Cold-active esterase from Psychrobacter sp. Ant300: Gene cloning, characterization, and the effects of Gly→Pro substitution near the active site on its catalytic activity and stability

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1696, Issue 1, 2004, Pages 59-65

  Kulakova, Ljudmila ^a   Galkin, Andrey ^a   Nakayama, Toru ^b   Nishino, Tokuzo ^b   Esaki, Nobuyoshi ^a  

^a KYOTO UNIVERSITY   (Japan)

^b TOHOKU UNIVERSITY   (Japan)

Author keywords

Esterase; Psychrobacter sp.; Substitution

Indexed keywords

ESTERASE; TRIACYLGLYCEROL LIPASE;

ARTICLE; CATALYSIS; CHEMICAL STRUCTURE; CONTROLLED STUDY; ENERGY TRANSFER; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE MUTATION; GENETIC CODE; GENETIC TRAIT; LOW TEMPERATURE; MOLECULAR CLONING; NONHUMAN; PREDICTION; PRIORITY JOURNAL; THERMAL ANALYSIS; WILD TYPE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PSYCHROBACTER SP.; PSYCHROBACTER SP. ANT300;

EID: 1242284208     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2003.09.008     Document Type: Article

References (31)

1. Feller G., Gerday C. Psychrophilic enzymes - molecular basis of cold adaptation. Cell. Mol. Life Sci. 53:1997;830-841.
2. Feller G., Narinx E., Arpigny J.L., Aittaleb M., Baise E., Genicot S., Gerday C. Enzymes from psychrophilic organisms. FEMS Microbiol. Rev. 18:1996;189-202.
3. Gerday C., Aittaleb M., Bentahir M., Chessa J.P., Claverie P., Collins T., D'Amico S., Dumont J., Garsoux G., Georlette D., Hoyoux A., Lonhienne T., Meuwis M.A., Feller G. Cold-adapted enzymes: from fundamentals to biotechnology. Trends Biotechnol. 18:2000;103-107.
4. Galkin A., Kulakova L., Nakayama T., Nishino T., Esaki N. Cold-active enzymes from cold-adapted microorganisms: their possible applications and structural relationships with mesophilic and thermophilic counterparts. Fingerman M., Ragabhushanam N. Recent Advances in Marine Biotechnology. 2003;1-27 Science Publishers, Enfield, NH, USA.
5. Gerday C., Aittaleb M., Arpigny J.L., Baise E., Chessa J.-P., Garsoux G., Petrescu I., Feller G. Psychrophilic enzymes: a thermodynamic challenge. Biochim. Biophys. Acta. 1342:1997;119-131.
6. Lonhienne T., Gerday C., Feller G. Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim. Biophys. Acta. 1543:2000;1-10.
7. Kulakova L., Galkin A., Nakayama T., Nishino T., Esaki N. Improvement of thermostability of cold-active serine alkaline protease from the psychrotrophic bacterium Schewanella sp. strain Ac10 by rational mutagenesis. J. Mol. Catal., B Enzym. 22:2003;113-117.
8. Kim S.Y., Hwang K.Y., Kim S.H., Sung H.C., Han Y.S., Cho Y. Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase a psychrophile Aquaspirillium arcticum. J. Biol. Chem. 274:1999;11761-11767.
9. D'Amico S., Marx J.C., Gerday C., Feller G. Activity-stability relationship in extremophilic enzymes. J. Biol. Chem. 278:2003;7891-7896.
10. Collins T., Meuwis M.A., Gerday C., Feller G. Activity stability and flexibility in glycosidases adapted to extreme thermal environments. J. Mol. Biol. 328:2003;419-428.
11. Georlette D., Damien B., Blaise V., Depiereux E., Uversky V.N., Gerday C., Feller G. Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic and thermophilic DNA ligases. J. Biol. Chem. 278:2003;37015-37023.
12. Herbert R.A. The perspective on the biotechnological potential of extremophiles. Trends Biotechnol. 10:1992;395-402.
13. Feller G., Thiry M., Arpigny J.L., Gerday C. Nucleotide sequence of the lipase gene Lip2 from the antarctic psychrotrophic Moraxella TA144 and site-specific mutagenesis of the conserved serine and histidine resides. DNA Cell Biol. 10:1991;381-388.
14. Choo D.W., Kurihara T., Suzuki T., Soda K., Esaki N. A cold-adapted lipase of an Alaskan psychrotroph, Pseudomonas sp. strain B11-1: gene cloning and enzyme purification and characterizatio. Appl. Environ. Microbiol. 64:1998;486-491.
15. Suzuki T., Nakayama T., Choo D.W., Hirano Y., Kurihara T., Nishino T., Esaki N. Cloning, heterologous expression, renaturation, and characterization of a cold-adapted esterase with unique primary structure from a psychrotroph Pseudomonas sp. strain B11-1. Protein Expr. Purif. 30:2003;171-178.
16. Suzuki T., Nakayama T., Kurihara T., Nishino T., Esaki N. Cold-active lipolytic activity of psychrotrophic Acinetobacter sp. strain no. 6. J. Biosci. Bioeng. 92:2001;144-148.
17. Suzuki T., Nakayama T., Kurihara T., Nishino T., Esaki N. A cold-active esterase with a substrate preference for vinyl esters from a psychrotroph, Acinetobacter sp. strain no. 6: gene cloning, purification, and characterization. J. Mol. Catal., B Enzym. 16:2002;255-263.
18. Suzuki T., Nakayama T., Kurihara T., Nishino T., Esaki N. Primary structure and catalytic properties of a cold-active esterase from a psychrotroph, Acinetobacter sp. strain no. 6 isolated from Siberian soil. Biosci. Biotechnol. Biochem. 66:2002;1682-1690.
19. Hemilä H., Koivula T.T., Palva I. Hormone-sensitive lipase is closely related several bacterial proteins, and distantly related to acetylcholinesterase and lipoprotein lipase: identification of a superfamily of esterases and lipases. Biochim. Biophys. Acta. 120:1994;249-253.
20. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: A Laboratory Manual. 2nd ed. 1989;1.1-1.110 Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
21. Saito H., Miura K. Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim. Biophys. Acta. 72:1963;619-629.
22. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
23. Wei Y., Contreras J.A., Sheffield P., Osterlund T., Derewenda U., Kneusel R.E., Matern U., Holm C., Derewenda Z.S. Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase. Nat. Struct. Biol. 6:1999;340-345.
24. Nardini M., Dijkstra B.W. α/β Hydrolase fold enzymes: the family keeps growing. Curr. Opin. Struct. Biol. 9:1999;732-737.
25. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
26. Kanaya S., Koyanagi T., Kanaya E. An esterase from Escherichia coli with a sequence similarity to hormone-sensitive lipase. Biochem. J. 332:1998;75-80.
27. Manco G., Adinolfi E., Pisani F.M., Ottolina G., Carrea G., Rossi M. Overexpression and properties of a new thermophilic and thermostable esterase from Bacillus acidocaldarius with sequence similarity to hormone-sensitive lipase family. Biochem. J. 332:1998;203-212.
28. Hochachka P., Lewis J. Enzyme variants in thermal acclimation. Trout liver citrate synthases. J. Biol. Chem. 245:1970;6567-6573.
29. Baldwin J., Hochachka P. Functional significance of isoenzymes in thermal acclimatization. Biochem. J. 116:1970;883-887.
30. Matthews B.W., Nicholson H., Becktel W.J. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. Natl. Acad. Sci. U. S. A. 84:1987;6663-6667.
31. Watanabe K., Chishiro K., Kitamura K., Suzuki Y. Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006. J. Biol. Chem. 266:1991;24287-24294.