Cocrystallization of a mutant aspartate aminotransferase with a C5- dicarboxylic substrate analog: Structural comparison with the enzyme-C4- dicarboxylic analog complex

Journal of Biochemistry

Volumn 127, Issue 2, 2000, Pages 337-343

  Oue, Shinya ^a   Okamoto, Akihiro ^a   Yano, Takato ^a   Kagamiyama, Hiroyuki ^a  

^a OSAKA MEDICAL COLLEGE   (Japan)

Author keywords

Aspartate aminotransferase; Crystallography; Directed evolution; Substrate specificity

Indexed keywords

ASPARTATE AMINOTRANSFERASE; BACTERIAL ENZYME; DICARBOXYLIC ACID DERIVATIVE; GLUTAMIC ACID; GLUTARIC ACID; MUTANT PROTEIN; PYRIDOXAL 5 PHOSPHATE; SUCCINIC ACID;

AMINO ACID METABOLISM; AMINO ACID SUBSTITUTION; ARTICLE; CRYSTALLIZATION; DIRECTED MOLECULAR EVOLUTION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034098472     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022612     Document Type: Article

References (35)

1. Velick, S.F. and Varva, J. (1962) A kinetic and equilibrium analysis of the glutamic oxalacetate transaminase mechanism. J. Biol. Chem. 237, 2109-2122
2. Kiick, D.M. and Cook, P.F. (1983) pH studies toward the elucidation of the auxiliary catalyst for pig heart aspartate aminotransferase. Biochemistry 22, 375-382
3. Jenkins, W.T. and Fonda, M.L. (1985) Kinetics, equilibria, and affinity for coenzymes and substrates in Transaminases (Christen, P. and Metzler, D.E., eds.) pp. 216-234, Wiley and Sons, New York
4. Kirsch, J.F., Eichele, G., Ford, G.C., Vincent, M.G., Jansonius, J.N., Gehring, H., and Christen, P. (1984) Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. J. Mol. Biol. 174, 497-525
5. Malcolm, B.A. and Kirsch, J.F. (1985) Site-directed mutagenesis of aspartate aminotransferase from E. coli. Biochem. Biophys. Res. Commun. 132, 915-921
6. Toney, M.D. and Kirsch, J.F. (1987) Tyrosine 70 increases the coenzyme affinity of aspartate aminotransferase. A site-directed mutagenesis study. J. Biol. Chem. 262, 12403-12405
7. Kuramitsu, S., Inoue, Y., Tanase, S., Morino, Y., and Kagamiyama, H. (1987) Substitution of an arginyl residue for the active site lysyl residue (Lys258) of aspartate aminotransferase. Biochem. Biophys. Res. Commun. 146, 416-421
8. Cronin, C.N. and Kirsch, J.F. (1988) Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis. Biochemistry 27, 4572-4579
9. Inoue, Y., Kuramitsu, S., Inoue, K., Kagamiyama, H., Hiromi, K., Tanase, S., and Morino, Y (1989) Substitution of a lysyl residue for arginine 386 of Escherichia coli aspartate aminotransferase. J. Biol. Chem. 264, 9673-9681
10. Ziak, M., Jäger, J., Malashkevich, V.N., Gehring, H., Jaussi, R., Jansonius, J.N., and Christen, P. (1993) Mutant aspartate aminotransferase (K258H) without pyridoxal-5′-phosphate-binding lysine residue. Structural and catalytic properties. Eur. J. Biochem. 211, 475-484
11. Yano, T., Kuramitsu, S., Tanase, S., Morino, Y., and Kagamiyama, H. (1992) Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5′-phosphate. Biochemistry 31, 5878-5887
12. Borisov, V.V., Barisova, S.N., Kachalova, G.S., Sosfenove, N.I., and Vainshtein, B.K. (1985) X-ray studies of chicken cytosolic aspartate aminotransferase in Transaminase (Christen, P. and Metzler, D.E., eds.) pp. 155-164, Wiley and Sons, New York
13. Arnone, A., Rogers, P.H., Hyde, C.C., Briley, P.D., Metzler, C.M., and Metzler, D.E. (1985) Pig cytosolic aspartate aminotransferase: the structures of the internal aldimine, external aldimine, and ketimine and of the β subform in Transaminases (Christen, P. and Metzler, D.E., eds.) pp. 138-155, Wiley and Sons, New York
14. Kamitori, S., Okamoto, A., Hirotsu, K., Higuchi, T., Kuramitsu, S., Kagamiyama, H., Matsuura, Y., and Katsube, Y. (1990) Three-dimensional structures of aspartate aminotransferase from Escherichia coli and its mutant enzyme at 2.5 Å resolution. J. Biochem. 108, 175-184
15. McPhalen, C.A., Vincent, M.G., and Jansonius, J.N. (1992) X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase. J. Mol. Biol. 225, 495-517
16. Okamoto, A., Higuchi, T., Hirotsu, K., Kuramitsu, S., and Kagamiyama, H. (1994) X-ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form. J. Biochem. 116, 95-107
17. Kawaguchi, S. and Kuramitsu, S. (1998) Thermodynamics and molecular simulation analysis of Hydrophobic substrate recognition by aminotransferases. J. Biol. Chem. 273, 18353-18364
18. Harutynyan, E.G., Malashkevich, V.N., Kochkina, V.M., and Torchinsky, Y.M. (1985) Three-dimensional structure of the complex of chicken cytosolic aspartate aminotransferase with 2-oxoglutarate in Transaminases (Christen, P. and Metzler, D.E., eds.) pp. 164-173, Wiley and Sons, New York
19. Picot, D., Sandmeier, E., Thaller, C., Vincent, M.G., Christen, P., and Jansonius, J.N. (1991) The open/closed conformational equilibrium of aspartate aminotransferase. Studies in the crystalline state and with a fluorescent probe in solution. Eur. J. Biochem. 196, 329-341
20. Malashkevich, V.N., Toney, M.D., and Jansonius, J.N. (1993) Crystal structures of true enzymatic reaction intermediate: Aspartate and glutamate ketimines in aspartate aminotransferase. Biochemistry 32, 13451-13462
21. Miyahara, I., Hirotsu, K., Hayashi, H., and Kagamiyama, H. (1994) X-ray crystallographic study of pyridoxamine 5′-phosphate-type aspartate aminotransferases from Escherichia coli in three forms. J. Biochem. 116, 1001-1012
22. Yano, T., Oue, S., and Kagamiyama, H. (1998) Directed evolution of an aspartate aminotransferase with new substrate specificities. Proc. Natl. Acad. Sci. USA 95, 5511-5515
23. Oue, S., Okamoto, A., Yano, T., and Kagamiyama, H. (1998) Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues. J. Biol. Chem. 274, 2344-2349
24. Yano, T., Kuramitsu, S., Tanase, S., Morino, Y., Hiromi, K., and Kagamiyama, H. (1991) The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase. J. Biol. Chem. 266, 6079-6085
25. Kuramitsu, S., Hiromi, K., Hayashi, H., Morino, Y., and Kagamiyama, H. (1990) Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity. Biochemistry 29, 5469-5476
26. Faesella, P., Giartosio, A., and Hammes, G.G. (1966) The interaction of aspartate aminotransferase with α-methylaspartic acid. Biochemistry 5, 197-202
27. Fonda, M.L. and Johnson, R.J. (1970) Computer analysis of spectra of enzyme-substrate and enzyme-inhibitor complexes involving aspartate aminotransferase. J. Biol. Chem. 245, 2709-2716
28. Higashi, T. (1990) Auto-indexing of oscillation images. J. Appl. Crystallogr. 23, 253-257
29. Brünger, A.T., Kuriyan, J., and Karplus, M. (1987) Crystallographic R-factor refinement by molecular dynamics. Science 235, 458-460
30. Engh, R.A. and Huber, R. (1991) Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A47, 392-400
31. McRee, D.E. (1992) A visual protein crystallographic software system for X11/Xview. J. Mol. Graphics 10, 44-47
32. Karmen, A. (1955) A note on the spectrophotometric assay of glutamic oxalacetate transaminase in human blood serum. J. Clin. Invest. 34, 131-133
33. Jenkins, W.T. and Siezer, I.W. (1957) Glutamic aspartic transaminase. J. Am. Chem. Soc. 79, 2655-2656
34. Kallen, R.K., Korpela, T., Martell, A.E., Matsushima, Y., Metzler, C.M., Metzler, D.E., Morozov, Y.V., Ralston, I.M., Savin, F.A., Torchinsky, Y.M., and Ueno, H. (1985) Chemical and spectroscopic properties of pyridoxal and pyridoxamine phosphates in Transaminases (Christen, P. and Metzler, D.E., eds.) pp. 37-108, Wiley and Sons, New York
35. Malashkevich, V.N., Onuffer, J.J., Kirsch, J.F., and Jansonius, J.N. (1995) Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase. Mol. Struc. Biol. 2, 548-553