Roles of three well-conserved arginine residues in mediating the catalytic activity of tobacco acetohydroxy acid synthase

Journal of Biochemistry

Volumn 138, Issue 1, 2005, Pages 35-40

  Le, Dung Tien ^a,d   Yoon, Moon Young ^b   Kim, Young Tae ^c   Choi, Jung Do ^a  

^a Chungbuk National University   (South Korea)

^b Hanyang University   (South Korea)

^c Pukyong National University   (South Korea)

^d NATIONAL FOOD RESEARCH INSTITUTE   (Japan)

Author keywords

Acetohydroxy acid synthase; Conserved arginine; Homology model; Site directed mutagenesis; Tobacco

Indexed keywords

ACETOLACTATE SYNTHASE; ARGININE; COCARBOXYLASE; FLAVINE ADENINE NUCLEOTIDE; HERBICIDE;

ARTICLE; CATALYSIS; DNA SEQUENCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME STRUCTURE; KINETICS; MUTANT; MUTATION; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; TOBACCO; WILD TYPE;

ACETOLACTATE SYNTHASE; ARGININE; BINDING SITES; CATALYSIS; CIRCULAR DICHROISM; FLAVIN-ADENINE DINUCLEOTIDE; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PLANTS, TOXIC; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SPECTROPHOTOMETRY; STRUCTURE-ACTIVITY RELATIONSHIP; TOBACCO;

NICOTIANA TABACUM;

EID: 23344448255     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvi099     Document Type: Article

References (30)

1. Duggleby, R.G. and Pang, S.S. (2000) Acetohydroxyacid Synthase. J. Biochem. Mol. Biol. 33, 1-36
2. LaRossa, R.A. and Schloss, J.V. (1984) The sulfonylurea herbicide Sulfometuron is an extremely potent and selective inhibitor of acetolactate synthase in Salmonella typhimurium. J. Biol. Chem. 259, 8753-8757
3. Ray, J.B. (1984) Site of action of chlorosulfuron: Inhibition of valine and isoleucine biosynthesis of plants. Plant Physiol. 75, 827-831
4. Shaner, D.L., Anderson, P.C., and Stidham, M.A. (1984) Imidazolinones: potent inhibitors of acetohydroxy acid synthase. Plant Physiol. 76, 545-546
5. Gerwick, B.C., Subramanian, M.V., Loney-Gallant, V., and Chander, D.P. (1990) Mechanism of action of the 1, 2, 4-triazolo[1, 5-a]pyrimidine. Pestic. Sci. 29, 357-364
6. Namgoong, S.K., Lee, H.J., Kim, Y.S., Shin, J.-H., Che, J.-K., Jang, D.Y., Kim, G.S., Yoo, J.W., Kang, M.-K., Kil, M.-W., Choi, J.-D., and Chang, S.-I. (1999) Synthesis of the quinoline-linked triazolopyrimidine analogues and their interactions with the recombinant tobacco acetolactate synthase. Biochem. Biophys. Res. Commun. 258, 797-801
7. Chang, S.-I., Kang, M.-K., Choi, J.-D., and Namgoong, S.K. (1997) Soluble overexpression in Escherichia coli, and purification and characterization of wild-type recombinant tobacco acetolactate synthase. Biochem. Biophys. Res. Commun. 234, 549-553
8. Chipman, D., Barak, Z., and Schloss, J.V. (1988) Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases. Biochim. Biophys. Acta 1385, 401-419
9. Le, D.T., Yoon M.-Y., Kim, Y.T., and Choi, J.-D. (2004). Homology modeling and examination of the active site of tobacco acetolactate synthase. Biochem. Biophys. Res. Commun. 317, 930-938
10. Yoon, T.-Y., Chung S.-M., Chang S.-I., Yoon M.-Y., Hahn T.-R., and Choi J.-D. (2002) Roles of lysine 219 and 255 residues in tobacco acetolactate synthase. Biochem. Biophys. Res. Commun. 293, 433-439
11. Chong, C.-K., Shin, H.-J., Chang, S.-I., and Choi, J.-D. (1999) Role of tryptophanyl residues in tobacco acetolactate synthase. Biochem. Biophys. Res. Commun. 259, 136-140
12. Shin, H.-J., Chong, C.-K., Chang, S.-I., and Choi, J.-D. (2000) Structural and functional role of cysteinyl residues in tobacco acetolactate synthase. Biochem. Biophys. Res. Commun. 271, 801-806
13. Oh, K.-J., Park, E.-J., Yoon, M.-Y., Han, J.-R., and Choi, J.-D. (2001) Roles of histidine residues in tobacco acetolactate synthase. Biochem. Biophys. Res. Commun. 282, 1237-1243
14. Le, D.T., Yoon, M.-Y., Kim, Y.T., and Choi, J.-D. (2003) Roles of conserved methionine residues in tobacco acetolactate synthase. Biochem. Biophys. Res. Commun. 306, 1075-1082
15. Chong, C.-K. and Choi, J.-D. (2000) Amino acid residues conferring herbicide tolerance in tobacco acetolactate synthase. Biochem. Biophys. Res. Commun. 279, 462-467
16. Bartlett, G.J., Porter C.T., Borkakoti N., and Thornton J.M. (2002) Analysis of catalytic residues in enzyme active sites. J. Mol. Biol. 324, 105-121
17. Kim, S.-H., Park, E.-J., Yoon, S.-S., and Choi, J.-D. (2003) An active site arginine residue in tobacco acetolactate synthase. Bull. Korean Chem. Soc. 24, 1799-1804
18. Pang, S.S., Duggleby, R.G., and Guddat, L.W. (2002) Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors. J. Mol. Biol. 317, 249-262
19. Pang, S.S., Guddat, L.W., and Duggleby, R.G. (2003) Molecular basis of Sulfonylureas herbicide inhibition of acetohydroxyacid synthase. J. Biol. Chem. 278, 7639-7644
20. Schwede, T., Kopp, J., Guex, N., and Peitsch, M.C. (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385
21. Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994) CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680
22. Sarkar, G. and Sommer, S.S. (1990) "Megaprimer" method of site-directed mutagenesis. Biotechniques 2, 404-407
23. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, USA
24. Sanger, F., Nicklen, S., and Coulson, A.R. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA 74, 5463-5467
25. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
26. Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
27. Westerfeld, W.W. (1945) A colorimetric determination of blood acetoin. J. Biol. Chem. 161, 495-502
28. Chong, C.-K., Chang, S.-I., and Choi, J.-D. (1997) Functional amino acid residues of recombinant tobacco acetolactate synthase. J. Biochem. Mol. Biol. 30, 274-279
29. Engel, S., Vyazmensky, M., Vinogradov, M, Berkovich, D., Bar-Ilan, A., Qimron, U., Rosiansky Y., Barak, Z., and Chipman, D.M. (2004) Role of a conserved Arginine in the mechanism of Acetohydroxy acid synthase: catalysis of condensation with a specific ketoacid substrate. J. Biol. Chem. 279, 24803-24812
30. Schloss, J.V., Ciskanik, L.M., and Van Dyk, D.E. (1988) Origin of the herbicide binding site of acetolactate synthase. Nature 331, 360-362