Stability and activity improvement of cephalosporin esterase EstB from Burkholderia gladioli by directed evolution and structural interpretation of muteins

Journal of Biotechnology

Volumn 129, Issue 1, 2007, Pages 98-108

  Valinger, Goran ^a   Hermann, Manuela ^a   Wagner, Ulrike G ^b   Schwab, Helmut ^a  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

^b UNIVERSITY OF GRAZ   (Austria)

Author keywords

Activity; Burkholderia gladioli; Cephalosporin C; Directed evolution; Esterase; Stability

Indexed keywords

BIOASSAY; GENES; METABOLISM; MUTAGENESIS; PH EFFECTS;

CEPHALOSPORIN C; DEACETYLATION; ESTERASES; MUTATIONS;

ENZYME KINETICS;

BETA LACTAMASE; CEPHALOSPORIN C;

ARTICLE; BURKHOLDERIA GLADIOLI; CHEMICAL REACTION; DEACETYLATION; MOLECULAR CLONING; MUTAGENESIS; PH; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; THERMOSTABILITY;

AMINO ACID SEQUENCE; BURKHOLDERIA GLADIOLI; CALORIMETRY, DIFFERENTIAL SCANNING; DIRECTED MOLECULAR EVOLUTION; ENZYME STABILITY; ESTERASES; HALF-LIFE; KINETICS; MODELS, MOLECULAR; MUTAGENESIS; MUTANT PROTEINS; MUTATION; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ANALYSIS, PROTEIN; TRANSITION TEMPERATURE;

BURKHOLDERIA GLADIOLI;

EID: 33947131105     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2006.10.008     Document Type: Article

References (26)

1. Arnold F.H. Combinatorial and computational challenges for biocatalyst design. Nature 409 6817 (2001) 253-257
2. Ausubel F.M., Brent R., Kingston R.E., Moore D.d., Seidman J.G., Smith J.A., and Struhl K. Current Protocols in Molecular Biology (1994), Wiley, New York
3. Bornscheuer U.T., and Pohl M. Improved biocatalysts by directed evolution and rational protein design. Curr. Opin. Chem. Biol. 5 2 (2001) 137-143
4. Cadwell R.C., and Joyce G.F. Randomization of genes by PCR mutagenesis. PCR Methods Appl. 2 1 (1992) 28-33
5. Chen K., and Arnold F.H. Enzyme engineering for non-aqueous solvents: random mutagenesis to enhance activity of subtilisin E in polar organic media. Biotechnology (NY) 9 (1991) 1073-1077
6. Chen K., and Arnold F.H. Tuning the activity of an enzyme for unusual environments: sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 5618-5622
7. Devereux J., Haeberli P., and Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucl. Acids Res. 12 (1984) 387-395
8. Eberl L., Kristensen C.S., Givskov M., Grohmann E., Gerlitz M., and Schwab H. Analysis of the multimer resolution system encoded by the parCBA operon of broad-host-range plasmid RP4. Mol. Microbiol. 12 1 (1994) 131-141
9. Faber K. Biotransformations of non-natural compounds: state of the art and future developments. Pure Appl. Chem. 69 (1997) 1613-1632
10. Giver L., Gershenson A., Freskgard P.-O., and Arnold F.H. Directed evolution of a thermostable esterase. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 12809-12813
11. Jaeger K.E., Eggert T., Eipper A., and Reetz M.T. Directed evolution and the creation of enantioselective biocatalysts. Appl. Microbiol. Biotechnol. 55 (2001) 519-530
12. Matthews B.W. Structural and genetic analysis of protein stability. Annu. Rev. Biochem. 62 (1993) 139-160
13. Matthews B.W. Studies on protein stability with T4 lysozyme. Adv. Protein Chem. 46 (1995) 249-278
14. McKay A.M. Microbial carboxylic ester hydrolases (EC 3.1.1.) in food biotechnology. Lett. Appl. Microbiol. 16 (1993) 1-6
15. Meiering E.M., Serrano L., and Fersht A.R. Effect of active site residues in barnase on activity and stability. J. Mol. Biol. 225 (1992) 585-589
16. Moore J.C., and Arnold F.H. Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents. Nat. Biotechnol. 14 (1996) 458-467
17. Moore J.C., Jin H.-M., Kuchner O., and Arnold F.H. Strategies for the in vitro evolution of protein function: enzyme evolution by random recombination of improved sequences. J. Mol. Biol. 272 (1997) 336-347
18. Nishiya Y., Harada N., Teshima S.-I., Yamashita M., Fuyi I., Hirayama N., and Murooka Y. Improvement of thermal stability of Streptomyces cholesterol oxidase by random mutagenesis and a structural interpretation. Protein Eng. 10 (1997) 231-235
19. Okuda H. Esterases. In: Kuby S.A. (Ed). A Study of Enzymes (1991), CRC Press, Boca Raton, FL, USA 563-577
20. Petersen E.I., Valinger G., Sölkner B., Stubenrauch G., and Schwab H. A novel esterase from Burkholderia gladioli which shows high deacetylation activity on cephalosporins is related to β-lactamases and DD-peptidases. J. Biotechnol. 89 (2001) 11-25
21. Shoichet B.K., Baase W.A., Kuroki R., and Matthews B.W. A relationship between protein stability and protein function. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 452-456
22. Spiller B., Gershenson A., Arnold F.H., and Stevens R.C. A structural view of evolutionary divergence. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 12305-12310
23. Stemmer W.P.C. Rapid evolution of a protein by in vitro DNA shuffling. Nature 370 (1994) 389-391
24. Stemmer W.P.C. DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 10747-10751
25. Wagner U.G., Sölkner B., Petersen E.I., Schlacher A., Schwab H., and Kratky C. Crystallization and preliminary X-ray diffraction studies of the Pseudomonas marginata esterase EstB. Acta Crystallogr. D53 (1997) 596-598
26. Wagner U.G., Petersen E.I., Schwab H., and Kratky C. EstB from Burkholderia gladioli: a novel esterase with a β-lactamase fold reveals steric factors to discriminate between esterolytic and β-lactam cleaving activity. Protein Sci. 11 (2002) 467-478