Characterization of a extreme thermostable fructose-1,6-bisphosphate aldolase from hyperthermophilic bacterium Aquifex aeolicus

Enzyme and Microbial Technology

Volumn 45, Issue 4, 2009, Pages 261-266

  La, Im Joung ^a   Eum, Da Young ^a   Gedi, Vinayakumar ^a   Kim, Jinheung ^b   Jeong, Byeongmoon ^b   Yoon, Moon Young ^a  

^a Hanyang University   (South Korea)

^b Ewha Womans University   (South Korea)

Author keywords

Aquifex aeolicus; Circular dichroism; Class II aldolase; Hyperthermophile; Thermostability

Indexed keywords

AQUIFEX AEOLICUS; CIRCULAR DICHROISM; CLASS II ALDOLASE; HYPERTHERMOPHILE; THERMOSTABILITY;

ACETONITRILE; CHARACTERIZATION; CHROMATOGRAPHIC ANALYSIS; CONDENSATION REACTIONS; DICHROISM; ENZYMES; ESCHERICHIA COLI; ETHERS; FRUCTOSE; GEL PERMEATION CHROMATOGRAPHY; GELATION; INDUSTRIAL APPLICATIONS; METHANOL; PURIFICATION;

ORGANIC SOLVENTS;

2 PROPANOL; ACETONITRILE; AMMONIA; COBALT; FRUCTOSE 1,6 BISPHOSPHATE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLYCERALDEHYDE 3 PHOSPHATE; ORGANIC SOLVENT; PHOSPHATE; RECOMBINANT PROTEIN;

AQUIFEX AEOLICUS; ARTICLE; BIOCATALYST; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME STABILITY; ESCHERICHIA COLI; GENE OVEREXPRESSION; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; TEMPERATURE; THERMOSTABILITY;

AQUIFEX AEOLICUS; BACTERIA (MICROORGANISMS);

EID: 68349157652     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2009.06.012     Document Type: Article

References (28)

1. Mu Y., and Gibbs R.A. Design and synthesis of chiral and racemic phosphonate-based haptens for the induction of aldolase catalytic antibodies. Bioorg Med Chem 5 (1997) 1327-1337
2. Morse D.E., and Horecker B.L. The mechanism of action of aldolases. Adv Enzymol Relat Areas Mol Biol 31 (1968) 125-181
3. Rutter W.J. Evolution of aldolase. Fed Proc 23 (1964) 1248-1257
4. Siebers B., Brinkmann H., Dorr C., Tjaden B., Liliei H., Oost J., et al. Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolase. J Biol Chem 271 (2001) 28710-28718
5. Sauve V., and Sygusch J. Molecular cloning, expression, purification, and characterization of fructose-1,6-bisphosphate aldolase from Thermus aquaticus. Prot Expr Purif 21 (2001) 293-302
6. Plaumann M., Pelzer-Reith B., Martin W.F., and Schnarrenberger C. Multiple recruitment of class-I aldolase to chloroplasts and eubacterial origin of eukaryotic class-II aldolases revealed by cDNAs from Euglena gracilis. Curr Genet 31 (1997) 430-438
7. Thomson G.J., Howlett G.J., Ashcroft A.E., and Berry A. The dhn A gene of Escherichia coli encodes a class I fructose bisphosphate aldolase. Biochem J 331 (1998) 437-445
8. Vonder Osten C.H., Barbas C.F.D., Wong C.H., and Sinskey A.J. Molecular cloning, nucleotide sequence and fine-structural analysis of the Corynebacterium glutamicum fda gene: structural comparison of C. glutamicum fructose-1,6-bisphosphate aldolase to class I and class II aldolases. Mol Microbiol 3 (1989) 1625-1637
9. Franck C., Philippe D., Virgil H., Soth S., and Laurence H. Chemoenzymatic synthesis of 5-thio-d-xylopyranose. Eur J Org Chem 24 (2006) 5526-5532
10. Lahssen El B., Mustapha A., Jean B., and Marielle L. Straightforward chemo-enzymatic synthesis of new aminocyclitols, analogues of valiolamine and their evaluation as glycosidase inhibitors. Tetrahedron: Asymm 17 (2006) 2684-2688
11. Niehaus F., Bertoldo C., Kahler M., and Antranikian G. Extremophiles as a source of novel enzymes for industrial application. Appl Microbiol Biotechnol 51 (1999) 711-729
12. Leuschner C., and Antranikian G. Heat-stable enzymes from extremely thermophilic and hyperthermophilic microorganisms. World J Microbiol Biotechnol 11 (1995) 95-114
13. Pouwels J. Activity and stability of hyperthermophilic enzymes: a comparative study on two archaeal β-glycosidases. Extremophiles 4 (2000) 157-164
14. Montigny D.E., and Sygusch C.J. Functional characterization of an extreme thermophilic class II fructose-1,6-bisphosphate aldolase. Eur J Biochem 241 (1996) 243-248
15. Ertunga N.S., Colak A., Belduz A.O., Canakci S., Karaoglu H., and Sandalli C. Cloning, expression, purification and characterization of fructose-1,6-bisphosphate aldolase from Anoxybacillus gonensis G2. J Biochem 141 (2007) 817-825
16. Howard R.L., and Becker R.R. Substrate inactivation of fructose-1,6-diphosphate aldolase from Bacillus stearothermophilus. Biochim Biophys Acta 268 (1972) 249-252
17. Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., et al. The complete genome of the hyperthermophilic bacterium Aquifex aeolicus. Nature 392 (1998) 353-358
18. Woese C.R., Kandler O., and Whellis M.L. Towards a natural system of organisms: proposal for the domains archaea, bacteria, and eucarya. Proc Natl Acad Sci USA 87 (1990) 4576-4579
19. Berry A., and Marshall K.E. Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli. FEBS Lett 318 (1993) 11-16
20. Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acid Res 22 (1994) 4673-4680
21. Hill H.A., Lobb R.R., Sharp S.L., Stokes A.M., Harris J.I., and Jack R.S. Metal-replacement studies in Bacillus stearothermophilus aldolase and a comparison of the mechanisms of class I and class II aldolases. Biochem J 153 (1976) 551-560
22. Freeze H., and Brock T.D. Thermostable aldolase from Thermus aquaticus. J Bacteriol 101 (1970) 541-550
23. Plater A.R., Zgiby S.M., Thomson G.J., Qamar S., Wharton C.W., and Berry A. Conserved residues in the mechanism of the Escherichia coli class II FBP-aldolase. J Mol Biol 285 (1999) 843-855
24. Vieille C., and Zeikus G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65 (2001) 1-43
25. Facchiano A.M., Colonna G., and Ragone R. Helix stabilizing factors and stabilization of thermophilic proteins: an X-ray based study. Prot Eng 11 (1998) 753-760
26. Choi I.G., Cho C.S., Cho Y., and Yu Y.G. Overproduction, purification, and characterization of heat stable aldolase from Methanococcus jannaschii, a hyperthermophic archaea. J Biochem Mol Biol 31 (1998) 130-134
27. Hao J., and Berry A. A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents. Prot Eng Des Sel 17 (2004) 689-697
28. Hall D.R., Leonard G.A., Reed C.D., Watt C.I., Berry A., and Hunter W.N. The crystal structure of Escherchia coli class II fructose-1,6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity. J Mol Biol 287 (1999) 383-394