Two plate-based colorimetric assays for screening α-amino acid ester hydrolase with high synthesis/hydrolysis ratio

Enzyme and Microbial Technology

Volumn 51, Issue 2, 2012, Pages 107-112

  Wang, Lu ^a,b   Ye, Li Juan ^a,b   Pan, Yue ^b   Cao, Yi ^a  

^a SICHUAN UNIVERSITY   (China)

^b Sichuan Industrial Institute of Antibiotics   (China)

Author keywords

Amino acid ester hydrolase; 7 ACCA; 7 ADCA; AEH; Cefaclor; D PGM; Parallel screening strategy; S H ratio; Spectrophotometric assay

Indexed keywords

7-ACCA; 7-ADCA; AEH; AMINO ACID ESTERS; CEFACLOR; D-PGM; PARALLEL SCREENING; S/H RATIO; SPECTROPHOTOMETRIC ASSAYS;

AMINO ACIDS; ANTIBIOTICS; ESTERIFICATION; ESTERS; GENES; GENETIC ENGINEERING; HYDROLASES; HYDROLYSIS; SPECTROPHOTOMETERS; SPECTROPHOTOMETRY; SYNTHESIS (CHEMICAL);

ASSAYS;

ALPHA AMINO ACID ESTER HYDROLASE; AMINO ACID DERIVATIVE; CEFACLOR; UNCLASSIFIED DRUG;

ARTICLE; BIOCATALYST; COLORIMETRY; CONTROLLED STUDY; DRUG SYNTHESIS; FLUORESCENCE; GENE MUTATION; GRAM NEGATIVE AEROBIC RODS AND COCCI; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HIGH THROUGHPUT SCREENING; HYDROLYSIS; NONHUMAN; POLYMERASE CHAIN REACTION; XANTHOMONAS RUBRILLINEANS;

ACINETOBACTER; ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; BASE SEQUENCE; BETA-LACTAMS; CARBOXYLIC ESTER HYDROLASES; CATALYTIC DOMAIN; CEFACLOR; COLORIMETRY; DNA, BACTERIAL; ENZYME ASSAYS; GLYCINE; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; XANTHOMONAS;

XANTHOMONAS;

EID: 84861725330     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2012.04.009     Document Type: Article

References (27)

1. Barber M.S., Giesecke U., Reichert A., Minas W. Industrial enzymatic production of cephalosporin-based β-lactams. Advances in Biochemical Engineering/Biotechnology 2004, 88:179-215.
2. Volpato G., Rodrigues R.C., Fernandez-Lafuente R. Use of enzymes in the production of semi-synthetic penicillins and cephalosporins: drawbacks and perspectives. Current Medicinal Chemistry 2010, 17:3855-3873.
3. Deaguero A.L., Blum J.K., Bommarius A.S. Wiley's encyclopedia of industrial biotechnology: bioprocess, bioseparation and cell technology. Biocatalytic synthesis of beta-lactam antibiotics 2010, 535-567. Wiley-VCH, Weinheim. M.C. Flickinger (Ed.).
4. Blinkovsky A.M., Markaryan A.N. Synthesis of β-lactam antibiotics containing α-aminophenylacetyl group in the acyl moiety catalyzed by d-(-)-phenylglycyl-β-lactamide amidohydrolase. Enzyme and Microbial Technology 1993, 15:965-973.
5. Schroën C.G.P.H., Nierstrasz V.A., Kroon P.J., Bosma R., Janssen A.E.M., Beeftink H.H., et al. Thermodynamically controlled synthesis of β-lactam antibiotics. Equilibrium concentrations and side-chain properties. Enzyme and Microbial Technology 1999, 24:498-506.
6. Barends T.R.M., Polderman-Tijmes J.J., Jekel P.A., Williams C., Wybenga G., Janssen D.B., et al. Acetobacter turbidans α-amino acid ester hydrolase. Journal of Biological Chemistry 2006, 281:5804-5810.
7. Fernandez-Lafuente R., Hernández-Jústiz O., Mateo C., Terreni M., Alonso J., Garcia-López J.L., et al. Stabilization of a tetrameric enzyme (α-amino acid ester hydrolase from Acetobacter turbidans) enables a very improved performance of ampicillin synthesis. Journal of Molecular Catalysis B: Enzymatic 2001, 11:633-638.
8. Kazlauskas R.J. Enzyme assays: high-throughput screening, genetic selection and fingerprinting. Quantitative assay of hydrolases for activity and selectivity using color changes 2005, 77. Wiley-VCH, Weinheim. J.L. Reymond (Ed.).
9. Alkema W.B.L., Hensgens C.M.H., Kroezinga E.H., de Vries E.J., Floris R., van der Laan J.M., et al. Characterization of the β-lactam binding site of penicillin acylase of Escherichia coli by structural and site-directed mutagenesis studies. Protein Engineering 2000, 13:857-863.
10. El-Shaboury S.R., Saleh G.A., Mohamed F.A., Rageh A.H. Analysis of cephalosporin antibiotics. Journal of Pharmaceutical and Biomedical Analysis 2007, 45:1-19.
11. Samanidou V.F., Hapeshi E.A., Papadoyannis I.N. Rapid and sensitive high-performance liquid chromatographic determination of four cephalosporin antibiotics in pharmaceuticals and body fluids. Journal of Chromatography B 2003, 78:147-158.
12. Hefnawy M., El-Shabrawy Y., Belal F. Spectrofluorometric determination of alpha-aminocephalosporins in biological fluids and pharmaceutical preparations. Journal of Pharmaceutical and Biomedical Analysis 1999, 21:703-707.
13. Ivama V.M., Rodrigues L.N.C., Guaratini C.C.I., Zanoni M.V.B. Spectrophotometric determination of cefaclor in pharmaceutical preparations. Quimica Nova 1999, 22:201-204.
14. Janes L.E., Loëwendahl A.C., Kazlauskas R.J. Quantitative screening of hydrolase libraries using pH indicators: identifying active and enantioselective hydrolases. Chemistry - A European Journal 1998, 4:2324-2331.
15. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976, 72:248-254.
16. Salazar O., Sun L. Evaluating a screen and analysis of mutant libraries. Directed enzyme evolution 2003, 85-97. Humana Press, NJ. F.H. Arnold, G. Georgiou (Eds.).
17. Morley K.L., Kazlauskas R.J. Improving enzyme properties: when are closer mutations better?. Trends in Biotechnology 2005, 23:231-237.
18. Polderman-Tijmes J.J., Jekel P.A., de Vries E.J., van Merode A.E.J., Floris R., van der Laan J.M., et al. Cloning, sequence analysis, and expression in Escherichia coli of the gene encoding an α-amino acid ester hydrolase from Acetobacter turbidans. Applied and Environment Microbiology 2002, 68:211-218.
19. Barends T.R.M., Polderman-Tijmes J.J., Jekel P.A., Hensgens C.M.H., de Vries E.J., Janssen D.B., et al. The sequence and crystal structure of the α-amino acid ester hydrolase from Xanthomonas citri define a new family of β-lactam antibiotic acylases. Journal of Biological Chemistry 2003, 278:23076-23084.
20. Morris G.M., Goodsell D.S., Halliday R.S., Huey R., Hart W.E., Belew R.K., et al. Automated docking using a lamarckian genetic algorithm and empirical binding free energy function. Journal of Computational Chemistry 1998, 19:1639-1662.
21. Yuryev R., Purkarthofer T., Gruber M., Grieng H., Liese A. Kinetic studies of the asymmetric Henry reaction catalyzed by hydroxynitrile lyase from Hevea brasiliensis. Biocatalysis and Biotransformation 2010, 28:348-356.
22. Carbonell P., Faulon J.L. Molecular signatures-based prediction of enzyme promiscuity. Bioinformatics 2010, 26:2012-2019.
23. Khersonsky O., Tawfik D.S. Enzyme promiscuity: a mechanistic and evolutionary perspective. Annual Review of Biochemistry 2010, 79:471-505.
24. Jäckel C., Kast P., Hilvert D. Protein design by directed evolution. Annual Review of Biophysics 2008, 37:153-173.
25. Kelly R.M., Hans Leemhuis H., Rozeboom H.J., van Oosterwijk N., Dijkstra B.W., Dijkhuizen L Elimination of competing hydrolysis and coupling side reactions of a cyclodextrin glucanotransferase by directed evolution. Biochemical Journal 2008, 413:517-525.
26. Ben-Yosef Sendovski M., Fishman A. Directed evolution of tyrosinase for enhanced monophenolase/diphenolase activity ratio. Enzyme and Microbial Technology 2010, 47:372-376.
27. DeLano W.L. The PyMOL molecular graphics system 2002, DeLano Scientific LLC, San Carlos, CA, USA, http://www.pymol.org.