메뉴 건너뛰기




Volumn 16, Issue 12, 2007, Pages 2636-2646

Saturation mutagenesis of Asn152 reveals a substrate selectivity switch in P99 cephalosporinase

Author keywords

lactamase; Enzymology; Kinetics; Microbial sensitivity tests; Saturation mutagenesis; Substrate selectivity

Indexed keywords

AMPICILLIN; ASPARAGINE; CEFALOTIN; CEFOTAXIME; CEFOXITIN; CEPHALOSPORINASE; CEPHALOSPORINASE P99; GLYCINE; MUTANT PROTEIN; NITROCEFIN; OXACILLIN; PENICILLIN G; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 36448945773     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073092407     Document Type: Article
Times cited : (9)

References (51)
  • 2
    • 15244340939 scopus 로고    scopus 로고
    • Altering protein specificity: Techniques and applications
    • Antikainen, N.M. and Martin, S.F. 2005. Altering protein specificity: Techniques and applications. Bioorg. Med. Chem. 13: 2701-2716.
    • (2005) Bioorg. Med. Chem , vol.13 , pp. 2701-2716
    • Antikainen, N.M.1    Martin, S.F.2
  • 3
    • 0036121221 scopus 로고    scopus 로고
    • Structural milestones in the reaction pathway of an amide hydrolase: Substrate, acyl, and product complexes of cephalothin with AmpC β-lactamase
    • Beadle, B.M., Trehan, I., Focia, P.J., and Shoichet, B.K. 2002. Structural milestones in the reaction pathway of an amide hydrolase: Substrate, acyl, and product complexes of cephalothin with AmpC β-lactamase. Structure 10: 413-424.
    • (2002) Structure , vol.10 , pp. 413-424
    • Beadle, B.M.1    Trehan, I.2    Focia, P.J.3    Shoichet, B.K.4
  • 4
    • 0024973407 scopus 로고
    • Structural plasticity broadens the specificity of an engineered protease
    • Bone, R., Silen, J.L., and Agard, D.A. 1989. Structural plasticity broadens the specificity of an engineered protease. Nature 339: 191-195.
    • (1989) Nature , vol.339 , pp. 191-195
    • Bone, R.1    Silen, J.L.2    Agard, D.A.3
  • 5
    • 0032500512 scopus 로고    scopus 로고
    • The role of residue 238 of TEM-1 β-lactamase in the hydrolysis of extended-spectrum antibiotics
    • Cantu, C. and Palzkill, T. 1998. The role of residue 238 of TEM-1 β-lactamase in the hydrolysis of extended-spectrum antibiotics. J. Biol. Chem. 273: 26603-26609.
    • (1998) J. Biol. Chem , vol.273 , pp. 26603-26609
    • Cantu, C.1    Palzkill, T.2
  • 6
    • 0035113737 scopus 로고    scopus 로고
    • Energetic, structural, and antimicrobial analyses of β-lactam side chain recognition by β-lactamases
    • Caselli, E., Powers, R.A., Blasczcak, L.C., Wu, C.Y., Prati, F., and Shoichet, B.K. 2001. Energetic, structural, and antimicrobial analyses of β-lactam side chain recognition by β-lactamases. Chem. Biol. 8: 17-31.
    • (2001) Chem. Biol , vol.8 , pp. 17-31
    • Caselli, E.1    Powers, R.A.2    Blasczcak, L.C.3    Wu, C.Y.4    Prati, F.5    Shoichet, B.K.6
  • 7
    • 0021113925 scopus 로고
    • Characterization of the membrane β-lactamase in Bacillus cereus 569/H/9
    • Connolly, A.K. and Waley, S.G. 1983. Characterization of the membrane β-lactamase in Bacillus cereus 569/H/9. Biochemistry 22: 4647-4651.
    • (1983) Biochemistry , vol.22 , pp. 4647-4651
    • Connolly, A.K.1    Waley, S.G.2
  • 8
    • 0031978726 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of the cloned metallo-β-lactamase L1 from Stenotrophomonas maltophilia
    • Crowder, M.W., Walsh, T.R., Banovic, L., Pettit, M., and Spencer, J. 1998. Overexpression, purification, and characterization of the cloned metallo-β-lactamase L1 from Stenotrophomonas maltophilia. Antimicrob. Agents Chemother. 42: 921-926.
    • (1998) Antimicrob. Agents Chemother , vol.42 , pp. 921-926
    • Crowder, M.W.1    Walsh, T.R.2    Banovic, L.3    Pettit, M.4    Spencer, J.5
  • 9
    • 0032985224 scopus 로고    scopus 로고
    • Escherichia coli mutants lacking all possible combinations of eight penicillin-binding proteins: Viability, characteristics, and implications for peptidoglycan synthesis
    • Denome, S.A., Elf, P.K., Henderson, T.A., Nelson, D.E., and Young, K.D. 1999. Escherichia coli mutants lacking all possible combinations of eight penicillin-binding proteins: Viability, characteristics, and implications for peptidoglycan synthesis. J. Bacteriol. 181: 3981-3993.
    • (1999) J. Bacteriol , vol.181 , pp. 3981-3993
    • Denome, S.A.1    Elf, P.K.2    Henderson, T.A.3    Nelson, D.E.4    Young, K.D.5
  • 10
    • 8544219754 scopus 로고    scopus 로고
    • Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in TEM-1 β-lactamase
    • Doucet, N., De Wals, P.Y., and Pelletier, J.N. 2004. Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in TEM-1 β-lactamase. J. Biol. Chem. 279: 46295-46303.
    • (2004) J. Biol. Chem , vol.279 , pp. 46295-46303
    • Doucet, N.1    De Wals, P.Y.2    Pelletier, J.N.3
  • 11
    • 0029068208 scopus 로고
    • Role of asparagine 152 in catalysis of β-lactam hydrolysis by Escherichia coli AmpC β-lactamase studied by site-directed mutagenesis
    • Dubus, A., Normark, S., Kania, M., and Page, M.G. 1995. Role of asparagine 152 in catalysis of β-lactam hydrolysis by Escherichia coli AmpC β-lactamase studied by site-directed mutagenesis. Biochemistry 34: 7757-7764.
    • (1995) Biochemistry , vol.34 , pp. 7757-7764
    • Dubus, A.1    Normark, S.2    Kania, M.3    Page, M.G.4
  • 12
    • 0029817551 scopus 로고    scopus 로고
    • The roles of residues Tyr150, Glu272, and His314 in class C β-lactamases
    • Dubus, A., Ledent, P., Lamotte-Brasseur, J., and Frère, J.M. 1996. The roles of residues Tyr150, Glu272, and His314 in class C β-lactamases. Proteins 25: 473-485.
    • (1996) Proteins , vol.25 , pp. 473-485
    • Dubus, A.1    Ledent, P.2    Lamotte-Brasseur, J.3    Frère, J.M.4
  • 13
    • 0019164846 scopus 로고
    • β-Lactamase proceeds via an acyl-enzyme intermediate. Interaction of the Escherichia coli RTEM enzyme with cefoxitin
    • Fisher, J., Belasco, J.G., Khosla, S., and Knowles, J.R. 1980. β-Lactamase proceeds via an acyl-enzyme intermediate. Interaction of the Escherichia coli RTEM enzyme with cefoxitin. Biochemistry 19: 2895-2901.
    • (1980) Biochemistry , vol.19 , pp. 2895-2901
    • Fisher, J.1    Belasco, J.G.2    Khosla, S.3    Knowles, J.R.4
  • 14
    • 14844362964 scopus 로고    scopus 로고
    • Bacterial resistance to β-lactam antibiotics: Compelling opportunism, compelling opportunity
    • Fisher, J.F., Meroueh, S.O., and Mobashery, S. 2005. Bacterial resistance to β-lactam antibiotics: Compelling opportunism, compelling opportunity. Chem. Rev. 105: 395-424.
    • (2005) Chem. Rev , vol.105 , pp. 395-424
    • Fisher, J.F.1    Meroueh, S.O.2    Mobashery, S.3
  • 16
    • 0024591706 scopus 로고
    • Quantitative relationship between sensitivity to β-lactam antibiotics and β-lactamase production in gram-negative bacteria. 1. Steady-state treatment
    • Frère, J.M. 1989. Quantitative relationship between sensitivity to β-lactam antibiotics and β-lactamase production in gram-negative bacteria. 1. Steady-state treatment. Biochem. Pharmacol. 38: 1415-1426.
    • (1989) Biochem. Pharmacol , vol.38 , pp. 1415-1426
    • Frère, J.M.1
  • 17
    • 0024563254 scopus 로고
    • Quantitative relationship between sensitivity to β-lactam antibiotics and β-lactamase production in gram-negative bacteria. 2. Non-steady-state treatment and progress curves
    • Frère, J.M., Joris, B., Crine, M., and Martin, H.H. 1989. Quantitative relationship between sensitivity to β-lactam antibiotics and β-lactamase production in gram-negative bacteria. 2. Non-steady-state treatment and progress curves. Biochem. Pharmacol. 38: 1427-1433.
    • (1989) Biochem. Pharmacol , vol.38 , pp. 1427-1433
    • Frère, J.M.1    Joris, B.2    Crine, M.3    Martin, H.H.4
  • 18
    • 0023759003 scopus 로고
    • A survey of the kinetic parameters of class C β-lactamases. Penicillins
    • Galleni, M. and Frère, J.M. 1988. A survey of the kinetic parameters of class C β-lactamases. Penicillins. Biochem. J. 255: 119-122.
    • (1988) Biochem. J , vol.255 , pp. 119-122
    • Galleni, M.1    Frère, J.M.2
  • 19
    • 0023777977 scopus 로고
    • A survey of the kinetic parameters of class C β-lactamases. Cephalosporins and other β-lactam compounds
    • Galleni, M., Amicosante, G., and Frère, J.M. 1988. A survey of the kinetic parameters of class C β-lactamases. Cephalosporins and other β-lactam compounds. Biochem. J. 255: 123-129.
    • (1988) Biochem. J , vol.255 , pp. 123-129
    • Galleni, M.1    Amicosante, G.2    Frère, J.M.3
  • 21
    • 0018256938 scopus 로고
    • A graphical method for extracting rate constants from some enzyme-catalyzed reactions not monitored to completion
    • Glick, B.R., Brubacher, L.J., and Leggett, D.J. 1978. A graphical method for extracting rate constants from some enzyme-catalyzed reactions not monitored to completion. Can. J. Biochem. 56: 1055-1057.
    • (1978) Can. J. Biochem , vol.56 , pp. 1055-1057
    • Glick, B.R.1    Brubacher, L.J.2    Leggett, D.J.3
  • 22
    • 0041842502 scopus 로고    scopus 로고
    • Identification of residues critical for catalysis in a class C β-lactamase by combinatorial scanning mutagenesis
    • Goldberg, S.D., Iannuccilli, W., Nguyen, T., Ju, J., and Cornish, V.W. 2003. Identification of residues critical for catalysis in a class C β-lactamase by combinatorial scanning mutagenesis. Protein Sci. 12: 1633-1645.
    • (2003) Protein Sci , vol.12 , pp. 1633-1645
    • Goldberg, S.D.1    Iannuccilli, W.2    Nguyen, T.3    Ju, J.4    Cornish, V.W.5
  • 23
    • 0035807996 scopus 로고    scopus 로고
    • Critical involvement of a carbamylated lysine in catalytic function of class D β-lactamases
    • Golemi, D., Maveyraud, L., Vakulenko, S., Samama, J.P., and Mobashery, S. 2001. Critical involvement of a carbamylated lysine in catalytic function of class D β-lactamases. Proc. Natl. Acad. Sci. 98: 14280-14285.
    • (2001) Proc. Natl. Acad. Sci , vol.98 , pp. 14280-14285
    • Golemi, D.1    Maveyraud, L.2    Vakulenko, S.3    Samama, J.P.4    Mobashery, S.5
  • 25
    • 0030884768 scopus 로고    scopus 로고
    • AmpC and AmpH, proteins related to the class C β-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli
    • Henderson, T.A., Young, K.D., Denome, S.A., and Elf, P.K. 1997. AmpC and AmpH, proteins related to the class C β-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli. J. Bacteriol. 179: 6112-6121.
    • (1997) J. Bacteriol , vol.179 , pp. 6112-6121
    • Henderson, T.A.1    Young, K.D.2    Denome, S.A.3    Elf, P.K.4
  • 26
    • 3843062433 scopus 로고    scopus 로고
    • Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferase
    • Hsiao, Y.S., Jogl, G., and Tong, L. 2004. Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferase. J. Biol. Chem. 279: 31584-31589.
    • (2004) J. Biol. Chem , vol.279 , pp. 31584-31589
    • Hsiao, Y.S.1    Jogl, G.2    Tong, L.3
  • 28
    • 0025092290 scopus 로고
    • Role of the conserved amino-acids of the SDN loop (Ser130, Asp131 and Asn132) in a class A β-lactamase studied by site-directed mutagenesis
    • Jacob, F., Joris, B., Lepage, S., Dusart, J., and Frère, J.M. 1990b. Role of the conserved amino-acids of the SDN loop (Ser130, Asp131 and Asn132) in a class A β-lactamase studied by site-directed mutagenesis. Biochem. J. 271: 399-406.
    • (1990) Biochem. J , vol.271 , pp. 399-406
    • Jacob, F.1    Joris, B.2    Lepage, S.3    Dusart, J.4    Frère, J.M.5
  • 29
    • 0038625074 scopus 로고    scopus 로고
    • Mimicking natural evolution in vitro: An N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity
    • Joerger, A.C., Mayer, S., and Fersht, A.R. 2003. Mimicking natural evolution in vitro: An N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity. Proc. Natl. Acad. Sci. 100: 5694-5699.
    • (2003) Proc. Natl. Acad. Sci , vol.100 , pp. 5694-5699
    • Joerger, A.C.1    Mayer, S.2    Fersht, A.R.3
  • 30
    • 0021795104 scopus 로고
    • The β-lactamase of Enterobacter cloacae P99. Chemical properties, N-terminal sequence and interaction with 6 β-halogenopenicillanates
    • Joris, B., De Meester, F., Galleni, M., Reckinger, G., Coyette, J., Frère, J.M., and Van Beeumen, J. 1985. The β-lactamase of Enterobacter cloacae P99. Chemical properties, N-terminal sequence and interaction with 6 β-halogenopenicillanates. Biochem. J. 228: 241-248.
    • (1985) Biochem. J , vol.228 , pp. 241-248
    • Joris, B.1    De Meester, F.2    Galleni, M.3    Reckinger, G.4    Coyette, J.5    Frère, J.M.6    Van Beeumen, J.7
  • 31
    • 0026244229 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. 1991. Molscript - A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950.
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 32
    • 1542267769 scopus 로고    scopus 로고
    • Kinetics of turnover of cefotaxime by the Enterobacter cloacae P99 and GCl β-lactamases: Two free enzyme forms of the P99 β-lactamase detected by a combination of pre- and post-steady state kinetics
    • Kumar, S., Adediran, S.A., Nukaga, M., and Pratt, R.F. 2004. Kinetics of turnover of cefotaxime by the Enterobacter cloacae P99 and GCl β-lactamases: Two free enzyme forms of the P99 β-lactamase detected by a combination of pre- and post-steady state kinetics. Biochemistry 43: 2664-2672.
    • (2004) Biochemistry , vol.43 , pp. 2664-2672
    • Kumar, S.1    Adediran, S.A.2    Nukaga, M.3    Pratt, R.F.4
  • 33
    • 0027428548 scopus 로고
    • Evolution of an enzyme activity: Crystallographic structure at 2 Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase
    • Lobkovsky, E., Moews, P.C., Liu, H., Zhao, H., Frère, J.M., and Knox, J.R. 1993. Evolution of an enzyme activity: Crystallographic structure at 2 Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase. Proc. Natl. Acad. Sci. 90: 11257-11261.
    • (1993) Proc. Natl. Acad. Sci , vol.90 , pp. 11257-11261
    • Lobkovsky, E.1    Moews, P.C.2    Liu, H.3    Zhao, H.4    Frère, J.M.5    Knox, J.R.6
  • 34
    • 23044482926 scopus 로고    scopus 로고
    • Amino acid residues that contribute to substrate specificity of class A β-lactamase SME-1
    • Majiduddin, F.K. and Palzkill, T. 2005. Amino acid residues that contribute to substrate specificity of class A β-lactamase SME-1. Antimicrob. Agents Chemother. 49: 3421-3427.
    • (2005) Antimicrob. Agents Chemother , vol.49 , pp. 3421-3427
    • Majiduddin, F.K.1    Palzkill, T.2
  • 35
    • 0032790081 scopus 로고    scopus 로고
    • XtalView Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee, D.E. 1999. XtalView Xfit - A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125: 156-165.
    • (1999) J. Struct. Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 36
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E.A. and Bacon, D.J. 1997. Raster3D: Photorealistic molecular graphics. Macromol. Crystallogr. B 277: 505-524.
    • (1997) Macromol. Crystallogr. B , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 37
    • 0028040823 scopus 로고
    • The role of lysine-67 in a class C β-lactamase is mainly electrostatic
    • Monnaie, D., Dubus, A., and Frére, J.M. 1994. The role of lysine-67 in a class C β-lactamase is mainly electrostatic. Biochem. J. 302: 1-4.
    • (1994) Biochem. J , vol.302 , pp. 1-4
    • Monnaie, D.1    Dubus, A.2    Frére, J.M.3
  • 38
    • 0028900778 scopus 로고
    • Substitution of Asp for Asn at position 132 in the active site of TEM β-lactamase. Activity toward different substrates and effects of neighboring residues
    • Osuna, J., Viadiu, H., Fink, A.L., and Soberòn, X. 1995. Substitution of Asp for Asn at position 132 in the active site of TEM β-lactamase. Activity toward different substrates and effects of neighboring residues. J. Biol. Chem. 270: 775-780.
    • (1995) J. Biol. Chem , vol.270 , pp. 775-780
    • Osuna, J.1    Viadiu, H.2    Fink, A.L.3    Soberòn, X.4
  • 39
  • 41
    • 21644480798 scopus 로고    scopus 로고
    • Structural consequences of the inhibitor-resistant Ser130Gly substitution in TEM-lactamase
    • Thomas, V.L., Golemi-Kotra, D., Kim, C., Vakulenko, S.B., Mobashery, S., and Shoichet, B.K. 2005. Structural consequences of the inhibitor-resistant Ser130Gly substitution in TEM-lactamase. Biochemistry 44: 9330-9338.
    • (2005) Biochemistry , vol.44 , pp. 9330-9338
    • Thomas, V.L.1    Golemi-Kotra, D.2    Kim, C.3    Vakulenko, S.B.4    Mobashery, S.5    Shoichet, B.K.6
  • 42
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 43
    • 34250872269 scopus 로고    scopus 로고
    • Minimalist active-site redesign: Teaching old enzymes new tricks
    • Toscano, M.D., Woycechowsky, K.J., and Hilvert, D. 2007. Minimalist active-site redesign: Teaching old enzymes new tricks. Angew. Chem. Int. Ed. Engl. 46: 3212-3236.
    • (2007) Angew. Chem. Int. Ed. Engl , vol.46 , pp. 3212-3236
    • Toscano, M.D.1    Woycechowsky, K.J.2    Hilvert, D.3
  • 44
    • 0035838468 scopus 로고    scopus 로고
    • Inhibition of AmpC β-lactamase through a destabilizing interaction in the active site
    • Trehan, I., Beadle, B.M., and Shoichet, B.K. 2001. Inhibition of AmpC β-lactamase through a destabilizing interaction in the active site. Biochemistry 40: 7992-7999.
    • (2001) Biochemistry , vol.40 , pp. 7992-7999
    • Trehan, I.1    Beadle, B.M.2    Shoichet, B.K.3
  • 45
    • 0038338497 scopus 로고    scopus 로고
    • Burkholderia pseudomallei class a β-lactamase mutations that confer selective resistance against ceftazidime or clavulanic acid inhibition
    • Tribuddharat, C., Moore, R.A., Baker, P., and Woods, D.E. 2003. Burkholderia pseudomallei class a β-lactamase mutations that confer selective resistance against ceftazidime or clavulanic acid inhibition. Antimicrob. Agents Chemother. 47: 2082-2087.
    • (2003) Antimicrob. Agents Chemother , vol.47 , pp. 2082-2087
    • Tribuddharat, C.1    Moore, R.A.2    Baker, P.3    Woods, D.E.4
  • 46
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang, L., Brock, A., Herberich, B., and Schultz, P.G. 2001. Expanding the genetic code of Escherichia coli. Science 292: 498-500.
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 47
    • 33746878510 scopus 로고    scopus 로고
    • Crystal structure and activity studies of the Mycobacterium tuberculosis β-lactamase reveal its critical role in resistance to β-lactam antibiotics
    • Wang, F., Cassidy, C., and Sacchettini, J.C. 2006. Crystal structure and activity studies of the Mycobacterium tuberculosis β-lactamase reveal its critical role in resistance to β-lactam antibiotics. Antimicrob. Agents Chemother. 50: 2762-2771.
    • (2006) Antimicrob. Agents Chemother , vol.50 , pp. 2762-2771
    • Wang, F.1    Cassidy, C.2    Sacchettini, J.C.3
  • 48
    • 33845496747 scopus 로고    scopus 로고
    • Discovery of a substrate selectivity switch in tyrosine ammonialyase, a member of the aromatic amino acid lyase family
    • Watts, K.T., Mijts, B.N., Lee, P.C., Manning, A.J., and Schmidt-Dannert, C. 2006. Discovery of a substrate selectivity switch in tyrosine ammonialyase, a member of the aromatic amino acid lyase family. Chem. Biol. 13: 1317-1326.
    • (2006) Chem. Biol , vol.13 , pp. 1317-1326
    • Watts, K.T.1    Mijts, B.N.2    Lee, P.C.3    Manning, A.J.4    Schmidt-Dannert, C.5
  • 49
    • 0023394374 scopus 로고
    • Recruitment of substrate-specificity properties from one enzyme into a related one by protein engineering
    • Wells, J.A., Cunningham, B.C., Graycar, T.P., and Estell, D.A. 1987. Recruitment of substrate-specificity properties from one enzyme into a related one by protein engineering. Proc. Natl. Acad. Sci. 84: 5167-5171.
    • (1987) Proc. Natl. Acad. Sci , vol.84 , pp. 5167-5171
    • Wells, J.A.1    Cunningham, B.C.2    Graycar, T.P.3    Estell, D.A.4
  • 50
    • 0026210430 scopus 로고
    • Alteration of enzyme specificity and catalysis by protein engineering
    • Wilks, H.M. and Holbrook, J.J. 1991. Alteration of enzyme specificity and catalysis by protein engineering. Curr. Opin. Biotechnol. 2: 561-567.
    • (1991) Curr. Opin. Biotechnol , vol.2 , pp. 561-567
    • Wilks, H.M.1    Holbrook, J.J.2
  • 51
    • 0032510667 scopus 로고    scopus 로고
    • Directed evolution of an aspartate aminotransferase with new substrate specificities
    • Yano, T., Oue, S., and Kagamiyama, H. 1998. Directed evolution of an aspartate aminotransferase with new substrate specificities. Proc. Natl. Acad. Sci. 95: 5511-5515.
    • (1998) Proc. Natl. Acad. Sci , vol.95 , pp. 5511-5515
    • Yano, T.1    Oue, S.2    Kagamiyama, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.