Effects of deletions at the C-terminus of tobacco acetohydroxyacid synthase on the enzyme activity and cofactor binding

Biochemical Journal

Volumn 384, Issue 1, 2004, Pages 59-68

  Kim, Joungmok ^a   Beak, Dong Gil ^a   Kim, Young Tae ^b   Choi, Jung Do ^c   Yoon, Moon Young ^a  

^a Hanyang University   (South Korea)

^b Pukyong National University   (South Korea)

^c Chungbuk National University   (South Korea)

Author keywords

Acetohydroxyacid synthase (AHAS); Cofactor binding; Deletion mutant; Functional domain analysis; Thiamine diphosphate; Tobacco

Indexed keywords

AMINO ACIDS; BIOSYNTHESIS; CATALYSIS; CHROMATOGRAPHIC ANALYSIS; DIMERS; ENZYMES; HERBICIDES; MICROORGANISMS; MUTAGENESIS; PLANTS (BOTANY); YEAST;

ACETOHYDROXYACID SYNTHASE (AHAS); COFACTOR BINDING; GEL-FILTRATION CHROMATOGRAPHY; HERBICIDE RESISTANCE;

TOBACCO;

ACETOLACTATE SYNTHASE; BIOLOGICAL FACTOR; BRANCHED CHAIN AMINO ACID; COCARBOXYLASE; COFACTOR; DIMER; ENZYME VARIANT; HERBICIDE; ISOLEUCINE; LEUCINE; MUTANT PROTEIN; UNCLASSIFIED DRUG; VALINE;

AMINO ACID METABOLISM; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; DELETION MUTANT; DRUG BINDING SITE; DRUG RESISTANCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME MODIFICATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME STRUCTURE; FUNCTIONAL DOMAIN ANALYSIS; GEL FILTRATION CHROMATOGRAPHY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; TOBACCO;

ACETOLACTATE SYNTHASE; ALTERNATIVE SPLICING; AMINO ACID SEQUENCE; CHROMATOGRAPHY, GEL; CLONING, MOLECULAR; COENZYMES; DATABASES, PROTEIN; MOLECULAR SEQUENCE DATA; PEPTIDES; PLANT PROTEINS; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE DELETION; THIAMINE PYROPHOSPHATE; TOBACCO;

NICOTIANA TABACUM;

EID: 9444292861     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040427     Document Type: Article

References (41)

1. Duggleby, R. G. and Pang, S. S. (2000) Acetohydroxyacid synthase. J. Biochem. Mol. Biol. 33, 1-36
2. Chipman, D., Barak, Z. and Schloss, J. V. (1998) Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases. Biochim. Biophys. Acta 1385, 401-419
3. Jordan, F., Nemeria, N., Guo, F., Baburina, I., Gao, Y., Kahyaoglu, A., Li, H., Wang, J., Yi, J., Guest, J. R. and Furey, W. (1998) Regulation of thiamin diphosphate-dependent 2-oxo acid decarboxylases by substrate and thiamin diphosphate. Mg(II) - evidence for tertiary and quaternary interactions. Biochim. Biophys. Acta 1385, 287-306
4. Shaner, D. L., Anderson, P. C. and Stidham, M. A. (1984) Imidazolinones: potent inhibitors of acetohydroxyacid synthase. Plant Physiol. 76, 545-546
5. Durner, J. and Boger, P. (1991) New aspects on inhibition of plant acetolactate synthase by chlorosulfuron and imazaquin. Plant Physiol. 95, 1144-1149
6. Chang, A. K. and Duggleby, R. G. (1998) Herbicide-resistant forms of Arabidopsis thaliana acetohydroxyacid synthase: characterization of the catalytic properties and sensitivity to inhibitors of four defined mutants. Biochem. J. 333, 765-777
7. Lee, Y. T. and Duggleby, R. G. (2000) Mutagenesis studies on the sensitivity of Escherichia coli acetohydroxyacid synthase II to herbicides and valine. Biochem. J. 350, 69-73
8. Hershey, H. P., Schwartz, L. J., Gale, J. P. and Abell, L. M. (1999) Cloning and functional expression of small subunit of acetolactate synthase from Nicotiana plumbaginifolia. Plant Mol. Biol. 40, 795-806
9. Lee, Y. T. and Duggleby, R. G. (2001) Identification of the regulatory subunit of Arabidopsis thaliana acetohydroxyacid synthase and reconstitution with its catalytic subunit. Biochemistry 40, 6836-6844
10. Sella, C., Weinstock, O., Barak, Z. and Chipman, D. M. (1993) Subunit association in acetohydroxy acid synthase isozyme III. J. Bacteriol. 175, 5339-5343
11. Vyazmensky, M., Sella, C., Barak, Z. and Chipman, D. M. (1996) Isolation and characterization of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme. Biochemistry 35, 10339-10346
12. Hill, C. M., Pang, S. S. and Duggleby, R. G. (1997) Purification of Escherichia coli acetohydroxyacid synthase isoenzyme II and reconstitution of active enzyme from its individual pure subunits. Biochem. J. 327, 891-898
13. Weinstock, O., Sella, C., Chipman, D. M. and and Barak, Z. (1992) Properties of subcloned subunits of bacterial acetohydroxy acid syntheses. J. Bacteriol. 174, 5560-5566
14. 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
15. Pang, S. S., Guddat, L. W. and Duggleby, R. G. (2003) Molecular basis of sulfonylurea herbicide inhibition of acetohydroxyacid synthase. J. Biol. Chem. 278, 7639-7644
16. Hasson, M. S., Muscate, A., McLeish, M. J., Polovnikova, L. S., Gerlt, J. A., Kenyon, G. L., Petsko, G. A. and Ringe, D. (1998) The crystal structure of benzoylformate decarboxylase at 1.6 Å resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes. Biochemistry 37, 9918-9930
17. Muller, Y. A. and Schulz, G. E. (1993) Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase. Science 259, 965-967
18. Dobritzsch, D., Konig, S., Schneider, G. and Lu, G. (1998) High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis: implications for substrate activation in pyruvate decarboxylases. J. Biol. Chem. 273, 20196-20204
19. Chang, A. K., Nixon, P. F. and Duggleby, R. G. (2000) Effects of deletions at the carboxyl terminus of Zymomonas mobilis pyruvate decarboxylase on the kinetic properties and substrate specificity. Biochemistry 39, 9430-9437
20. Ibdah, M., Bar-Ilan, A., Livnah, O., Schloss, J. V., Barak, Z. and Chipman, D. M. (1996) Homology modeling of the structure of bacterial acetohydroxy acid synthase and examination of the active site by site-directed mutagenesis. Biochemistry 35, 16282-16291
21. Westerfeld, W. W. (1945) A colorimetric determination of blood acetoin. J. Biol. Chem. 161, 495-502
22. Cleland, W. W. (1979) Statistical analysis of enzyme kinetic data. Methods Enzymol. 63, 103-138
23. Chong, C. K. and Choi, J. D. (2000) Amino acid residues conferring herbicide tolerance in tobacco acetolactate synthase. Biochem. Biophys. Res. Commun. 279, 462-427
24. 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
25. Yoon, M. Y., Hwang, J. H., Choi, M. K., Baek, D. K., Kim, J., Kim, Y T. and Choi, J. D. (2003) The active site and mechanism of action of recombinant acetohydroxy acid synthase from tobacco. FEBS Lett. 555, 185-191
26. 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
27. Bar-Ilan, A., Balan, V., Tittmann, K., Golbik, R., Vyazmensky, M., Hubner, G., Barak, Z. and Chipman, D. M. (2001) Binding and activation of thiamin diphosphate in acetohydroxyacid synthase. Biochemistry 40, 11946-11954
28. Gollop, N., Damri, B., Barak, Z. and Chipman, D. M. (1989) Kinetics and mechanism of acetohydroxyacid synthase isozyme III from Escherichia coli. Biochemistry 28, 6310-6317
29. Candy, J. M. and Duggleby, R. G. (1994) Investigation of the cofactor-binding site of Zymomonas mobilis pyruvate decarboxylase by site-directed mutagenesis. Biochem. J. 300, 7-13
30. Pang, S. S. and Duggleby, R. G. (1999) Expression, purification, characterization, and reconstitution of the large and small subunits of yeast acetohydroxyacid synthase. Biochemistry 38, 5222-5231
31. Li, H., Furey, W. and Jordan, F. (1999) Role of glutamate 91 in information transfer during substrate activation of yeast pyruvate decarboxylase. Biochemistry 38, 9992-10003
32. Hawkins, C. F., Borges, A. and Perham, R. N. (1989) A common structural motif in thiamin pyrophosphate-binding enzymes. FEBS Lett. 255, 77-82
33. Lakowicz, J. R. (1999) Principles of Fluorescence Spectroscopy, 2nd edn., Kluwer Academic, New York
34. Liu, M., Sergienko, E. A., Guo, F, Wang, J., Tittmann, K., Hubner, G., Furey, W. and Jordan, F. (2001) Catalytic acid-base groups in yeast pyruvate decarboxylase. 1. Site-directed mutagenesis and steady-state kinetic studies on the enzyme with the D28A, H114F, and E477Q substitutions. Biochemistry 40, 7355-7368
35. Sergienko, E. A. and Jordan, F. (2001) Catalytic acid-base groups in yeast pyruvate decarboxylase. 2. Insights into the specific roles of D28 and E477 from the rates and stereospecificity of formation of carboligase side products. Biochemistry 40, 7369-7381
36. Jordan, F, Akinyosoye, O., Dikada, G., Kudzin, Z. H. and Kuo, D. J. (1988) in Thiamin Pyrophosphate Biochemistry (Schowen, R. L. and Schellenberger, A., eds.), vol. 1, pp. 79-92, CRC Press. Boca Raton
37. Ermer, J., Schellenberger, A. and Hubner, G. (1992) Kinetic mechanism of pyruvate decarboxylase. Evidence for a specific protonation of the enzymic intermediate. FEBS Lett. 299, 163-165
38. Harris, T. K. and Washabaugh, M. W. (1995) Solvent-derived protons in catalysis by brewers' yeast pyruvate decarboxylase. Biochemistry 34, 14001-14011
39. Dyda, F., Furey, W., Swaminathan, S., Sax, M., Farrenkopf, B. and Jordan, F. (1993) Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4 Å resolution. Biochemistry 32, 6165-6170
40. Lobell, M. and Crout, D. H. G. (1996) Pyruvate decarboxylase: a molecular modeling study of pyruvate decarboxylation and acyloin formation. J. Am. Chem. Soc. 118, 1867-1873
41. Alvarez, F. J., Ermer, J., Huebner, G., Schellenberger, A. and Schowen, R. L. (1995) The linkage of catalysis and regulation in enzyme action: solvent isotope effects as probes of protonic sites in the yeast pyruvate decarboxylase mechanism. J. Am. Chem. Soc. 117, 1678-1683