Binding of phage displayed Bacillus subtilis lipase A to a phosphonate suicide inhibitor

Journal of Biotechnology

Volumn 101, Issue 1, 2003, Pages 19-28

  Dröge, Melloney J ^a   Rüggeberg, Carsten J ^b   Van der Sloot, Almer M ^a   Schimmel, Judith ^a   Dijkstra, Dolf Swaving ^a   Verhaert, Raymond M D ^a   Reetz, Manfred T ^b   Quax, Wim J ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b MAX PLANCK INSTITUT FÜR KOHLENFORSCHUNG   (Germany)

Author keywords

1,2 O isopropylidene sn glycerol; Bacillus subtilis lipase; Phage display; Phosphonate suicide inhibitor

Indexed keywords

HYDROLYSIS; MUTAGENESIS; PROTEINS;

PHAGE DISPLAY;

BACTERIOPHAGES;

1,2 O ISOPROPYLIDENE GLYCEROL; 4 NITROPHENYLCAPRYLATE; ACID LIPASE; COAT PROTEIN; GLYCEROL DERIVATIVE; HYBRID PROTEIN; MUTANT PROTEIN; OCTANOIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS SUBTILIS; BACTERIAL GENE; BACTERIOPHAGE; CELL SURFACE; CHIRALITY; CONTROLLED STUDY; ENANTIOSELECTIVITY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; GENE SEQUENCE; HALF LIFE TIME; HYDROLYSIS; METHODOLOGY; MOLECULAR CLONING; MOLECULAR EVOLUTION; MOLECULAR INTERACTION; NONHUMAN; NUCLEOTIDE SEQUENCE; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; REPRODUCIBILITY; SOLUBILITY;

BACILLUS PHAGES; BACILLUS SUBTILIS; BACTERIOPHAGE M13; CELLS, CULTURED; CLONING, MOLECULAR; ENZYME INHIBITORS; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; ISOMERISM; LIPASE; PEPTIDE LIBRARY; PHOSPHONIC ACIDS; PROTEIN BINDING; PROTEIN ENGINEERING; RECOMBINANT FUSION PROTEINS; SUBSTRATE SPECIFICITY;

BACILLUS SUBTILIS; ENTEROBACTERIA PHAGE FD; UNIDENTIFIED BACTERIOPHAGE;

EID: 0346035833     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(02)00289-4     Document Type: Article

References (41)

1. Atwell S., Wells J.A. Selection for improved subtiligases by phage display. Proc. Natl. Acad. Sci. USA. 96:1999;9497-9502.
2. Avalle B., Vanwetswinkel S., Fastrez J. In vitro selection for catalytic turnover from a library of β-lactamase mutants and penicillin-binding proteins. Bioorg. Med. Chem. Lett. 7:1997;479-484.
3. Birnboim H., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7:1979;1513-1523.
4. Chen C.S., Fujimoto Y., Girdaukas G., Sih C.J. Quantitative analyses of biochemical kinetic resolutions of enantiomers. J. Am. Chem. Soc. 104:1982;7294-7299.
5. Danielsen S., Eklund M., Deussen H.-J., Gräslund T., Nygren P.-A., Borchert T.V. In vitro selection of enzymatically active lipase variants from phage libraries using a mechanism-based inhibitor. Gene. 272:2001;267-274.
6. Dartois V., Baulard A., Schanck K., Colson C. Cloning, nucleotide sequence and expression in Escherichia coli of a lipase gene from Bacillus subtilis 168. Biochem. Biophys. Acta. 1131:1992;253-260.
7. Demartis S., Huber A., Viti F., Lozzi L., Giovannoni L., Neri P., Winter G., Neri D. A strategy for the isolation of catalytic activities from repertoires of enzymes displayed on phage. J. Mol. Biol. 286:1999;617-633.
8. Deussen H.-J., Danielsen S., Breinholt J., Borchert T.V. Design and synthesis of triglyceride analogue biotinylated suicide inhibitors for directed molecular evolution of lipolytic enzymes. Bioorg. Med. Chem. Lett. 10:2000;2027-2031.
9. Deussen H.-J., Danielsen S., Breinholt J., Borchert T.V. A novel biotinylated suicide inhibitors for directed molecular evolution of lipolytic enzymes. Bioorg. Med. Chem. 8:2000;507-513.
10. Dröge M.J., Bos R., Quax W.J. Paralogous gene analysis reveals a highly enantioselective 1,2-O-isopropylideneglycerol caprylate esterase of Bacillus subtilis. Eur. J. Biochem. 268:2001;3332-3338.
11. Eggert T., Pencreac'h G., Douchet I., Verger R., Jaeger K.-E. A novel extracellular esterase from Bacillus subtilis and its conversion to a monoacylglycerol hydrolase. Eur. J. Biochem. 267:2000;6459-6469.
12. Frenken L.G.J., Bos J.W., Visser C., Müller W., Tommassen J., Verrips C.T. An accessory gene, lipB, required for the production of active Pseudomonas glumae lipase. Mol. Microbiol. 9:1993;579-589.
13. Hobsin A.H., Buckley C.M., Aamand J.L., Jorgensen S.T., Diderichsen B., McConnell D.J. Activation of a bacterial lipase by its chaperone. Proc. Natl. Acad. Sci. USA. 90:1993;5682-5686.
14. Jaeger K.-E., Ransac S., Dijkstra B.W., Colson C., van Heuvel M., Misset O. Bacterial lipases. FEMS Microbiol. Rev. 15:1994;29-63.
15. Jestin J.-L., Kristensen P., Winter G. A method for the selection of catalytic activity using phage display and proximity coupling. Angew. Chem. Int. Ed. 38:1999;1124-1127.
16. Jorgensen S., Skov K.W., Diderichsen B. Cloning, sequencing, and expression of a lipase gene from Pseudomonas cepacia: lipase production in heterologous hosts requires two Pseudomonas genes. J. Bacteriol. 173:1991;559-567.
17. Koeller K.M., Wong C.-H. Enzymes for chemical synthesis. Nature. 409:2001;232-240.
18. Laemmi U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
19. Lesuisse E., Schanck K., Colson C. Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme. Eur. J. Biochem. 216:1993;155-160.
20. Liebeton K., Zonta A., Schimossek K., Nardini M., Lang D., Dijkstra B.W., Reetz M.T., Jaeger K.-E. Directed evolution of an enantioselective lipase. Chem. Biol. 7:2000;709-718.
21. Mannesse M.L.M., Boots J.-W.P., Dijkman R., Slotboom A.J., van Hijden H.T.W.M., Egmond M.R., Verheij H.M., de Haas G.H. Phosphonate analogues of triacylglycerols are potent inhibitors of lipase. Biochim. Biophys. Acta. 1259:1995;56-64.
22. Marrs B., Delagrave S., Murphy D. Novel approaches for discovering industrial enzymes. Curr. Opin. Microbiol. 2:1999;241-245.
23. Milled N., Beisson F., de Caro J., de Caro A., Arondel V., Verger R. Interfacial catalysis by lipases. J. Mol. Catalysis B: Enzymatic. 11:2001;165-171.
24. van Pouderoyen G., Eggert T., Jaeger K.-E., Dijkstra B.W. The crystal structure of Bacillus subtilis lipase A: a minimal α/β hydrolase fold enzyme. J. Mol. Biol. 309:2001;215-226.
25. Reetz M.T., Jaeger K.-E. Overexpression, immobilization and biotechnological application of Pseudomonas lipases. Chem. Phys. Lipids. 93:1998;3-14.
26. Reetz, M.T., Rüggeberg, C.J., Dröge, M.J., Quax, W.J., 2002. Immobilization of chiral enzyme inhibitors on solid supports by amide-forming coupling and olefin metathesis. Tetrahedron, in press.
27. Rosenstein R., Götz F. Staphylococcal lipases: biochemical and molecular characterization. Biochimie. 82:2000;1005-1014.
28. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: A Laboratory Manual. second ed:1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
29. Schmidt-Dannert C. Recombinant microbial lipases for biotechnological applications. Bioorg. Med. Chem. 7:1999;2123-2130.
30. Schmid A., Dordick J.S., Klener A., Wubbolts M., Witholt B. Industrial biocatalysis today and tomorrow. Nature. 409:2001;258-268.
31. Smith G.P. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science. 228:1985;1315-1317.
32. Soberón-Chávez G., Palmeros B. Pseudomonas lipases: molecular genetics and potential industrial applications. Crit. Rev. Microbiol. 20:1994;95-105.
33. Soumillion P., Jespers L., Bouchet M., Marchand-Brynaert J., Winter G., Fastrez J. Selection of β-lactamase on filamentous bacteriophage by catalytic activity. J. Mol. Biol. 237:1994;415-422.
34. Stadler P., Zandonella G., Haalck L., Spener F., Hermetter A., Paltauf F. Inhibition of microbial lipases with stereoisomeric triadylglycerol analog phosphonates. Biochim. Biophys. Acta. 1304:1996;229-244.
35. Tesar M., Beckmann C., Röttgen P., Haase B., Faude U., Timmis K.N. Monoclonal antibody against pIII of filamentous phage: an immunological tool to study pIII fusion protein expression in phage display systems. Immunotechnology. 1:1995;53-64.
36. Vanwetswinkel S., Touillaux R., Fastrez J., Marchand-Brynaert J. Bifunctional activity labels for selection of filamentous bacteriophages displaying enzymes. Bioorg. Med. Chem. 7:1995;907-915.
37. Vanwetswinkel S., Marchand-Brynaert J., Fastrez J. Selection of the most active enzymes from a mixture of phage-displayed β-lactamase mutants. Bioorg. Med. Chem. Lett. 6:1996;789-792.
38. Verhaert R.M.D., van Duin J., Quax W.J. Processing and functional display of the 86 kDa heterodimeric penicillin G acylase on the surface of phage fd. Biochem. J. 342:1999;415-422.
39. Widersten M., Hansson L.O., Tronstad L., Mannervik B. Use of phage display and transition-state analogs to select enzyme variants with altered catalytic properties: glutathione transferase as an example. Methods Enzymol. 328:2000;389-404.
40. Wilson D.R., Finlay B.B. Phage display: applications, innovations, and issues in phage and host biology. Can. J. Microbiol. 44:1998;313-329.
41. Wind T., Stausbol-Gron B., Kjaer S., Kahns L., Jensen K.H., Clark B.F.C. Retrieval of phage displayed scFv fragments using direct bacterial elution. J. Immunol. Methods. 209:1997;75-83.