Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure

Journal of Molecular Biology

Volumn 259, Issue 3, 1996, Pages 458-466

  Dreyer, Matthias K ^a   Schulz, Georg E ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

Author keywords

Class II aldolase; Enzymatic mechanism; Protein structure; X ray diffraction; Zinc enzyme

Indexed keywords

BACTERIAL ENZYME; DIHYDROXYACETONE PHOSPHATE; ENZYME INHIBITOR; FRUCTOSE BISPHOSPHATE ALDOLASE; FUCULOSE ALDOLASE; UNCLASSIFIED DRUG; ZINC;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STRUCTURE; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTON TRANSPORT; STEREOCHEMISTRY; X RAY DIFFRACTION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0029942857     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0332     Document Type: Article

References (23)

1. Bednardski, M. D., Simon, E. S., Bischofberger, N., Fessner, W.-D., Kim, M.-J., Saito, T., Waldmann, H. & Whitesides, G. M. (1989). Rabbit muscle aldolase as a catalyst in organic syntheses. J. Am. Chem. Soc. 111, 627-635.
2. Brünger, A. T. (1992a). X-PLOR Manual Version 3.0, Yale University New Haven.
3. Brünger, A. T. (1992b). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 355, 472-475.
4. Collaborative Computational Project (1994). The CCP4 Suite: programs for protein crystallography Acta Crystallog. sect. D, 50, 760-763.
5. Collins, K. D. (1974). An activated intermediate analogue. The use of phosphoglycolohydroxamate as a stable analogue of a transiently occurring dihydroxyacetone phosphate-derived enolate in enzymatic catalysis. J. Biol. Chem. 249, 136-142.
6. Dreyer, M. K. & Schulz, G. E. (1993). The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli. J. Mol. Biol. 231, 549-553.
7. Dreyer, M. K. & Schulz, G. E. (1996). The refined high resolution structure of the metal ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli. Protein Sci. In the press.
8. Fessner, W.-D. (1995). Enzyme catalyzed aldol additions. In Houben-Weyl Methods of Organic Chemistry (Helmchen, G., Hoffmann, R. W., Mulzer, J. & Schaumann, E., eds), vol. E21b, pp. 1736-1747, Thieme, Stuttgart.
9. Fessner, W.-D., Sinerius, G., Schneider, A., Dreyer, M., Schulz, G. E., Badia, J. & Aguilar, J. (1991). Diastereoselective enzymatic aldol additions: L-rhamnulose and L-fuculose-1-phosphate aldolases from E.coli. Angew. Chem. Int. Ed. Engl. 30, 555-558.
10. Fleischmann, R. D. et al. & Venter, C. (1995). Whole genome random sequencing and assembly of Haemophilus influenzae Rd. Science, 269, 469-512.
11. Ghalambor, M. A. & Heath, E. C. (1966). L-Fuculose-1-phosphate aldolase. Methods Enzymol. 9, 538-542.
12. Horecker, B. L., Tsolas, O. & Lai, C. Y. (1972). Aldolases. In The Enzymes (Boyer, P. D., ed.), 3rd edit. vol. 7, pp. 213-258, Academic Press, New York.
13. Izard, T., Lawrence, M. C., Malby, R. L., Lilly, G. G. & Colman, P. (1994). The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli. Structure, 2, 361-369.
14. Kabsch, W. (1988). Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallog. 21, 916-924.
15. Littlechild, J. A. & Watson, H. C. (1993). A data-based reaction mechanism for type I fructose bisphosphate aldolase. Trends Biochem. Sci. 18, 36-39.
16. Luzzati, V. (1952). Traitement statistique des erreurs dans la détermination des structures cristallines. Acta Crystallog. 5, 802-810.
17. Mavridis, M., Hatada, M. H., Tulinsky A. & Lebioda, L. (1982). Structure of 2-keto-3-deoxy-phosphogluconate aldolase at 2.8 À resolution. J. Mol. Biol. 162, 419-444.
18. Müller-Dieckmann, C. (1994). Gezielte Mutagenese, Präparation, kinetische Untersuchungen sowie Kristallisation von Fuculose-1-phosphat Aldolase aus Escherichia coli. Diplomarbeit, Universität Freiburg im Breisgau.
19. Ozaki, A., Toone, E. J., v.d. Osten, C. H., Sinskey A. & Whitesides, G. M. (1990). Overproduction and substrate specificity of a bacterial fuculose-1-phosphate aldolase. J. Am. Chem. Soc. 112, 4970-4971.
20. Read, R. J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallog. sect. A, 42, 140-149.
21. Schneider, A. (1994). Isolierung und Charakterisierung der L-Fuculose-1-phosphat-Aldolase und der Rhamnulose-Kinase. Enzymatische Synthese seltener Ketose-phosphate. Dissertation, Universität Freiburg im Breisgau.
22. Whitesides, G. M. & Wong, C.-H. (1985). Enzymes as catalysts in synthetic organic chemistry Angew. Chem. Int. Ed. Engl. 24, 617-638.
23. Wong, C.-H., Halcomb, R. H., Ichikawa Y. & Kajimoto T. (1995). Enzymes in organic synthesis - application to the problems of carbohydrate recognition I. Angew. Chem. Int. Ed. Engl. 34, 412-432.