus . FEBS Letters,579,6865-9 .
    • (2005) FEBS Letters , vol.579 , pp. 6865-6869
    • Lamble, H.J.1    Theodossis, A.2    Milburn, C.C.3    Taylor, G.L.4    Bull, S.D.5    Hough, D.W.6    Danson, M.J.7
  • 43
    • 33745006617 scopus 로고    scopus 로고
    • The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus
    • Milburn, C.C., Lamble, H.J., Theodossis, A., Bull, S.D., Hough, D.W., Danson, M. J., and Taylor, G.L. (2006) The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus . The Journal of Biological Chemistry,281,14796-804 .
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 14796-14804
    • Milburn, C.C.1    Lamble, H.J.2    Theodossis, A.3    Bull, S.D.4    Hough, D.W.5    Danson, M.J.6    Taylor, G.L.7
  • 44
    • 0035846958 scopus 로고    scopus 로고
    • In vitro evolution of beta-glucuronidase into a beta-galactosidase proceeds through non-specifi c intermediates
    • Matsumura, I., and Ellington, A.D. (2001) In vitro evolution of beta-glucuronidase into a beta-galactosidase proceeds through non-specifi c intermediates . The Journal of Biological Chemistry,305,331-9 .
    • (2001) The Journal of Biological Chemistry , vol.305 , pp. 331-339
    • Matsumura, I.1    Ellington, A.D.2
  • 45
    • 21644470988 scopus 로고    scopus 로고
    • Alkaline phosphatase catalysis is ultrasensitive to charge sequestered between the active site zinc ions
    • Nikolic-Hughes, I., O'Brien, P.J., and Herschlag, D. (2005) Alkaline phosphatase catalysis is ultrasensitive to charge sequestered between the active site zinc ions . Journal of the American Chemical Society,127,9314-15 .
    • (2005) Journal of the American Chemical Society , vol.127 , pp. 9314-9315
    • Nikolic-Hughes, I.1    O'Brien, P.J.2    Herschlag, D.3
  • 46
    • 0041846667 scopus 로고    scopus 로고
    • Reactions of trans-3-chloroacrylic acid dehalogenase with acetylene substrates: consequences of and evidence for a hydration reaction
    • Wang, S.C., Person, M.D., Johnson, W.H., and Whitman, C.P. (2003) Reactions of trans-3-chloroacrylic acid dehalogenase with acetylene substrates: consequences of and evidence for a hydration reaction . Biochemistry,42,8762-73 .
    • (2003) Biochemistry , vol.42 , pp. 8762-8773
    • Wang, S.C.1    Person, M.D.2    Johnson, W.H.3    Whitman, C.P.4
  • 47
    • 25444445359 scopus 로고    scopus 로고
    • Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from combinatorial mutagenesis and selection
    • Kunzler, D.E., Sasso, S., Gamper, M., Hilvert, D., and Kast, P. (2005)Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from combinatorial mutagenesis and selection . The Journal of Biological Chemistry,280,32827-34 .
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 32827-32834
    • Kunzler, D.E.1    Sasso, S.2    Gamper, M.3    Hilvert, D.4    Kast, P.5
  • 48
    • 0035543093 scopus 로고    scopus 로고
    • The depth of chemical time and the power of enzymes as catalysts
    • Wolfenden, R., and Snider, M.J. (2001) The depth of chemical time and the power of enzymes as catalysts . Accounts of Chemical Research,34,938-45 .
    • (2001) Accounts of Chemical Research , vol.34 , pp. 938-945
    • Wolfenden, R.1    Snider, M.J.2
  • 49
    • 0038286174 scopus 로고    scopus 로고
    • The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic profi ciencies of protein and inositol phosphatases
    • Lad, C., Williams, N.H., and Wolfenden, R. (2003) The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic profi ciencies of protein and inositol phosphatases . Proceedings of the National Academy of Sciences of the United States of America,10,5607-10 .
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.10 , pp. 5607-5610
    • Lad, C.1    Williams, N.H.2    Wolfenden, R.3
  • 50
    • 0028918401 scopus 로고
    • A profi cient enzyme
    • Radzicka, A., and Wolfenden, R. (1995) A profi cient enzyme . Science,267,90-3 .
    • (1995) Science , vol.267 , pp. 90-93
    • Radzicka, A.1    Wolfenden, R.2
  • 51
    • 33748592810 scopus 로고    scopus 로고
    • Degrees of diffi culty of water-consuming reactions in the absence of enzymes
    • Wolfenden, R. (2006) Degrees of diffi culty of water-consuming reactions in the absence of enzymes . Chemical Reviews,106,3379-96 .
    • (2006) Chemical Reviews , vol.106 , pp. 3379-3396
    • Wolfenden, R.1
  • 52
    • 33845283317 scopus 로고
    • Origin of rate accelerations in an enzyme model-the para-nitrophenyl ester syndrome
    • Menger, F.M., and Ladika, M. (1987) Origin of rate accelerations in an enzyme model-the para-nitrophenyl ester syndrome . Journal of the American Chemical Society,109,3145-6 .
    • (1987) Journal of the American Chemical Society , vol.109 , pp. 3145-3146
    • Menger, F.M.1    Ladika, M.2
  • 54
    • 0032839614 scopus 로고    scopus 로고
    • Structure and nuclease activity of simple dinuclear metal complexes: quantitative dissection of the role of metal ions
    • Williams, N.H., Takasaki, B., Wall, M., and Chin, J. (1999) Structure and nuclease activity of simple dinuclear metal complexes: quantitative dissection of the role of metal ions . Accounts of Chemical Research,32,485-93 .
    • (1999) Accounts of Chemical Research , vol.32 , pp. 485-493
    • Williams, N.H.1    Takasaki, B.2    Wall, M.3    Chin, J.4
  • 55
    • 0032882552 scopus 로고    scopus 로고
    • Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes
    • Christianson, D.W., and Cox, J.D. (1999) Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes . Annual Review of Biochemistry,68,33-57 .
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 33-57
    • Christianson, D.W.1    Cox, J.D.2
  • 56
    • 0032760684 scopus 로고    scopus 로고
    • The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site-specifi c mutagenesis
    • Holtz, K.M., and Kantrowitz, E.R. (1999) The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site-specifi c mutagenesis . FEBS Letters,462,7-11 .
    • (1999) FEBS Letters , vol.462 , pp. 7-11
    • Holtz, K.M.1    Kantrowitz, E.R.2
  • 57
    • 0034705337 scopus 로고    scopus 로고
    • A revised mechanism for the alkaline phosphatase reaction involving three metal ions
    • Stec, B., Holtz, K.M., and Kantrowitz, E.R. (2000) A revised mechanism for the alkaline phosphatase reaction involving three metal ions . Journal of Molecular Biology,299,1303-11 .
    • (2000) Journal of Molecular Biology , vol.299 , pp. 1303-1311
    • Stec, B.1    Holtz, K.M.2    Kantrowitz, E.R.3
  • 59
    • 0033605749 scopus 로고    scopus 로고
    • A model of the transition state in the alkaline phosphatase reaction
    • Holtz, K.M., Stec, B., and Kantrowitz, E.R. (1999) A model of the transition state in the alkaline phosphatase reaction . The Journal of Biological Chemistry,274,8351-4 .
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 8351-8354
    • Holtz, K.M.1    Stec, B.2    Kantrowitz, E.R.3
  • 60
    • 0034401916 scopus 로고    scopus 로고
    • Dinuclear metallo-phosphodiesterase models: application of calix[4]arenes as molecular scaffolds
    • Molenveld, P., Engbersen, J.F.J., and Reinhoudt, D.N. (2000) Dinuclear metallo-phosphodiesterase models: application of calix[4]arenes as molecular scaffolds . Chemical Society Reviews,29,75-86 .
    • (2000) Chemical Society Reviews , vol.29 , pp. 75-86
    • Molenveld, P.1    Engbersen, J.F.J.2    Reinhoudt, D.N.3
  • 62
    • 33846563482 scopus 로고    scopus 로고
    • Catalytic promiscuity in biomimetic systems: catecholase-like activity, phosphatase-like activity, and hydrolytic DNA cleavage promoted by a new dicopper(II) hydroxo-bridged complex
    • Rey, N.A., Neves, A., Bortoluzzi, A.J., Pich, C.T., and Terenzi, H. (2007) Catalytic promiscuity in biomimetic systems: catecholase-like activity, phosphatase-like activity, and hydrolytic DNA cleavage promoted by a new dicopper(II) hydroxo-bridged complex . Inorganic Chemistry,46,348-50 .
    • (2007) Inorganic Chemistry , vol.46 , pp. 348-350
    • Rey, N.A.1    Neves, A.2    Bortoluzzi, A.J.3    Pich, C.T.4    Terenzi, H.5
  • 63
    • 31944441501 scopus 로고    scopus 로고
    • Alkaline phosphatase mono-and diesterase reactions: comparative transition state analysis
    • Zalatan, J.G., and Herschlag, D. (2006) Alkaline phosphatase mono-and diesterase reactions: comparative transition state analysis . Journal of the American Chemical Society,128,1293-303 .
    • (2006) Journal of the American Chemical Society , vol.128 , pp. 1293-1303
    • Zalatan, J.G.1    Herschlag, D.2
  • 64
    • 0035873714 scopus 로고    scopus 로고
    • Functional interrelationships in the alkaline phosphatase superfamily: phosphodiesterase activity of Escherichia coli alkaline phosphatase
    • O'Brien, P.J., and Herschlag, D. (2001) Functional interrelationships in the alkaline phosphatase superfamily: phosphodiesterase activity of Escherichia coli alkaline phosphatase . Biochemistry,40,5691-9 .
    • (2001) Biochemistry , vol.40 , pp. 5691-5699
    • O'Brien, P.J.1    Herschlag, D.2
  • 66
    • 2542529286 scopus 로고    scopus 로고
    • A new activity for an old enzyme: Escherichia coli bacterial alkaline phosphatase is a phosphite-dependent hydrogenase
    • Yang, K., and Metcalf, W.W. (2004) A new activity for an old enzyme: Escherichia coli bacterial alkaline phosphatase is a phosphite-dependent hydrogenase . Proceedings of the National Academy of Sciences of the United States of America,101,7919-24 .
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , pp. 7919-7924
    • Yang, K.1    Metcalf, W.W.2
  • 68
    • 33748591572 scopus 로고    scopus 로고
    • Enzymatic mechanisms of phosphate and sulfate transfer
    • Cleland, W.W., and Hengge, A.C. (2006) Enzymatic mechanisms of phosphate and sulfate transfer . Chemical Reviews,106,3252-78 .
    • (2006) Chemical Reviews , vol.106 , pp. 3252-3278
    • Cleland, W.W.1    Hengge, A.C.2
  • 69
    • 0032547320 scopus 로고    scopus 로고
    • Reactivity of phosphate diesters doubly coordinated to a dinuclear cobalt(III) complex: Dependence of the reactivity on the basicity of the leaving group
    • Williams, N.H., Cheung, W., and Chin, J. (1998) Reactivity of phosphate diesters doubly coordinated to a dinuclear cobalt(III) complex: Dependence of the reactivity on the basicity of the leaving group . Journal of the American Chemical Society,120,8079-87 .
    • (1998) Journal of the American Chemical Society , vol.120 , pp. 8079-8087
    • Williams, N.H.1    Cheung, W.2    Chin, J.3
  • 71
    • 33644633050 scopus 로고    scopus 로고
    • Catalytic promiscuity and the divergent evolution of DNA repair enzymes
    • O'Brien, P.J. (2006) Catalytic promiscuity and the divergent evolution of DNA repair enzymes . Chemical Reviews,106,720-52 .
    • (2006) Chemical Reviews , vol.106 , pp. 720-752
    • O'Brien, P.J.1
  • 72
    • 0343319790 scopus 로고
    • Exonuclease III and endonuclease IV remove 3 ' blocks from DNA synthesis primers in H 2 O 2-damaged Escherichia coli
    • Demple, B., Johnson, A., and Fung, D. (1986) Exonuclease III and endonuclease IV remove 3 ' blocks from DNA synthesis primers in H 2 O 2-damaged Escherichia coli . Proceedings of the National Academy of Sciences,83,7731-5 .
    • (1986) Proceedings of the National Academy of Sciences , vol.83 , pp. 7731-7735
    • Demple, B.1    Johnson, A.2    Fung, D.3
  • 75
    • 17644367506 scopus 로고    scopus 로고
    • Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase
    • Khersonsky, O., and Tawfik, D.S. (2005) Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase . Biochemistry,44,6371-82 .
    • (2005) Biochemistry , vol.44 , pp. 6371-6382
    • Khersonsky, O.1    Tawfik, D.S.2
  • 76
    • 0000326477 scopus 로고
    • Kinetic evidence for the formation of acyl-enzyme intermediates in the alpha-chymotrypsin-catalyzed hydrolyses of specifi c substrates
    • Zerner, B., Bond, R.P.M., and Bender, M.L. (1964) Kinetic evidence for the formation of acyl-enzyme intermediates in the alpha-chymotrypsin-catalyzed hydrolyses of specifi c substrates . Journal of the American Chemical Society,86,3674-9 .
    • (1964) Journal of the American Chemical Society , vol.86 , pp. 3674-3679
    • Zerner, B.1    Bond, R.P.M.2    Bender, M.L.3
  • 78
    • 2342449187 scopus 로고    scopus 로고
    • Arginine deiminase uses an active-site cysteine in nucleophilic catalysis of L-arginine hydrolysis
    • Lu, X., Galkin, A., Herzberg, O., and Dunaway-Mariano, D. (2004) Arginine deiminase uses an active-site cysteine in nucleophilic catalysis of L-arginine hydrolysis . Journal of the American Chemical Society,126,5374-5 .
    • (2004) Journal of the American Chemical Society , vol.126 , pp. 5374-5375
    • Lu, X.1    Galkin, A.2    Herzberg, O.3    Dunaway-Mariano, D.4
  • 79
    • 31544455800 scopus 로고    scopus 로고
    • Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides insight into structural determinants of function
    • Lu, X., Li, L., Wu, R., Feng, X., Li, Z., Yang, H., Wang, C., Guo, H., Galkin, A., Herzberg, O. et al . (2006) Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides insight into structural determinants of function . Biochemistry,45,1162-72 .
    • (2006) Biochemistry , vol.45 , pp. 1162-1172
    • Lu, X.1    Li, L.2    Wu, R.3    Feng, X.4    Li, Z.5    Yang, H.6    Wang, C.7    Guo, H.8    Galkin, A.9    Herzberg, O.10
  • 82
    • 28844466075 scopus 로고    scopus 로고
    • High-throughput screening of enzyme libraries: thiolactonases evolved by fl uorescence-activated sorting of single cells in emulsion compartments
    • Aharoni, A., Amitai, G., Bernath, K., Magdassi, S., and Tawfik, D.S. (2005) High-throughput screening of enzyme libraries: thiolactonases evolved by fl uorescence-activated sorting of single cells in emulsion compartments . Chemistry and Biology,12,1281-9 .
    • (2005) Chemistry and Biology , vol.12 , pp. 1281-1289
    • Aharoni, A.1    Amitai, G.2    Bernath, K.3    Magdassi, S.4    Tawfik, D.S.5
  • 85
    • 0030009782 scopus 로고    scopus 로고
    • A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution
    • Larsen, T.M., Wedekind, J.E., Rayment, I., and Reed, G.H. (1996) A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution . Biochemistry,35,4349-58 .
    • (1996) Biochemistry , vol.35 , pp. 4349-4358
    • Larsen, T.M.1    Wedekind, J.E.2    Rayment, I.3    Reed, G.H.4
  • 87
    • 0029200309 scopus 로고
    • The refi ned x-ray structure of muconate lactonizing enzyme from Pseudomonas putida prs2000 at 1.85 A resolution
    • Helin, S., Kahn, P.C., Guha, B.L., Mallows, D.G., and Goldman, A. (1995) The refi ned x-ray structure of muconate lactonizing enzyme from Pseudomonas putida prs2000 at 1.85 A resolution . Journal of Molecular Biology,254,918-41 .
    • (1995) Journal of Molecular Biology , vol.254 , pp. 918-941
    • Helin, S.1    Kahn, P.C.2    Guha, B.L.3    Mallows, D.G.4    Goldman, A.5
  • 88
    • 0034609515 scopus 로고    scopus 로고
    • Evolution of enzymatic activity in the enolase superfamily: structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg2+ and o-succinylbenzoate
    • Thompson, T.B., Garrett, J.B., Taylor, E.A., Meganathan, R., Gerlt, J.A., and Rayment, I. (2000) Evolution of enzymatic activity in the enolase superfamily: structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg2+ and o-succinylbenzoate . Biochemistry,39,10662-76 .
    • (2000) Biochemistry , vol.39 , pp. 10662-1076
    • Thompson, T.B.1    Garrett, J.B.2    Taylor, E.A.3    Meganathan, R.4    Gerlt, J.A.5    Rayment, I.6
  • 89
    • 0035951075 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the enolase superfamily: crystal structures of the L-ALA-D/L-Glu epimerases from Escherichia coli and Bacillus subtilis
    • Gulick, A.M., Schmidt, D.M.Z., Gerlt, J.A., and Rayment, I. (2001) Evolution of enzymatic activities in the enolase superfamily: crystal structures of the L-ALA-D/L-Glu epimerases from Escherichia coli and Bacillus subtilis . Biochemistry,40,15716-24 .
    • (2001) Biochemistry , vol.40 , pp. 15716-15724
    • Gulick, A.M.1    Schmidt, D.M.Z.2    Gerlt, J.A.3    Rayment, I.4
  • 90
    • 0033528659 scopus 로고    scopus 로고
    • Unexpected divergence of enzyme function and sequence:'N-acylamino acid racemase'is o-succinylbenzoate synthase
    • Palmer, D.R., Garrett, J.B., Sharma, V., Meganathan, R., Babbitt, P.C., and Gerlt, J.A. (1999) Unexpected divergence of enzyme function and sequence:'N-acylamino acid racemase'is o-succinylbenzoate synthase . Biochemistry,38,4252-8 .
    • (1999) Biochemistry , vol.38 , pp. 4252-4258
    • Palmer, D.R.1    Garrett, J.B.2    Sharma, V.3    Meganathan, R.4    Babbitt, P.C.5    Gerlt, J.A.6
  • 91
    • 13544274134 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the orotidine 5 '-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase
    • Wise, E.L., Yew, W.S., Akana, J., Gerlt, J.A., and Rayment, I. (2005) Evolution of enzymatic activities in the orotidine 5 '-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase . Biochemistry,44,1816-23 .
    • (2005) Biochemistry , vol.44 , pp. 1816-1823
    • Wise, E.L.1    Yew, W.S.2    Akana, J.3    Gerlt, J.A.4    Rayment, I.5
  • 92
    • 13544277381 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the orotidine 5 '-monophosphate decarboxylase suprafamily: enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase
    • Yew, W.S., Akana, J., Wise, E.L., Rayment, I., and Gerlt, J.A. (2005) Evolution of enzymatic activities in the orotidine 5 '-monophosphate decarboxylase suprafamily: enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase . Biochemistry,44,1807-15 .
    • (2005) Biochemistry , vol.44 , pp. 1807-1815
    • Yew, W.S.1    Akana, J.2    Wise, E.L.3    Rayment, I.4    Gerlt, J.A.5
  • 93
    • 0033564943 scopus 로고    scopus 로고
    • Interchange of catalytic activity within the 2-enoyl-coenzyme A hydratase/isomerase superfamily based on a common active site template
    • Xiang, H., Luo, L., Taylor, K.L., and Dunaway-Mariano, D. (1999) Interchange of catalytic activity within the 2-enoyl-coenzyme A hydratase/isomerase superfamily based on a common active site template . Biochemistry,38,7638-52 .
    • (1999) Biochemistry , vol.38 , pp. 7638-7652
    • Xiang, H.1    Luo, L.2    Taylor, K.L.3    Dunaway-Mariano, D.4
  • 94
    • 33645677238 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway for the irreversible conversion of D-to L-amino acids
    • Sakai, A., Xiang, D.F., Xu, C., Song, L., Yew, W.S., Raushel, F.M., and Gerlt, J.A. (2006) Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway for the irreversible conversion of D-to L-amino acids . Biochemistry,45,4455-62 .
    • (2006) Biochemistry , vol.45 , pp. 4455-4462
    • Sakai, A.1    Xiang, D.F.2    Xu, C.3    Song, L.4    Yew, W.S.5    Raushel, F.M.6    Gerlt, J.A.7
  • 95
    • 33845401627 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris
    • Yew, W.S., Fedorov, A.A., Fedorov, E.V., Rakus, J.F., Pierce, R.W., Almo, S.C., and Gerlt, J.A. (2006) Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris . Biochemistry,45,14582-97 .
    • (2006) Biochemistry , vol.45 , pp. 14582-14597
    • Yew, W.S.1    Fedorov, A.A.2    Fedorov, E.V.3    Rakus, J.F.4    Pierce, R.W.5    Almo, S.C.6    Gerlt, J.A.7
  • 96
    • 33845398832 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the enolase superfamily: D-tartrate dehydratase from Bradyrhizobium japonicum
    • Yew, W.S., Fedorov, A.A., Fedorov, E.V., Wood, B.M., Almo, S.C., and Gerlt, J.A. (2006) Evolution of enzymatic activities in the enolase superfamily: D-tartrate dehydratase from Bradyrhizobium japonicum . Biochemistry,45,14598-608 .
    • (2006) Biochemistry , vol.45 , pp. 14598-14608
    • Yew, W.S.1    Fedorov, A.A.2    Fedorov, E.V.3    Wood, B.M.4    Almo, S.C.5    Gerlt, J.A.6
  • 97
    • 2442612271 scopus 로고    scopus 로고
    • Evolution of enzymatic activity in the enolase superfamily: structural studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis
    • Thoden, J.B., Taylor Ringia, E.A., Garrett, J.B., Gerlt, J.A., Holden, H.M., and Rayment, I. (2004) Evolution of enzymatic activity in the enolase superfamily: structural studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis . Biochemistry,43,5716-27 .
    • (2004) Biochemistry , vol.43 , pp. 5716-5727
    • Thoden, J.B.1    Taylor Ringia, E.A.2    Garrett, J.B.3    Gerlt, J.A.4    Holden, H.M.5    Rayment, I.6
  • 98
    • 0035843184 scopus 로고    scopus 로고
    • Modular enzymes
    • Khosla, C., and Harbury, P. (2001) Modular enzymes . Nature,409,247-52 .
    • (2001) Nature , vol.409 , pp. 247-252
    • Khosla, C.1    Harbury, P.2
  • 101
    • 0030050491 scopus 로고    scopus 로고
    • 4-Oxalocrotonate tautomerase: pH dependence of catalysis and pKa values of active site residues
    • Stivers, J.T., Abeygunawardana, C., Mildvan, A.S., Hajipour, G., and Whitman, C.P. (1996) 4-Oxalocrotonate tautomerase: pH dependence of catalysis and pKa values of active site residues . Biochemistry,35,814-23 .
    • (1996) Biochemistry , vol.35 , pp. 814-823
    • Stivers, J.T.1    Abeygunawardana, C.2    Mildvan, A.S.3    Hajipour, G.4    Whitman, C.P.5
  • 102
    • 1842531456 scopus 로고    scopus 로고
    • The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: a kinetic, NMR, and mutational analysis
    • Azurmendi, H.F., Wang, S.C., Massiah, M.A., Poelarends, G.J., Whitman, C.P., and Mildvan, A.S. (2004) The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: a kinetic, NMR, and mutational analysis . Biochemistry,43,4082-91 .
    • (2004) Biochemistry , vol.43 , pp. 4082-4091
    • Azurmendi, H.F.1    Wang, S.C.2    Massiah, M.A.3    Poelarends, G.J.4    Whitman, C.P.5    Mildvan, A.S.6
  • 103
    • 33746914768 scopus 로고    scopus 로고
    • Evolution of enzymatic activity in the tautomerase superfamily: mechanistic and structural consequences of the L8R mutation in 4-oxalocrotonate tautomerase
    • Poelarends, G.J., Almrud, J.J., Serrano, H., Darty, J.E., Johnson, W.H. Jr, Hackert, M.L., and Whitman, C.P. (2006) Evolution of enzymatic activity in the tautomerase superfamily: mechanistic and structural consequences of the L8R mutation in 4-oxalocrotonate tautomerase . Biochemistry,45,7700-8 .
    • (2006) Biochemistry , vol.45 , pp. 7700-7708
    • Poelarends, G.J.1    Almrud, J.J.2    Serrano, H.3    Darty, J.E.4    Johnson Jr., W.H.5    Hackert, M.L.6    Whitman, C.P.7
  • 104
    • 33748601470 scopus 로고    scopus 로고
    • Structural biology and chemistry of the terpenoid cyclases
    • Christianson, D.W. (2006) Structural biology and chemistry of the terpenoid cyclases . Chemical Reviews,106,3412-42 .
    • (2006) Chemical Reviews , vol.106 , pp. 3412-3442
    • Christianson, D.W.1
  • 105
    • 0031891866 scopus 로고    scopus 로고
    • Sesquiterpene synthases from grand fi r (Abies grandis). Comparison of constitutive and wound-induced activities, and cDNA isolation, characterization, and bacterial expression of delta-selinene synthase and gamma-humulene synthase
    • Steele, C.L., Crock, J., Bohlmann, J., and Croteau, R. (1998) Sesquiterpene synthases from grand fi r (Abies grandis). Comparison of constitutive and wound-induced activities, and cDNA isolation, characterization, and bacterial expression of delta-selinene synthase and gamma-humulene synthase . The Journal of Biological Chemistry,273,2078-89 .
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 2078-2089
    • Steele, C.L.1    Crock, J.2    Bohlmann, J.3    Croteau, R.4
  • 107
    • 33646178621 scopus 로고    scopus 로고
    • Designed divergent evolution of enzyme function
    • Yoshikuni, Y., Ferrin, T.E., and Keasling, J.D. (2006) Designed divergent evolution of enzyme function . Nature,440,1078-82 .
    • (2006) Nature , vol.440 , pp. 1078-1082
    • Yoshikuni, Y.1    Ferrin, T.E.2    Keasling, J.D.3
  • 109
    • 34147178365 scopus 로고    scopus 로고
    • Chimeras of two isoprenoid synthases catalyze all four coupling reactions in isoprenoid biosynthesis
    • Thulasiram, H.V., Erickson, H.K., and Poulter, C.D. (2007) Chimeras of two isoprenoid synthases catalyze all four coupling reactions in isoprenoid biosynthesis . Science,316,73-6 .
    • (2007) Science , vol.316 , pp. 73-76
    • Thulasiram, H.V.1    Erickson, H.K.2    Poulter, C.D.3
  • 110
    • 0032538627 scopus 로고    scopus 로고
    • Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites
    • Warshel, A. (1998) Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites . The Journal of Biological Chemistry,42,27035-8 .
    • (1998) The Journal of Biological Chemistry , vol.42 , pp. 27035-2708
    • Warshel, A.1
  • 112
    • 0000176677 scopus 로고
    • Acceleration of P-O cleavage reactions of phosphate monoester dianions in dipolar aprotic solvents
    • Abell, K.W.Y., and Kirby, A.J. (1986) Acceleration of P-O cleavage reactions of phosphate monoester dianions in dipolar aprotic solvents . Tetrahedron Letters,27,1085 .
    • (1986) Tetrahedron Letters , vol.27 , pp. 1085
    • Abell, K.W.Y.1    Kirby, A.J.2
  • 113
    • 33749003453 scopus 로고    scopus 로고
    • Thermodynamic origin of the increased rate of hydrolysis of phosphate and phosphorothioate esters in DMSO/ water mixtures
    • Sorensen-Stowell, K., and Hengge, A.C. (2006) Thermodynamic origin of the increased rate of hydrolysis of phosphate and phosphorothioate esters in DMSO/ water mixtures . The Journal of Organic Chemistry,71,7180-4 .
    • (2006) The Journal of Organic Chemistry , vol.71 , pp. 7180-7184
    • Sorensen-Stowell, K.1    Hengge, A.C.2
  • 115
    • 0035943306 scopus 로고    scopus 로고
    • On the magnitude and specifi city of medium effects in enzyme-like catalysts for proton transfer
    • Hollfelder, F., Kirby, A.J., and Tawfik, D.S. (2001) On the magnitude and specifi city of medium effects in enzyme-like catalysts for proton transfer . The Journal of Organic Chemistry,66,5866-74 .
    • (2001) The Journal of Organic Chemistry , vol.66 , pp. 5866-5874
    • Hollfelder, F.1    Kirby, A.J.2    Tawfik, D.S.3
  • 116
    • 34250832691 scopus 로고    scopus 로고
    • Polyethylene imine derivatives ('synzymes') accelerate phosphate transfer in the absence of metal
    • Avenier, F., Domingos, J.B., Vliet, L.D., and Hollfelder, F. (2007) Polyethylene imine derivatives ('synzymes') accelerate phosphate transfer in the absence of metal . Journal of the American Chemical Society,129,7611-19 .
    • (2007) Journal of the American Chemical Society , vol.129 , pp. 7611-7619
    • Avenier, F.1    Domingos, J.B.2    Vliet, L.D.3    Hollfelder, F.4
  • 120
    • 0029793086 scopus 로고    scopus 로고
    • Off-the-shelf proteins that rival tailor-made antibodies as catalysts
    • Hollfelder, F., Kirby, A.J., and Tawfik, D.S. (1996) Off-the-shelf proteins that rival tailor-made antibodies as catalysts . Nature,383,60-2 .
    • (1996) Nature , vol.383 , pp. 60-62
    • Hollfelder, F.1    Kirby, A.J.2    Tawfik, D.S.3
  • 121
    • 0016804683 scopus 로고
    • Acetylation of human serum albumin by p-nitrophenyl acetate
    • Means, G.E., and Bender, M.L. (1975) Acetylation of human serum albumin by p-nitrophenyl acetate . Biochemistry,14,4989-94 .
    • (1975) Biochemistry , vol.14 , pp. 4989-4994
    • Means, G.E.1    Bender, M.L.2
  • 123
    • 0035188466 scopus 로고    scopus 로고
    • Catalytic and binding poly-reactivities shared by two unrelated proteins: the potential role of promiscuity in enzyme evolution
    • James, L.C., and Tawfik, D.S. (2001) Catalytic and binding poly-reactivities shared by two unrelated proteins: the potential role of promiscuity in enzyme evolution . Protein Science,10,2600-7 .
    • (2001) Protein Science , vol.10 , pp. 2600-2607
    • James, L.C.1    Tawfik, D.S.2
  • 124
    • 33748630485 scopus 로고    scopus 로고
    • Metals and their scaffolds to promote diffi cult enzymatic reactions
    • Ragsdale, S.W. (2006) Metals and their scaffolds to promote diffi cult enzymatic reactions . Chemical Reviews,106,3317-37 .
    • (2006) Chemical Reviews , vol.106 , pp. 3317-3337
    • Ragsdale, S.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.