메뉴 건너뛰기




Volumn 44, Issue 14, 2005, Pages 5444-5452

Directed evolution of the promiscuous esterase activity of carbonic anhydrase II

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CATALYSIS; ESTERS; HYDRATION; MUTAGENESIS;

EID: 16844379112     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0475471     Document Type: Article
Times cited : (88)

References (42)
  • 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, Chem. Biol. 6, R91-R105.
    • (1999) Chem. Biol. , vol.6
    • O'Brien, P.J.1    Herschlag, D.2
  • 2
    • 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, Curr. Opin. Chem. Biol. 7, 265-272.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 265-272
    • Copley, S.D.1
  • 3
    • 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, Angew. Chem., Int. Ed. 43, 6032-6040.
    • (2004) Angew. Chem., Int. Ed. , vol.43 , pp. 6032-6040
    • Bornscheuer, U.T.1    Kazlauskas, R.J.2
  • 4
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution - A 60-year-old hypothesis revisited
    • James, L. C., and Tawfik, D. S. (2003) Conformational diversity and protein evolution - A 60-year-old hypothesis revisited, Trends Biochem. Sci. 28, 361-368.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 5
    • 3042553541 scopus 로고    scopus 로고
    • The role of inhibition in enzyme evolution
    • McLoughlin, S. Y., and Ollis, D. L. (2004) The role of inhibition in enzyme evolution, Chem. Biol. 11, 735-737.
    • (2004) Chem. Biol. , vol.11 , pp. 735-737
    • McLoughlin, S.Y.1    Ollis, D.L.2
  • 7
    • 4744343021 scopus 로고    scopus 로고
    • The altered evolutionary trajectories of gene duplicates
    • Lynch, M., and Katju, V. (2004) The altered evolutionary trajectories of gene duplicates, Trends Genet. 20, 544-549.
    • (2004) Trends Genet. , vol.20 , pp. 544-549
    • Lynch, M.1    Katju, V.2
  • 9
    • 11244261591 scopus 로고    scopus 로고
    • In search of the limits of evolution
    • Kondrashov, F. A. (2005) In search of the limits of evolution, Nat. Genet. 37, 9-10.
    • (2005) Nat. Genet. , vol.37 , pp. 9-10
    • Kondrashov, F.A.1
  • 10
    • 0036471942 scopus 로고    scopus 로고
    • Crystal structure of human carbonic anhydrase II complexed with an anti-convulsant sugar sulphamate
    • Recacha, R., Costanzo, M. J., Maryanoff, B. E., and Chattopadhyay, D. (2002) Crystal structure of human carbonic anhydrase II complexed with an anti-convulsant sugar sulphamate, Biochem. J. 361, 437-441.
    • (2002) Biochem. J. , vol.361 , pp. 437-441
    • Recacha, R.1    Costanzo, M.J.2    Maryanoff, B.E.3    Chattopadhyay, D.4
  • 11
    • 0346252639 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors: X-ray crystallographic structure of the adduct of human isozyme II with EMATE, a dual inhibitor of carbonic anhydrases and steroid sulfatase
    • Abbate, F., Winum J.-Y., Potter, B. V. L., Casini, A., Montero, J.-L., Scozzafava, A., and Supuran, C. T. (2004) Carbonic anhydrase inhibitors: X-ray crystallographic structure of the adduct of human isozyme II with EMATE, a dual inhibitor of carbonic anhydrases and steroid sulfatase, Bioorg. Med. Chem. Lett. 14, 231-234.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 231-234
    • Abbate, F.1    Winum, J.-Y.2    Potter, B.V.L.3    Casini, A.4    Montero, J.-L.5    Scozzafava, A.6    Supuran, C.T.7
  • 12
    • 0031887344 scopus 로고    scopus 로고
    • Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: Molecular basis of isozyme - Drug discrimination
    • Stams, T., Chen, Y., Boriack-Sjodin, P. A., Hurt, J. D., Liao, J., May, J. A., Dean, T., Laipis, P., Silverman, D. N., and Christianson, D. W. (1998) Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: Molecular basis of isozyme - drug discrimination, Protein Sci. 7, 556-563.
    • (1998) Protein Sci. , vol.7 , pp. 556-563
    • Stams, T.1    Chen, Y.2    Boriack-Sjodin, P.A.3    Hurt, J.D.4    Liao, J.5    May, J.A.6    Dean, T.7    Laipis, P.8    Silverman, D.N.9    Christianson, D.W.10
  • 13
    • 1842871152 scopus 로고    scopus 로고
    • Changing the efficiency and specificity of the esterase activity of human carbonic anhydrase II by site-specific mutagenesis
    • Elleby, B., Sjoblom, B., and Lindskog, S. (1999) Changing the efficiency and specificity of the esterase activity of human carbonic anhydrase II by site-specific mutagenesis, Eur. J. Biochem. 262, 516-521.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 516-521
    • Elleby, B.1    Sjoblom, B.2    Lindskog, S.3
  • 14
    • 0031283056 scopus 로고    scopus 로고
    • Histidine → carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity
    • Lesburg, C. A., Huang, C., Christianson, D. W., and Fierke, C. A. (1997) Histidine → carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity, Biochemistry 36, 15780-15791.
    • (1997) Biochemistry , vol.36 , pp. 15780-15791
    • Lesburg, C.A.1    Huang, C.2    Christianson, D.W.3    Fierke, C.A.4
  • 15
    • 0026316929 scopus 로고
    • Functional consequences of engineering the hydrophobic pocket of carbonic anhydrase II
    • Fierke, C. A., Calderone, T. L., and Krebs, J. F. (1991) Functional consequences of engineering the hydrophobic pocket of carbonic anhydrase II, Biochemistry 30, 11054-11063.
    • (1991) Biochemistry , vol.30 , pp. 11054-11063
    • Fierke, C.A.1    Calderone, T.L.2    Krebs, J.F.3
  • 16
    • 0014180115 scopus 로고
    • Studies of the esterase activity and the anion inhibition of bovine zinc and cobalt carbonic anhydrases
    • Thorslund, A., and Lindskog, S. (1967) Studies of the esterase activity and the anion inhibition of bovine zinc and cobalt carbonic anhydrases, Eur. J. Biochem. 3, 117-123.
    • (1967) Eur. J. Biochem. , vol.3 , pp. 117-123
    • Thorslund, A.1    Lindskog, S.2
  • 17
    • 0035839131 scopus 로고    scopus 로고
    • Expansion of the zinc metallo-hydrolase family of the β-lactamase fold
    • Daiyasu, H., Osaka, K., Ishino, Y., and Toh, H. (2001) Expansion of the zinc metallo-hydrolase family of the β-lactamase fold, FEBS Lett. 503, 1-6.
    • (2001) FEBS Lett. , vol.503 , pp. 1-6
    • Daiyasu, H.1    Osaka, K.2    Ishino, Y.3    Toh, H.4
  • 18
    • 33845283317 scopus 로고
    • Origin of rate accelerations in an enzyme model: The p-nitrophenyl ester syndrome
    • Menger, F. M., and Ladika, M. (1987) Origin of rate accelerations in an enzyme model: The p-nitrophenyl ester syndrome, J. Am. Chem. Soc. 109, 3145-3146.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 3145-3146
    • Menger, F.M.1    Ladika, M.2
  • 19
    • 0000992327 scopus 로고
    • Base catalysis of imidazole catalysis of ester hydrolysis
    • Kirsch, J. F., and Jencks, W. P. (1964) Base catalysis of imidazole catalysis of ester hydrolysis, J. Am. Chem. Soc. 86, 833-837.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 833-837
    • Kirsch, J.F.1    Jencks, W.P.2
  • 20
    • 0025946277 scopus 로고
    • Conformational mobility of His-64 in the Thr-200-Ser mutant of human carbonic anhydrase II
    • Krebs, J. F., Fierke, C. A., Alexander, R. S., and Christianson, D. W. (1991) Conformational mobility of His-64 in the Thr-200-Ser mutant of human carbonic anhydrase II, Biochemistry 30, 9153-9160.
    • (1991) Biochemistry , vol.30 , pp. 9153-9160
    • Krebs, J.F.1    Fierke, C.A.2    Alexander, R.S.3    Christianson, D.W.4
  • 22
    • 0033280672 scopus 로고    scopus 로고
    • Exploring nonnatural evolutionary pathways by saturation mutagenesis: Rapid improvement of protein function
    • Miyazaki, K., and Arnold, F. H. (1999) Exploring nonnatural evolutionary pathways by saturation mutagenesis: Rapid improvement of protein function, J. Mol. Evol. 49, 716-720.
    • (1999) J. Mol. Evol. , vol.49 , pp. 716-720
    • Miyazaki, K.1    Arnold, F.H.2
  • 23
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W. P. C (1994) Rapid evolution of a protein in vitro by DNA shuffling, Nature, 370, 389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 25
    • 0015239422 scopus 로고
    • The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C
    • Khalifah, R. G. (1971) The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C, J. Biol. Chem. 246, 2561-2573.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2561-2573
    • Khalifah, R.G.1
  • 26
    • 0141858715 scopus 로고    scopus 로고
    • The specificity of cross-reactivity: Promiscuous antibody binding involves specific hydrogen bonds rather than nonspecific hydrophobic stickiness
    • James, L. C., and Tawfik, D. S. (2003) The specificity of cross-reactivity: Promiscuous antibody binding involves specific hydrogen bonds rather than nonspecific hydrophobic stickiness, Protein Sci. 12, 2183-2193.
    • (2003) Protein Sci. , vol.12 , pp. 2183-2193
    • James, L.C.1    Tawfik, D.S.2
  • 27
    • 0033013283 scopus 로고    scopus 로고
    • Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones
    • Khalameyzer, V., Fischer, I., Bornscheuer, U. T., and Altenbuchner, J. (1999) Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones, Appl. Environ. Microbiol. 65, 477-482.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 477-482
    • Khalameyzer, V.1    Fischer, I.2    Bornscheuer, U.T.3    Altenbuchner, J.4
  • 28
    • 0028935889 scopus 로고
    • Structural basis of inhibitor affinity to variants of human carbonic anhydrase II
    • Nair, S. K., Krebs, J. F., Christianson, D. W., and Fierke, C. A. (1995) Structural basis of inhibitor affinity to variants of human carbonic anhydrase II, Biochemistry 34, 3981-3989.
    • (1995) Biochemistry , vol.34 , pp. 3981-3989
    • Nair, S.K.1    Krebs, J.F.2    Christianson, D.W.3    Fierke, C.A.4
  • 29
    • 0027418070 scopus 로고
    • Importance of the conserved active-site residues Tyr7, Glu106, and Thr199 for the catalytic function of human carbonic anhydrase II
    • Liang, Z., Xue, Y., Behravan, G., Jonsson, B. H., and Lindskog, S. (1993) Importance of the conserved active-site residues Tyr7, Glu106, and Thr199 for the catalytic function of human carbonic anhydrase II, Eur. J. Biochem. 211, 821-827.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 821-827
    • Liang, Z.1    Xue, Y.2    Behravan, G.3    Jonsson, B.H.4    Lindskog, S.5
  • 30
    • 0026006499 scopus 로고
    • Some properties of site-specific mutants of human carbonic anhydrase II having active-site residues characterizing carbonic anhydrase III
    • Ren, X. L., Jonsson, B. H., and Lindskog, S. (1991) Some properties of site-specific mutants of human carbonic anhydrase II having active-site residues characterizing carbonic anhydrase III, Eur. J. Biochem. 201, 417-420.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 417-420
    • Ren, X.L.1    Jonsson, B.H.2    Lindskog, S.3
  • 31
    • 0027439522 scopus 로고
    • Determinants of catalytic activity and stability of carbonic anhydrase II as revealed by random mutagenesis
    • Krebs, J. F., and Fierke, C. A. (1993) Determinants of catalytic activity and stability of carbonic anhydrase II as revealed by random mutagenesis, J. Biol. Chem. 268, 948-954.
    • (1993) J. Biol. Chem. , vol.268 , pp. 948-954
    • Krebs, J.F.1    Fierke, C.A.2
  • 33
    • 0035943306 scopus 로고    scopus 로고
    • On the magnitude and specificity of medium effects in enzyme-like catalysts for proton transfer
    • Hollfelder, F., Kirby, A. J., and Tawfik, D. S. (2001) On the magnitude and specificity of medium effects in enzyme-like catalysts for proton transfer, J. Org. Chem. 66, 5866-5874.
    • (2001) J. Org. Chem. , vol.66 , pp. 5866-5874
    • Hollfelder, F.1    Kirby, A.J.2    Tawfik, D.S.3
  • 35
    • 0030050546 scopus 로고    scopus 로고
    • Unexpected binding mode of the sulfonamide fluorophore 5-dimethylamino-1-naphthalene sulfonamide to human carbonic anhydrase II. Implications for the development of a zinc biosensor
    • Nair, S. K., Elbaum, D., and Christianson, D. W. (1996) Unexpected binding mode of the sulfonamide fluorophore 5-dimethylamino-1-naphthalene sulfonamide to human carbonic anhydrase II. Implications for the development of a zinc biosensor, J. Biol. Chem. 271, 1003-1007.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1003-1007
    • Nair, S.K.1    Elbaum, D.2    Christianson, D.W.3
  • 36
    • 0026047767 scopus 로고
    • Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase 11 mutants at residue Val-121
    • Nair, S. K., Calderone, T. L., Christianson, D. W., and Fierke, C. A. (1991) Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase 11 mutants at residue Val-121, J. Biol. Chem. 266, 17320-17325.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17320-17325
    • Nair, S.K.1    Calderone, T.L.2    Christianson, D.W.3    Fierke, C.A.4
  • 38
    • 0016722749 scopus 로고
    • The catalytic mechanism of carbonic anhydrase. Hydrogen-isotope effects on the kinetic parameters of the human C isoenzyme
    • Steiner, H., Jonsson, B. H., and Lindskog, S. (1975) The catalytic mechanism of carbonic anhydrase. Hydrogen-isotope effects on the kinetic parameters of the human C isoenzyme, Eur. J. Biochem. 59, 253-259.
    • (1975) Eur. J. Biochem. , vol.59 , pp. 253-259
    • Steiner, H.1    Jonsson, B.H.2    Lindskog, S.3
  • 39
    • 0035188466 scopus 로고    scopus 로고
    • Catalytic and binding polyreactivities shared by two unrelated proteins: The potential role of promiscuity in enzyme evolution
    • James, L. C., and Tawfik, D. S. (2001) Catalytic and binding polyreactivities shared by two unrelated proteins: The potential role of promiscuity in enzyme evolution, Protein Sci. 10, 2600-2607.
    • (2001) Protein Sci. , vol.10 , pp. 2600-2607
    • James, L.C.1    Tawfik, D.S.2
  • 40
    • 4344578623 scopus 로고    scopus 로고
    • Phosphorylation-independent dimer-dimer interactions by the enhancer-binding activator NtrC of Escherichia coli: A third function for the C-terminal domain
    • Yang, X. F., Ji, Y., Schneider, B. L., and Reitzer, L. (2004) Phosphorylation-independent dimer-dimer interactions by the enhancer-binding activator NtrC of Escherichia coli: A third function for the C-terminal domain, J. Biol. Chem. 279, 36708-36714.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36708-36714
    • Yang, X.F.1    Ji, Y.2    Schneider, B.L.3    Reitzer, L.4
  • 41
    • 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, Antimicrob. Agents Chemother. 48, 23-29.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 23-29
    • Miller, K.1    O'Neill, A.J.2    Chopra, I.3
  • 42
    • 0036306115 scopus 로고    scopus 로고
    • Why are proteins so robust to site mutations?
    • Taverna, D. M., and Goldstein, R. A. (2002) Why are proteins so robust to site mutations? J. Mol. Biol. 315, 479-484.
    • (2002) J. Mol. Biol. , vol.315 , pp. 479-484
    • Taverna, D.M.1    Goldstein, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.