Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus

Biochemical and Biophysical Research Communications

Volumn 347, Issue 3, 2006, Pages 616-625

  Lee, Jun Hyuck ^a   Bae, Jungdon ^b,c   Kim, Dooil ^b,c   Choi, Yongseok ^b   Im, Young Jun ^a   Koh, Sukhoon ^b   Kim, Joong Su ^b   Kim, Mun Kyoung ^a   Kang, Gil Bu ^a   Hong, Suk In ^c   Lee, Dae Sil ^b   Eom, Soo Hyun ^a  

^a Gwangju Institute of Science and Technology (GIST)   (South Korea)

^b Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^c Korea University   (South Korea)

Author keywords

Crystal structure; Fructose 1,6 bisphosphate aldolase; Stereoselectivity; Tagatose 1,6 bisphosphate aldolase

Indexed keywords

ENZYME; FRUCTOSE BISPHOSPHATE ALDOLASE; HYDROXAMIC ACID DERIVATIVE; PHOSPHOGLYCOLOHYDROXAMATE; TAGATOSE 1,6 DIPHOSPHATE ALDOLASE; UNCLASSIFIED DRUG;

ARTICLE; CONCENTRATION (PARAMETERS); CRYSTAL STRUCTURE; ENZYME ANALYSIS; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; STEREOCHEMISTRY; THERMUS CALDOPHILUS; X RAY CRYSTALLOGRAPHY;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; FRUCTOSE-BISPHOSPHATE ALDOLASE; FRUCTOSEDIPHOSPHATES; HEXOSEDIPHOSPHATES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, AMINO ACID; SEQUENCE ALIGNMENT; STEREOISOMERISM; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY; THERMUS;

ESCHERICHIA COLI; THERMUS CALDOPHILUS;

EID: 33746210081     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.06.139     Document Type: Article

References (41)

1. Machajewski T.D., and Wong C.H. The catalytic asymmetric aldol reaction. Angrew Chem. Int. Ed. 39 (2000) 1352-1374
2. Fessner W.D., and Helaine V. Biocatalytic synthesis of hydroxylated natural products using aldolases and related enzymes. Curr. Opin. Biotechnol. 12 (2001) 574-586
3. Breuer M., and Hauer B. Carbon-carbon coupling in biotransformation. Curr. Opin. Biotechnol. 14 (2003) 570-576
4. Schoevaart R., Van Rantwijk F., and Sheldon R.A. A four-step enzymatic cascade for the one-pot synthesis of non-natural carbohydrates from glycerol. J. Org. Chem. 65 (2000) 6940-6943
5. Sanchez-Moreno I., Garcia-Garcia J.F., Bastida A., and Garcia-Junceda E. Multienzyme system for dihydroxyacetone phosphate-dependent aldolase catalyzed C-C bond formation from dihydroxyacetone. Chem. Commun. (2004) 1634-1635
6. Dalby A., Dauter Z., and Littlechild J.A. Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications. Protein Sci. 8 (1999) 291-297
7. Gamblin S.J., Davies G.J., Grimes J.M., Jackson R.M., Littlechild J.A., and Watson H.C. Activity and specificity of human aldolases. J. Mol. Biol. 219 (1991) 573-576
8. Hester G., Holzach O.B., Rossi F.A., Donatz M.S., Winterhalter K.H., Smit J.D., and Piontek K. The crystal structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster at 2.5 Å resolution. FEBS Lett. 292 (1991) 237-242
9. Sygusch J., Beaudry D., and Allaire M. Molecular architecture of rabbit skeletal muscle aldolase at 2.7 Å resolution. Proc. Natl. Acad. Sci. USA 84 (1987) 7846-7850
10. Zhang R., Villeret V., Lipscomb W.N., and Fromm H.J. Kinetics and mechanisms of activation and inhibition of porcine liver fructose-1,6-bisphosphatase by monovalent cations. Biochemistry 35 (1996) 3038-3043
11. Blom N.S., and Sygusch J. Product binding and role of the C-terminal region in class I d-fructose 1,6-bisphosphate aldolase. Nat. Struct. Biol. 4 (1997) 36-39
12. Kim H., Certa U., Dobeli H., Jakob P., and Hol W.G. Crystal structure of fructose-1,6-bisphosphate aldolase from the human malaria parasite Plasmodium falciparum. Biochemistry 37 (1998) 4388-4396
13. Choi K.H., Mazurkie A.S., Morris A.J., Utheza D., Tolan D.R., and Allen K.N. Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 Å. Biochemistry 38 (1999) 12655-12664
14. Alefounder P.R., Baldwin S.A., Perham R.N., and Short N.J. Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli. Biochem. J. 257 (1989) 529-534
15. Brändén C.I. The TIM barrel-the most frequently occurring folding motif in proteins. Curr. Opin. Struct. Biol. 1 (1991) 978-983
16. Marsh J.J., and Lebherz H.G. Fructose-bisphosphate aldolases: an evolutionary history. Trends Biochem. Sci. 17 (1992) 110-113
17. 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
18. Blom N.S., Tetreault S., Coulombe R., and Sygusch J. Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase. Nat. Struct. Biol. 3 (1996) 856-862
19. Cooper S.J., Leonard G.A., McSweeney S.M., Thompson A.W., Naismith J.H., Qamar S., Plater A., Berry A., and Hunter W.N. The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold. Structure 4 (1996) 1303-1315
20. Hall D.R., Leonard G.A., Reed C.D., Watt C.I., Berry A., and Hunter W.N. The crystal structure of Escherichia 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
21. Plater A.R., Zgiby S.M., Thomson G.J., Qamar S., Wharton C.W., and Berry A. Conserved residues in the mechanism of the E. coli class II FBP-aldolase. J. Mol. Biol. 285 (1999) 843-855
22. Zgiby S.M., Thomson G.J., Qamar S., and Berry A. Exploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolases. Eur. J. Biochem. 267 (2000) 1858-1868
23. Hall D.R., Bond C.S., Leonard G.A., Watt C.I., Berry A., and Hunter W.N. Structure of tagatose-1,6-bisphosphate aldolase. Insight into chiral discrimination, mechanism, and specificity of class II aldolases. J. Biol. Chem. 277 (2002) 22018-22024
24. Zgiby S.M., Plater A.R., Bates M.A., Thomson G.J., and Berry A. A functional role for a flexible loop containing Glu182 in the class II fructose-1,6-bisphosphate aldolase from Escherichia coli. J. Mol. Biol. 315 (2002) 131-140
25. Sauve V., and Sygusch J. Molecular cloning, expression, purification, and characterization of fructose-1,6-bisphosphate aldolase from Thermus aquaticus. Protein Expr. Purif. 21 (2001) 293-302
26. Izard T., and Sygusch J. Induced fit movements and metal cofactor selectivity of class II aldolases: structure of Thermus aquaticus fructose-1,6-bisphosphate aldolase. J. Biol. Chem. 279 (2004) 11825-11833
27. Williams G.J., Domann S., Nelson A., and Berry A. Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution. Proc. Natl. Acad. Sci. USA 100 (2003) 3143-3148
28. Hao J., and Berry A. A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents. Protein Eng. Des. Sel. 17 (2004) 689-697
29. Lee J.H., Im Y.J., Rho S.-H., Park S.H., Kim M.-K., Cho S.J., Kim T.-Y., Oh J.H., Shin H.-J., Lee D.-S., and Eom S.H. Crystallization and preliminary X-ray analysis of class II fructose-1,6-bisphosphate aldolase from Thermus caldophilus. Protein Pept. Lett. 10 (2003) 511-515
30. Bae J., Kim D., Choi Y., Koh S., Park J.E., Kim J.S., Moon S.H., Park B.H., Park M., Song H.E., Hong S.-I., and Lee D.-S. A hexokinase with broad sugar specificity from a thermophilic bacterium. Biochem. Biophys. Res. Commun. 334 (2005) 754-763
31. Leslie A.G.W. MOSFLM User Guide (1992), MRC-Laboratory Molecular Biology, Cambridge, UK
32. Bailey S. The CCP4 suite-programs for protein crystallography. Acta Crystallogr. Sect. D Biol. Crystallogr. 50 (1994) 760-776
33. Smith J.L. Determination of three-dimensional structure by multiwavelength anomalous diffraction. Curr. Opin. Struct. Biol. 1 (1991) 1002-1011
34. Terwilliger T.C., and Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr. Sect. D Biol. Crystallogr. 55 (1999) 849-861
35. Terwilliger T.C. Maximum likelihood density modification. Acta Crystallogr. Sect. D Biol. Crystallogr. 56 (2000) 965-972
36. Jones T.A., Zhou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
37. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., GrosseKunstleve R.W., Jiang J.-S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., and Warren G.L. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. Sect. D Biol. Crystallogr. 54 (1998) 905-921
38. Miranker A., and Karplus M. Functionality maps of binding sites: a multiple copy simultaneous search method. Proteins 11 (1991) 29-34
39. Brooks B.R., Bruccoleri R.E., Olafson B.D., States D.J., Swaminathan S., and Karplus M. CHARMM: a program for macromolecular energy, minimization, and dynamics calculations. J. Comp. Chem. 4 (1983) 187-217
40. Kleywegt G.J., and Jones T.A. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr. Sect. D Biol. Crystallogr. 50 (1994) 178-185
41. Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK-a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291