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Volumn 1784, Issue 5, 2008, Pages 811-815

Converting human carbonic anhydrase II into a benzoate ester hydrolase through rational redesign

Author keywords

Carbonic anhydrase; Hydrolysis; Mutagenesis; Protein engineering; Rational design; Specificity

Indexed keywords

4 NITROPHENYLACETIC ACID; 4 NITROPHENYLBENZOATE; ACETIC ACID DERIVATIVE; BENZOATE ESTER HYDROLASE; BENZOIC ACID DERIVATIVE; CARBONATE DEHYDRATASE II; ENZYME VARIANT; HUMAN CARBONIC ANHYDRASE II; HYDROLASE; MUTANT PROTEIN; UNCLASSIFIED DRUG;

EID: 41949141811     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.02.007     Document Type: Article
Times cited : (13)

References (30)
  • 1
    • 33749626714 scopus 로고    scopus 로고
    • Redesign of human carbonic anhydrase II for increased esterase activity and specificity towards esters with long acyl chains
    • Höst G., Mårtensson L.G., and Jonsson B.H. Redesign of human carbonic anhydrase II for increased esterase activity and specificity towards esters with long acyl chains. Biochim. Biophys. Acta 1764 (2006) 1601-1606
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1601-1606
    • Höst, G.1    Mårtensson, L.G.2    Jonsson, B.H.3
  • 3
    • 33750368541 scopus 로고    scopus 로고
    • A cold active (2R,3R)-(-)-di-O-benzoyl-tartrate hydrolyzing esterase from Rhodotorula mucilaginosa
    • Zimmer C., Platz T., Cadez N., Giffhorn F., and Kohring G.W. A cold active (2R,3R)-(-)-di-O-benzoyl-tartrate hydrolyzing esterase from Rhodotorula mucilaginosa. Appl. Microbiol. Biotechnol. 73 (2006) 132-140
    • (2006) Appl. Microbiol. Biotechnol. , vol.73 , pp. 132-140
    • Zimmer, C.1    Platz, T.2    Cadez, N.3    Giffhorn, F.4    Kohring, G.W.5
  • 4
    • 0142119565 scopus 로고    scopus 로고
    • The Rhodococcus sp. cocaine esterase: a bacterial candidate for novel pharmacokinetic-based therapies for cocaine abuse
    • Ascenzi P., Clementi E., and Polticelli F. The Rhodococcus sp. cocaine esterase: a bacterial candidate for novel pharmacokinetic-based therapies for cocaine abuse. Life 55 (2003) 397-402
    • (2003) Life , vol.55 , pp. 397-402
    • Ascenzi, P.1    Clementi, E.2    Polticelli, F.3
  • 5
    • 0033217160 scopus 로고    scopus 로고
    • Purification and characterization of a novel extracellular lipase catalyzing hydrolysis of oleyl benzoate from Acinetobacter nov. sp. strain KM109
    • Mitsuhashi K., Yamashita M., Hwan Y.S., Ihara F., Nihira T., and Yamada Y. Purification and characterization of a novel extracellular lipase catalyzing hydrolysis of oleyl benzoate from Acinetobacter nov. sp. strain KM109. Biosci. Biotechnol. Biochem. 63 (1999) 1959-1964
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 1959-1964
    • Mitsuhashi, K.1    Yamashita, M.2    Hwan, Y.S.3    Ihara, F.4    Nihira, T.5    Yamada, Y.6
  • 9
    • 3543137968 scopus 로고
    • Inherited variant of erythrocyte carbonic anhydrase in micronesians from Guam and Saipan
    • Tashian R.E., Plato C.C., and Shows T.B. Inherited variant of erythrocyte carbonic anhydrase in micronesians from Guam and Saipan. Science 140 (1963) 53-54
    • (1963) Science , vol.140 , pp. 53-54
    • Tashian, R.E.1    Plato, C.C.2    Shows, T.B.3
  • 10
    • 0014062860 scopus 로고
    • The catalytic versatility of erythrocyte carbonic anhydrase. III. Kinetic studies of the enzyme-catalyzed hydrolysis of p-nitrophenyl acetate
    • Pocker Y., and Stone J.T. The catalytic versatility of erythrocyte carbonic anhydrase. III. Kinetic studies of the enzyme-catalyzed hydrolysis of p-nitrophenyl acetate. Biochemistry 6 (1967) 668-678
    • (1967) Biochemistry , vol.6 , pp. 668-678
    • Pocker, Y.1    Stone, J.T.2
  • 11
    • 0014180115 scopus 로고
    • Studies of the esterase activity and the anion inhibition of bovine zinc and cobalt carbonic anhydrases
    • Thorslund A., and Lindskog S. Studies of the esterase activity and the anion inhibition of bovine zinc and cobalt carbonic anhydrases. Eur. J. Biochem. 3 (1967) 117-123
    • (1967) Eur. J. Biochem. , vol.3 , pp. 117-123
    • Thorslund, A.1    Lindskog, S.2
  • 12
    • 34548765952 scopus 로고    scopus 로고
    • Combined enzyme and substrate design: Grafting of a cooperative two-histidine catalytic motif into a protein targeted at the scissile bond in a designed ester substrate
    • Höst G.E., Razkin J., Baltzer L., and Jonsson B.H. Combined enzyme and substrate design: Grafting of a cooperative two-histidine catalytic motif into a protein targeted at the scissile bond in a designed ester substrate. ChemBioChem 8 (2007) 1570-1576
    • (2007) ChemBioChem , vol.8 , pp. 1570-1576
    • Höst, G.E.1    Razkin, J.2    Baltzer, L.3    Jonsson, B.H.4
  • 13
    • 0026047767 scopus 로고
    • Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121
    • Nair S.K., Calderone T.L., Christianson D.W., and Fierke C.A. Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121. J. Biol. Chem. 266 (1991) 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
  • 14
    • 0027389744 scopus 로고
    • Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis
    • Mårtensson L.G., Jonsson B.H., Freskgård P.O., Kihlgren A., Svensson M., and Carlsson U. Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis. Biochemistry 32 (1993) 224-231
    • (1993) Biochemistry , vol.32 , pp. 224-231
    • Mårtensson, L.G.1    Jonsson, B.H.2    Freskgård, P.O.3    Kihlgren, A.4    Svensson, M.5    Carlsson, U.6
  • 16
    • 0017378545 scopus 로고
    • Carbon-13 nuclear magnetic resonance probe of active-site ionizations in human carbonic anhydrase B
    • Khalifah R.G., Strader D.J., Bryant S.H., and Gibson S.M. Carbon-13 nuclear magnetic resonance probe of active-site ionizations in human carbonic anhydrase B. Biochemistry 16 (1977) 2241-2247
    • (1977) Biochemistry , vol.16 , pp. 2241-2247
    • Khalifah, R.G.1    Strader, D.J.2    Bryant, S.H.3    Gibson, S.M.4
  • 17
    • 0000750472 scopus 로고
    • Amino acid composition of various forms of bovine and human erythrocyte carbonic anhydrase
    • Nyman P.O., and Lindskog S. Amino acid composition of various forms of bovine and human erythrocyte carbonic anhydrase. Biochim. Biophys. Acta 85 (1964) 141-151
    • (1964) Biochim. Biophys. Acta , vol.85 , pp. 141-151
    • Nyman, P.O.1    Lindskog, S.2
  • 20
    • 0025135112 scopus 로고
    • Automated docking of substrates to proteins by simulated annealing
    • Goodsell D.S., and Olson A.J. Automated docking of substrates to proteins by simulated annealing. Proteins: Struct., Funct., Genet. 8 (1990) 195-202
    • (1990) Proteins: Struct., Funct., Genet. , vol.8 , pp. 195-202
    • Goodsell, D.S.1    Olson, A.J.2
  • 21
    • 0030203710 scopus 로고    scopus 로고
    • Distributed automated docking of flexible ligands to proteins: parallel applications of Autodock 2.4
    • Morris G.M., Goodsell D.S., Huey R., and Olson A.J. Distributed automated docking of flexible ligands to proteins: parallel applications of Autodock 2.4. J. Comput.-Aided Mol. Des. 10 (1996) 293-304
    • (1996) J. Comput.-Aided Mol. Des. , vol.10 , pp. 293-304
    • Morris, G.M.1    Goodsell, D.S.2    Huey, R.3    Olson, A.J.4
  • 23
    • 0026463503 scopus 로고
    • Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes
    • Håkansson K., Carlsson M., Svensson L.A., and Liljas A. Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes. J. Mol. Biol. 227 (1992) 1192-1204
    • (1992) J. Mol. Biol. , vol.227 , pp. 1192-1204
    • Håkansson, K.1    Carlsson, M.2    Svensson, L.A.3    Liljas, A.4
  • 24
    • 0037103119 scopus 로고    scopus 로고
    • Successful virtual screening for novel inhibitors of human carbonic anhydrase: strategy and experimental confirmation
    • Grüneberg S., Stubbs M.T., and Klebe G. Successful virtual screening for novel inhibitors of human carbonic anhydrase: strategy and experimental confirmation. J. Med. Chem. 45 (2002) 3588-3602
    • (2002) J. Med. Chem. , vol.45 , pp. 3588-3602
    • Grüneberg, S.1    Stubbs, M.T.2    Klebe, G.3
  • 25
    • 0038354636 scopus 로고    scopus 로고
    • Synthesis and evaluation of esters and carbamates to identify critical functional groups for esterase-specific metabolism
    • Yoon K.J.P., Morton C.L., Potter P.M., Danks M.K., and Lee R.E. Synthesis and evaluation of esters and carbamates to identify critical functional groups for esterase-specific metabolism. Bioorg. Med. Chem. 11 (2003) 3237-3244
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 3237-3244
    • Yoon, K.J.P.1    Morton, C.L.2    Potter, P.M.3    Danks, M.K.4    Lee, R.E.5
  • 26
    • 0030571564 scopus 로고    scopus 로고
    • Inhibition of chicken liver carboxylesterase by activated carbonyls and carbonyl hydrates
    • Berndt M.C., Bowles M.R., King G.J., and Zerner B. Inhibition of chicken liver carboxylesterase by activated carbonyls and carbonyl hydrates. Biochim. Biophys. Acta 1298 (1996) 159-166
    • (1996) Biochim. Biophys. Acta , vol.1298 , pp. 159-166
    • Berndt, M.C.1    Bowles, M.R.2    King, G.J.3    Zerner, B.4
  • 27
    • 0000046295 scopus 로고
    • Carbonic anhydrases from human erythrocytes. Preparation and properties of two enzymes.
    • Rickli E.E., Ghazanfar S.A., Gibbons B.H., and Edsall J.T. Carbonic anhydrases from human erythrocytes. Preparation and properties of two enzymes. J. Biol. Chem. 239 (1964) 1065-1078
    • (1964) J. Biol. Chem. , vol.239 , pp. 1065-1078
    • Rickli, E.E.1    Ghazanfar, S.A.2    Gibbons, B.H.3    Edsall, J.T.4
  • 28
    • 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., Sjöblom B., and Lindskog S. Changing the efficiency and specificity of the esterase activity of human carbonic anhydrase II by site-specific mutagenesis. Eur. J. Biochem. 262 (1999) 516-521
    • (1999) Eur. J. Biochem. , vol.262 , pp. 516-521
    • Elleby, B.1    Sjöblom, B.2    Lindskog, S.3
  • 29
    • 0026019002 scopus 로고
    • Fine tuning of the catalytic properties of human carbonic anhydrase II. Effects of varying active-site residue 200
    • Behravan G., Jonsson B.H., and Lindskog S. Fine tuning of the catalytic properties of human carbonic anhydrase II. Effects of varying active-site residue 200. Eur. J. Biochem. 195 (1991) 393-396
    • (1991) Eur. J. Biochem. , vol.195 , pp. 393-396
    • Behravan, G.1    Jonsson, B.H.2    Lindskog, S.3
  • 30
    • 16844379112 scopus 로고    scopus 로고
    • Directed evolution of the promiscuous esterase activity of carbonic anhydrase II
    • Gould S.M., and Tawfik D.S. Directed evolution of the promiscuous esterase activity of carbonic anhydrase II. Biochemistry 44 (2005) 5444-5452
    • (2005) Biochemistry , vol.44 , pp. 5444-5452
    • Gould, S.M.1    Tawfik, D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.