The SGNH-hydrolase of Streptomyces coelicolor has (aryl)esterase and a true lipase activity

Biochimie

Volumn 91, Issue 3, 2009, Pages 390-400

  Bielen, Ana ^a,b   Ćetković, Helena ^a   Long, Paul F ^c   Schwab, Helmut ^d   Abramić, Marija ^a   Vujaklija, Dušica ^a  

^a RUDER BO KOVI INSTITUTE   (Croatia)

^b UNIVERSITY OF ZAGREB   (Croatia)

^c UNIVERSITY OF LONDON   (United Kingdom)

^d GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

Author keywords

(Aryl)esterase; GDSL SGNH family; Lipase; Streptomyces coelicolor

Indexed keywords

CLONING, MOLECULAR; COMPUTATIONAL BIOLOGY; DNA, BACTERIAL; ESTERASES; GENES, BACTERIAL; HYDROGEN-ION CONCENTRATION; HYDROLASES; KINETICS; LIPASE; PHYLOGENY; PLASMIDS; SEQUENCE ANALYSIS, DNA; SEQUENCE ANALYSIS, PROTEIN; STREPTOMYCES COELICOLOR; SUBSTRATE SPECIFICITY; TEMPERATURE;

ACTINOMYCETALES; ASCOMYCOTA; NEMATODA; STREPTOMYCES COELICOLOR; STREPTOMYCES LIVIDANS;

EID: 60249097583     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2008.10.018     Document Type: Article

References (54)

1. Sharma R., Chisti Y., and Banerjee U.C. Production, purification, characterization, and applications of lipases. Biotechnol. Advances 19 (2001) 627-662
2. Arpigny J.L., and Jaeger K.-E. Bacterial lipolytic enzymes: classification and properties. Biochem. J. 343 (1999) 177-183
3. Upton C., and Buckley J.T. A new family of lipolytic enzymes?. Trends. Biochem. Sci. 20 (1995) 178-179
4. Molgaard A., Kauppinen S., and Larsen S. Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases. Structure. Fold. Des. 8 (2000) 373-383
5. Akoh C.C., Lee G.-C., Liaw Y.-C., Huang T.-H., and Shaw J.-F. GDSL family of serine esterases/lipases. Prog. Lipid. Res. 43 (2004) 534-552
6. Koshland D.E. Application of a theory of enzyme specificity to protein synthesis (in symposium on aminoacid activation). Proc. Natl. Acad. Sci. U S A 44 (1958) 98-104
7. Sztajer H., Maliszewska I., and Wieczorek J. Production of exogeneous lipases by bacteria, fungi, and actinomycetes. Enzyme. Microb. Technol. 10 (1988) 492-497
8. Gandolfi R., Marinelli F., Lazzarini A., and Molinari F. Cell-bound and extracellular carboxylesterases from Streptomyces: hydrolytic and synthetic activities. J. Appl. Microbiol. 89 (2001) 870-875
9. Pérez C., Juárez K., García-Castells E., Soberón G., and Servín-González L. Cloning, characterization, and expression in Streptomyces lividans 66 of an extracellular lipase-encoding gene from Streptomyces sp. M11. Gene 123 (1993) 109-114
10. Cruz H., Pérez C., Wellington E., Castro C., and Servín-González L. Sequence of the Streptomyces albus G lipase-encoding gene reveals the presence of a prokaryotic lipase family. Gene 144 (1994) 141-142
11. Valdez F., González-Cerón G., Kieser H.M., and Servín-González L. The Streptomyces coelicolor A3(2) lipAR operon encodes an extracellular lipase and a new type of transcriptional regulator. Microbiologica 145 (1999) 2365-2374
12. Sommer P., Bormann C., and Gotz F. Genetic and biochemical characterization of a new extracellular lipase from Streptomyces cinnamomeus. Appl. Environ. Microbiol. 63 (1997) 3553-3560
13. Vujaklija D., Schröder W., Abramić M., et al. A novel streptomycete lipase: cloning, sequencing and high-level expression of the Streptomyces rimosus GDS(L)-lipase gene. Arch. Microbiol. 178 (2002) 124-130
14. Abramić M., Leščić I., Korica T., Vitale Lj., Saenger W., and Pigac J. Purification and properties of extracellular lipase from Streptomyces rimosus. Enzyme. Microb. Technol. 25 (1999) 522-529
15. Leščić I., Vukelić B., Majerić-Elenkov M., Saenger W., and Abramić M. Substrate specificity and effects of water-miscible solvents on the activity and stability of extracellular lipase from Streptomyces rimosus. Enzyme. Microb. Technol. 29 (2001) 548-553
16. Vujaklija D., Abramić M., Leščić I., Maršić T., and Pigac J. Streptomyces rimosus GDS(L) lipase: production, heterologous overexpression and structure-stability relationship. Food Technol. Biotechnol. 41 (2003) 89-93
17. Zehl M., Leščić I., Abramić M., Rizzi A., Kojić-Prodić B., and Allmaier G. Characterization of covalently inhibited extracellular lipase from Streptomyces rimosus by matrix-assisted laser desorption/ionization time-of-flight and matrix-assisted laser desorption/ionization quadrupole ion trap reflectron time-of-flight mass spectrometry: localization of the active site serine. J. Spectrom. 39 (2004) 1474-1483
18. Leščić Ašler I., Zehl M., Kovačić F., et al. Mass spectrometric evidence of covalently-bound tetrahydrolipstatin at the catalytic serine of Streptomyces rimosus lipase. Biochim. Biophys. Acta. 1770 (2007) 163-170
19. Bentley S.D., Chater K.F., Cerdeño-Tárraga A.M., et al. Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature 417 (2002) 141-147
20. Ōmura S., Ikeda H., Ishikawa J., et al. Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites. Proc. Natl. Acad. Sci. U S A 98 (2001) 12215-12220
21. Ohnishi Y., Ishikawa J., Hara H., et al. Genome sequence of the streptomycin-producing microorganism Streptomyces griseus IFO 13350. J. Bacteriol. 190 (2008) 4050-4060
22. Côté A., and Shareck F. Cloning, purification and characterization of two lipases from Streptomyces coelicolor A3(2). Enzyme. Microb. Technol. 42 (2008) 381-388
23. DeSanti C.L., and Strohl W.R. Characterization of the Streptomyces sp. Strain C5 snp locus and development of snp-derived expression vectors. Appl. Environ. Microbiol. 69 (2003) 1647-1654
24. Sambrook J., Fritsch E.F., and Maniatis T. Molecular Cloning - A Laboratory Manual. second ed. (1989), Cold Spring Harbor Laboratory Press, New York
25. Kieser T., Bibb M.J., Buttner M.J., Chater K.F., and Hopwood D.A. Practical Streptomyces Genetics (2000), The John Innes Foundation, Norwich
26. Redenbach M., Kieser H.M., Denapaite D., et al. A set of ordered cosmids and a detailed genetic and physical map for the 8 Mb Streptomyces coelicolor A3(2) chromosome. Mol. Microbiol. 21 (1996) 77-96
27. Altschul S.F., Madden T.L., Schäffer A.A., Zhang J., Zhang Z., Millerand W., and Lipman D.J. Gapped Blast and PSI-BLAST: a new generation of protein database search programs. Nucleic. Acids. Res. 25 (1997) 3389-3402
28. Larkin M.A., Blackshields G., Brown N.P., et al. ClustalW and ClustalX version 2. Bioinformatics 23 (2007) 2947-2948
29. Nicholas K.B., Nicholas H.B.J., and Deerfield D.W. GeneDoc: analysis and visualization of genetic variation. Available from: (1997). http://www.cris.com/Ketchup/genedoc.html [accessed 03.07.08]
30. Page R.D.M. Treeview: an application to display phylogenetic trees on personal computers. Comput. Appl. Biosci. 12 (1996) 357-358
31. Nielsen H., Engelbrecht J., Brunak S., and von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein. Eng. 10 (1997) 1-6
32. Bendtsen J.D., Nielsen H., von Heijne G., and Brunak S. Improved prediction of signal peptides: signal P 3.0. J. Mol. Biol. 340 (2004) 783-795
33. Unniraman S., Prakash R., and Nagaraja V. Conserved economics of transcription termination in eubacteria. Nucleic. Acids. Res. 30 (2002) 675-684
34. Rutherford K., Parkhill J., Crook J., et al. Artemis: sequence visualization and annotation. Bioinformatics 16 (2000) 944-945
35. Winkler U.K., and Stuckmann M. Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serrratia marescens. J. Bacteriol. 138 (1979) 663-670
36. Reiter B., Glieder A., Talker D., and Schwab H. Cloning and characterization of EstC from Bulkolderia gladioli, a novel-type esterase related to plant enzymes. Appl. Microbiol. Biotechnol. 54 (2000) 778-785
37. Hempelmann E., and Kaminsky R. Long-term stabilility of colors after silver staining. Electrophoresis 7 (1986) 481
38. Whitmore L., and Wallace B.A. Dichroweb: an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic. Acids. Res. 32 (2004) 668-673
39. Gravius B., Bezmalinović T., Hranueli D., and Cullum J. Genetic instability and strain degeneration in Streptomyces rimosus. Appl. Environ. Microbiol. 59 (1993) 2220-2228
40. Strohl W.R. Compilation and analysis of DNA sequences associated with apparent streptomycete promoters. Nucleic. Acids. Res. 20 (1992) 961-974
41. Ahel I., Vujaklija D., Mikoč A., and Gamulin V. Transcriptional analysis of the recA gene in Streptomyces rimosus: identification of the new type of promoter. FEMS. Microbiol. Lett. 209 (2002) 133-137
42. Bourn W.R., and Babb B. Computer assisted identification and classification of streptomycete promoters. Nucleic. Acids. Res. 23 (1995) 3696-3703
43. Laing E., Mersinias V., Smith C.P., and Hubbard S.J. Analysis of gene expression in operons of Streptomyces coelicolor. Genome. Biol. 7 (2006) R46
44. Marga F., Ghakis C., Dupont C., Morosoli R., and Kluepfel D. Improved production of mannanase by Streptomyces lividans. Appl. Environ. Microbiol. 62 (1996) 4656-4658
45. Servin-Gonzales L., Castro C., Perez C., Rubio M., and Valdez F. bldA-Dependent expression of the Streptomyces exfoliatus M11 lipase gene (lipA) is mediated by the product of a contiguous gene, lipR, encoding a putative transcriptional activator. J. Bacteriol. 179 (1997) 7816-7826
46. Horinouchi S. A microbial hormone, A-factor, as a master switch for morphological differentiation and secondary metabolism in Streptomyces griseus. Front. Biosci. 7 (2002) 2045-2057
47. Leščić I., Zehl M., Müller R., et al. Structural characterization of extracellular lipase from Streptomyces rimosus: assignment of disulfide bridge pattern by mass spectrometry. Biol. Chem. 385 (2004) 1147-1156
48. Werten M.W.T., Wisselink W.T., Jansen-van den Bosch T.J., de Bruin E.C., and de Wolf F.A. Secreted production of a custom-designed, highly hydrophilic gelatin in Pichia pastoris. Protein. Eng. 14 (2001) 447-454
49. Carson M., Johnson D.H., McDonald H., Brouillette C., and Delucas L.J. His-tag impact on structure. Acta. Crystallogr. D. Biol. Crystallogr. 63 (2007) 295-301
50. + synthetase from Bacillus anthracis. Acta. Crystallogr. 63 (2007) 891-905
51. Lee Y.L., Su M.S., Huang T.H., and Shaw J.F. C-terminal His-tagging results in substrate specificity changes of the thioesterase I from Escherichia coli. J. Am. Oil. Chem. Soc. 76 (1999) 1113-1118
52. Lee Y.L., Chang R.C., and Shaw J.F. Facile purification of a C-terminal extended His-tagged Vibrio mimicus arylesterase and characterization of the purified enzyme. J. Am. Oil. Chem. Soc. 74 (1997) 1371-1376
53. K-Jaeger E., Dijkstra B.W., and Reetz M.T. Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu. Rev. Mibrobiol. 53 (1999) 315-351
54. Klibanov A.M. Improving enzymes by using them in organic solvents. Nature 409 (2001) 241-246