Application of Site-Directed Lipase Mutants on Regioselective Acylation of Monosaccharides

Journal of Carbohydrate Chemistry

Volumn 22, Issue 7-8, 2003, Pages 631-644

  Cipolla, Laura ^a   Lotti, Marina ^a   De Gioia, Luca ^a   Nicotra, Francesco ^a  

^a UNIVERSITY OF MILANO BICOCCA   (Italy)

Author keywords

Biocatalysis; Lipases; Monosaccharides; Site directed mutagenesis

Indexed keywords

4,6 O BENZYLIDENE ALPHA DEXTRO GALACTOPYRANOSIDE; 4,6 O BENZYLIDENE ALPHA DEXTRO GLUCOPYRANOSIDE; CARBOHYDRATE DERIVATIVE; ENZYME VARIANT; MONOSACCHARIDE; MUTANT PROTEIN; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

ACYLATION; ARTICLE; CANDIDA RUGOSA; CHEMICAL REACTION; CHEMICAL REACTION KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; MOLECULAR MODEL; PROTON NUCLEAR MAGNETIC RESONANCE; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; WILD TYPE;

CANDIDA RUGOSA;

EID: 0348108210     PISSN: 07328303     EISSN: None     Source Type: Journal    
DOI: 10.1081/CAR-120026464     Document Type: Article

References (31)

1. Schmidt, R.D.; Verger, R. Lipases: interfacial enzymes with attractive applications. Angew. Chem., Int. Ed. Engl. 1998, 37, 1608-1633.
2. Jaeger, K.-E.; Dijkstra, B.W.; Reetz, M.T. Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu. Rev. Microbiol. 1999, 53, 315-351.
3. Villeneuve, P.; Muderhwa, J.M.; Graille, J.; Haas, M.J. Customizing lipases for biocatalysis: a survey of chemical, physical and molecular biological approaches. J. Mol. Catal., B Enzym. 2000, 9, 113-148.
4. Rich, J.O.; Michels, P.C.; Khmelnitsky, Y.L. Combinatorial biocatalysis. Curr. Opin. Chem. Biol. 2002, 6, 161-167.
5. Vulfson, E.N. Lipases, Their Structure, Biochemistry and Application; Woolley, P., Petersen, S.B., Eds.; Cambridge University Press, 1994; 271-287.
6. Schmid, A.; Dordick, J.; Hauer, B.; Kiener, A.; Wubbolts, M.; Witholt, B. Industrial biocatalysis today and tomorrow. Nature 2001, 409, 258-268.
7. Koeller, K.M.; Wong, C.-H. Enzymes for chemical synthesis. Nature 2001, 409, 232-240.
8. Klibanov, A.M. Improving enzymes by using them in organic solvents. Nature 2001, 409, 241-246.
9. Arnold, F.H. Combinatorial and computational challenges for biocatalyst design. Nature 2001, 409, 253-257.
10. Zhao, H.; Chockalingam, K.; Chen, Z. Directed evolution of enzymes and pathways for industrial biocatalysis. Curr. Opin. Biotechnol. 2002, 13, 104-110.
11. Farinas, E.T.; Bulter, T.; Arnold, F.H. Directed enzyme evolution. Curr. Opin. Biotechnol. 2001, 12, 545-551.
12. Jaeger, K.-E.; Reetz, M.T. Directed evolution of enantioselective enzymes for organic chemistry. Curr. Opin. Chem. Biol. 2000, 4, 68-73.
13. Jaeger, K.-E.; Reetz, M.T. Microbial lipases form versatile tools for biotechnology. Trends Biotechnol. 1998, 16, 396-403.
14. Magnusson, A.; Hult, K.; Holmquist, M. Creation of an enantioselective hydrolase by engineered substrate-assisted catalysis. J. Am. Chem. Soc. 2001, 123, 4354-4355.
15. Svendsen, A. Lipase protein engineering. Biochim. Biophys. Acta 2000, 1543, 223-238.
16. Kovac, A.; Scheib, H.; Pleiss, J.; Schmid, R.D.; Paltauf, F. Molecular basis of lipase stereoselectivity. Eur. J. Lipid Sci. Technol. 2000, 102, 61-77.
17. Therisod, M.; Klibanov, A.M. Regioselective acylation of secondary hydroxyl groups in sugars catalyzed by lipases in organic solvents. J. Am. Chem. Soc. 1987, 109, 3977-3981.
18. Henne, W.J.; Sweers, H.M.; Wang, Y.-F.; Wong, C.-H. Enzymes in carbohydrate synthesis. Lipase-catalyzed selective acylation and deacylation of furanose and pyranose derivatives. J. Org. Chem. 1988, 53, 4939-4945.
19. Therisod, M.; Klibanov, A.M. Facile enzymatic preparation of monoacylated sugars in pyridine. J. Am. Chem. Soc. 1986, 108, 5638-5640.
20. Brocca, S.; Schmidt-Dannert, C.; Lotti, M.; Alberghina, L.; Schmid, R.D. Design, total synthesis and functional overexpression of the Candida rugosa lip1 gene coding for a major industrial lipase. Protein Sci. 1998, 7, 1415-1422.
21. Grochulski, P.; Li, Y.; Schrag, J.D.; Cygler, M. Two conformational states of Candida rugosa lipase. Protein Sci. 1994, 3, 82-91.
22. Grochulski, P.; Bouthilier, F.; Kazlauskas, R.J.; Serreqi, A.N.; Schrag, J.D.; Ziomek, E.; Cygler, M. Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase. Biochemistry 1994, 33, 3494-3500.
23. Manetti, F.; Mileto, D.; Corelli, F.; Soro, S.; Palocci, C.; Cernia, E.; D'Acquarica, I.; Lotti, M.; Alberghina, L.; Botta, M. Design and realization of a tailor-made enzyme to modify the molecular recognition of 2-arylpropionic esters by Candida rugosa lipase. Biochim. Biophys. Acta 2000, 1543/1, 146-158.
24. Sagt, C.M.J.; Mueller, W.H.; Boonstra, J.; Verkleij, A.J.; Verrips, C.T. Impaired secretion of a hydrophobic cutinase by Saccharomyces cerevisiae cells correlates with an increased association with immunoglobulin heavy-chain binding protein (BiP). Appl. Environ. Microbiol. 1998, 64, 316-324.
25. Brocca, S.; Secundo, F.; Ossola, M.; Alberghina, L.; Carrera, G.; Lotti, M. Sequence of the lid affects activity and specificity of Candida rugosa lipase isoenzymes. Prot. Sci., in press.
26. Degueil-Castaing, M.; DeJesco, B.; Drouillard, S.; Maillard, B. Enzyme reactions in organic synthesis: ester interchange of vinyl esters. Tetrahedron Lett. 1987, 28, 953-954.
27. McManus, D.A.; Vulfson, E.N. Substituent effects on the regioselectivity of enzymatic acylation of 6-O-alkylglycopyranosides using Pseudomonas cepacia lipase. Carbohydr. Res. 1995, 279, 281-291.
28. Panza, L.; Luisetti, M.; Crociati, E.; Riva, S. Selective acylation of 4,6-O-benzylideneglycopyranosides by enzymatic catalysis. J. Carbohydr. Chem. 1993, 12, 125-130.
29. Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 1970, 227, 680-685.
30. Bradford, M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
31. Douber-Osguthorpe, P.; Roberts, V.A.; Osguthorpe, D.J.; Wolff, J.; Genest, A.T.; Hagler, A.T. Structure and energetics of ligand binding to proteins: E. coli dihydrofolate reductase-trimethoprim, a drug-receptor system. Prot. Struct. Funct. Genet. 1988, 4, 31.