Loop Grafting of Bacillus subtilis Lipase A: Inversion of Enantioselectivity

Chemistry and Biology

Volumn 15, Issue 8, 2008, Pages 782-789

  Boersma, Ykelien L ^a   Pijning, Tjaard ^b   Bosma, Margriet S ^a   van der Sloot, Almer M ^c   Godinho, Luís F ^a   Dröge, Melloney J ^d   Winter, Remko T ^a   van Pouderoyen, Gertie ^b   Dijkstra, Bauke W ^b   Quax, Wim J ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

^c CENTRE FOR GENOMIC REGULATION CRG   (Spain)

^d ABL BV   (Netherlands)

Author keywords

CHEMBIO; PROTEINS

Indexed keywords

ACETYLESTERASE; ACETYLXYLAN ESTERASE; CARBOXYLESTERASE; CUTINASE; TRIACYLGLYCEROL LIPASE;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS SUBTILIS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DIRECTED MOLECULAR EVOLUTION; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; MUTATION; PROTEIN CONFORMATION; PROTEIN ENGINEERING; STEREOISOMERISM;

ACETYLESTERASE; AMINO ACID SEQUENCE; BACILLUS SUBTILIS; BINDING SITES; CARBOXYLIC ESTER HYDROLASES; DIRECTED MOLECULAR EVOLUTION; LIPASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; PROTEIN ENGINEERING; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

BACILLUS SUBTILIS; FUSARIUM SOLANI; PENICILLIUM PURPUROGENUM;

EID: 49449092589     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2008.06.009     Document Type: Article

References (38)

1. Akoh C.C., Lee G.-C., and Shaw J.-F. Protein engineering and applications of Candida rugosa lipase isoforms. Lipids 39 (2004) 513-526
2. Arnold K., Bordoli L., Kopp J., and Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22 (2006) 195-201
3. Beisson F., Tiss A., Rivière C., and Verger R. Methods for lipase detection and assay: a critical review. Eur. J. Lipid Sci. Technol. 102 (2000) 133-153
4. Blaser H.-U., Pugin B., and Spindler F. Progress in enantioselective catalysis assessed from an industrial point of view. J. Mol. Catal. Chem. 231 (2005) 1-20
5. Bloom J.D., Meyer M.M., Meinhold P., Otey C.R., MacMillan D., and Arnold F.H. Evolving strategies for enzyme engineering. Curr. Opin. Struct. Biol. 15 (2005) 447-452
6. Boersma Y.L., Dröge M.J., van der Sloot A.M., Pijning T., Cool R.H., Dijkstra B.W., and Quax W.J. A novel selection system for enantioselectivity of Bacillus subtilis lipase A based on bacterial growth. ChemBioChem 9 (2008) 1110-1115
7. Breuer M., Ditrich K., Habicher T., Hauer B., Kesseler M., Stürmer R., and Zelinski T. Industrial methods for the production of optically active intermediates. Angew. Chem. Int. Ed. Engl. 43 (2005) 788-824
8. Brocca S., Secundo F., Ossola M., Alberghina L., Carrea G., and Lotti M. Sequence of the lid affects activity and specificity of Candida rugosa lipase isoenzymes. Protein Sci. 12 (2003) 2312-2319
9. Carrière F., Thirstrup K., Hjorth S., Ferrato F., Nielsen P.F., Withers-Martinez C., Cambillau C., Boel E., Thim L., and Verger R. Pancreatic lipase structure-function relationships by domain exchange. Biochemistry 36 (1997) 239-248
10. Chen C.S., Fujimoto Y., Girdaukas G., and Sih C.J. Quantitative analyses of biochemical kinetic resolutions of enantiomers. J. Am. Chem. Soc. 109 (1982) 7294-7299
11. Dartois V., Baulard A., Schanck K., and Colson C. Cloning, nucleotide sequence and expression in Escherichia coli of a lipase gene from Bacillus subtilis 168. Biochim. Biophys. Acta 1131 (1992) 253-260
12. Dartois V., Coppée J.Y., Colson C., and Baulard A. Genetic analysis and overexpression of lipolytic activity in Bacillus subtilis. Appl. Environ. Microbiol. 60 (1994) 1670-1673
13. Dröge M.J., Bos R., Woerdenbag H.J., and Quax W.J. Chiral gas chromatography for the determination of 1,2-O-isopropylidene-sn-glycerol stereoisomers. J. Sep. Sci. 26 (2003) 1-6
14. Dröge M.J., Rüggeberg C.J., van der Sloot A.M., Schimmel J., Dijkstra D.S., Verhaert R.M.D., Reetz M.T., and Quax W.J. Binding of phage displayed Bacillus subtilis lipase A to a phosphonate suicide inhibitor. J. Biotechnol. 101 (2003) 19-28
15. Dröge M.J., Boersma Y.L., Van Pouderoyen G., Vrenken T.E., Rüggeberg C.J., Reetz M.T., Dijkstra B.W., and Quax W.J. Directed evolution of Bacillus subtilis Lipase A by use of enantiomeric phosphonate inhibitors: crystal structures and phage display selection. ChemBioChem 7 (2006) 149-157
16. Dugi K.A., Dichek H.L., and Santamarina-Fojo S. Human hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity. J. Biol. Chem. 270 (1995) 25396-25401
17. Eggert T., Leggewie C., Puls M., Streit W., Van Pouderoyen G., Dijkstra B.W., and Jaeger K.-E. Novel biocatalysts by identification and design. Biocatal. Biotransform. 22 (2004) 139-144
18. Eggert T., Funke S.A., Rao N.M., Acharya P., Krumm H., Reetz M.T., and Jaeger K.-E. Multiplex-PCR-based recombination as a novel high-fidelity method for directed evolution. ChemBioChem 6 (2005) 1062-1067
19. Ghosh D., Erman M., Sawicki M., Lala P., Weeks D.R., Li N., Pangborn W., Thiel D.J., Jörnvall H., Gutierrez R., and Eyzaguirre J. Determination of a protein structure by iodination: the structure of iodinated acetylxylan esterase. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 779-784
20. Grunberg R., Nilges M., and Leckner J. Biskit-a software platform for structural bioinformatics. Bioinformatics 23 (2007) 769-770
21. Holmquist M. α/β hydrolase fold enzymes: structures, functions and mechanisms. Curr. Protein Pept. Sci. 1 (2000) 209-235
22. Holmquist M., and Berglund P. Creation of a synthetically useful lipase with higher than wild-type enantioselectivity and maintained catalytic activity. Org. Lett. 1 (1999) 763-765
23. Krissinel E., and Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60 (2005) 2256-2268
24. Lesuisse E., Schanck K., and 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
25. Longhi S., Czjzek M., Lamzin V., Nicolas A., and Cambillau C. Atomic resolution (1.0 Å) crystal structure of Fusarium solani cutinase: stereochemical analysis. J. Mol. Biol. 268 (1997) 779-799
26. Martinez C., De Geus P., Lauwereys M., Matthyssens M., and Cambillau C. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature 356 (1992) 615-618
27. Nardini M., and Dijkstra B.W. [α]/[β] Hydrolase fold enzymes: the family keeps growing. Curr. Opin. Struct. Biol. 9 (1999) 732-737
28. O'Sullivan O., Suhre K., Abergel C., Higgins D.G., and Notredame C. 3DCoffee: combining protein sequences and structures within multiple sequence alignments. J. Mol. Biol. 340 (2004) 385-395
29. Reetz M.T. Controlling the enantioselectivity of enzymes by directed evolution: practical and theoretical ramifications. Proc. Natl. Acad. Sci. USA 101 (2004) 5716-5722
30. Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
31. Sambrook J., Fritsch E.F., and Maniatis T. Molecular Cloning: A Laboratory Manual (1989), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
32. Santarossa G., Lafranconi P.G., Alquati C., DeGioia L., Alberghina L., Fantucci P., and Lotti M. Mutations in the "lid" region affect chain length specificity and thermostability of a Pseudomonas fragi lipase. FEBS Lett. 579 (2005) 2383-2386
33. Schmid A., Dordick J.S., Hauer B., Kiener A., Wubbolts M., and Witholt B. Industrial biocatalysis today and tomorrow. Nature 409 (2001) 258-268
34. Secundo F., Carrea G., Tarabiono C., Brocca S., and Lotti M. Activity and enantioselectivity of wildtype and lid mutated Candida rugosa lipase isoform 1 in organic solvents. Biotechnol. Bioeng. 86 (2004) 236-240
35. Seizaburo S., Masaji I., Harukazu F., Masahiro N., and Mitsuyoshi U. Creation of Rhizopus oryzae lipase having a unique oxyanion hole by combinatorial mutagenesis in the lid domain. Appl. Microbiol. Biotechnol. 68 (2005) 779-785
36. Van Pouderoyen G., Eggert T., Jaeger K.-E., and Dijkstra B.W. The crystal structure of Bacillus subtilis Lipase: a minimal α/β hydrolase fold enzyme. J. Mol. Biol. 309 (2001) 215-226
37. Verger R. 'Interfacial activation' of lipases: facts and artifacts. Trends Biotechnol. 15 (1997) 32-38
38. Zhao H., Chockalingam K., and Chen Z. Directed evolution of enzymes and pathways for industrial biocatalysis. Curr. Opin. Biotechnol. 13 (2002) 104-110