Erratum: Mechanisms of acetohydroxyacid synthases (Current Opinion in Chemical Biology (2005) 9 (475-481) DOI: 10.1016/j.cbpa.2005.07.002;Mechanisms of acetohydroxyacid synthases

Current Opinion in Chemical Biology

Volumn 9, Issue 5, 2005, Pages 475-481

  Chipman, David M ^a   Duggleby, Ronald G ^b   Tittmann, Kai ^c  

^a BEN GURION UNIVERSITY OF THE NEGEV   (Israel)

^b UNIVERSITY OF QUEENSLAND   (Australia)

^c MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACETOLACTATE SYNTHASE; HERBICIDE;

DECARBOXYLATION; DIELECTRIC CONSTANT; DISSOCIATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME RELEASE; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SYNTHESIS; LACTOBACILLUS PLANTARUM; OXIDATION REDUCTION REACTION; OXYGEN CONSUMPTION; REVIEW; STRUCTURE ANALYSIS; WILD TYPE;

EID: 25144494007     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2006.01.016     Document Type: Erratum

References (50)

1. D. Chipman, Z. Barak, and J.V. Schloss Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases Biochim Biophys Acta 1385 1998 401 419
2. R.G. Duggleby, and S.S. Pang Acetohydroxyacid synthase J Biochem Mol Biol 33 2000 1 36
3. F.C. Stormer Isolation of crystalline pH 6 acetolactate-forming enzyme from Aerobacter aerogenes J Biol Chem 242 1967 1756 1759
4. W.D. Holtzclaw, and L.F. Chapman Degradative acetolactate synthase of Bacillus subtilis: purification and properties J Bacteriol 121 1975 917 922
5. L. Eoyang, and P.M. Silverman Purification and subunit composition of acetohydroxyacid synthase I from Escherichia coli K-12 J Bacteriol 157 1984 184 189
6. P. Friden, J. Donegan, J. Mullen, P. Tsui, M. Freundlich, L. Eoyang, R. Weber, and P.M. Silverman The ilvB locus of Escherichia coli K-12 is an operon encoding both subunits of acetohydroxyacid synthase I Nucleic Acids Res 13 1985 3979 3993
7. S. Mendel, M. Vinogradov, M. Vyazmensky, D.M. Chipman, and Z. Barak The N-terminal domain of the regulatory subunit is sufficient for complete activation of acetohydroxyacid synthase III from Escherichia coli J Mol Biol 325 2003 275 284 The authors propose that the N-terminal domains of the regulatory subunits of AHAS isozyme III are structurally homologous to the C-terminal regulatory domains of 3-phosphoglycerate dehydrogenase. A pair of these domains forms two binding sites for feedback inhibition by valine.
8. S. Mendel, T. Elkayam, C. Sella, V. Vinogradov, M. Vyazmensky, D.M. Chipman, and Z. Barak Acetohydroxyacid synthase: a proposed structure for regulatory subunits supported by evidence from mutagenesis J Mol Biol 307 2001 465 477
9. Y.T. Lee, and R.G. Duggleby Regulatory interactions in Arabidopsis thaliana acetohydroxyacid synthase FEBS Lett 512 2002 180 184
10. Y.T. Lee, and R.G. Duggleby Identification of the regulatory subunit of Arabidopsis thaliana acetohydroxyacid synthase and reconstitution with its catalytic subunit Biochemistry 40 2001 6836 6844
11. R.P. Lawther, R.C. Wek, J.M. Lopes, R. Pereira, B.E. Taillon, and G.W. Hatfield The complete nucleotide sequence of the ilvGMEDA operon of Escherichia coli K-12 Nucleic Acids Res 15 1987 2137 2155
12. R.P. Lawther Point mutations in the regulatory region of the ilvGMEDA operon of Escherichia coli K-12 J Bacteriol 171 1989 1188 1191
13. R.P. Lawther, J.M. Lopes, M.J. Ortuno, and M.C. White Analysis or regulation of the ilvGMEDA operon by using leader-attenuator-galK gene fusions J Bacteriol 172 1990 2320 2327
14. K. Tittmann, K. Schroder, R. Golbik, J. McCourt, A. Kaplun, R.G. Duggleby, Z. Barak, D.M. Chipman, and G. Hübner Electron transfer in acetohydroxy acid synthase as a side reaction of catalysis. Implications for the reactivity and partitioning of the carbanion/enamine form of (α-hydroxyethyl)thiamin diphosphate in a "nonredox" flavoenzyme Biochemistry 43 2004 8652 8661 Evidence for a hitherto uncharacterized intramolecular electron transfer reaction between the central thiamin enamine intermediate and the flavin is presented. The apparent rate of this side reaction of catalysis is small compared to the competing carboligation reaction.
15. S.S. Pang, R.G. Duggleby, and L.W. Guddat Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors J Mol Biol 317 2002 249 262 The 2.6 Å resolution crystal structure of the catalytic subunit of yeast AHAS is reported. The active site is at the dimer interface and near the proposed herbicide-binding site. The conformation of FAD and its position in the active site are defined.
16. S.S. Pang, L.W. Guddat, and R.G. Duggleby Molecular basis of sulfonylurea herbicide inhibition of acetohydroxyacid synthase J Biol Chem 278 2003 7639 7644 The crystal structure of yeast AHAS in a complex with a sulfonylurea herbicide, chlorimuron ethyl, is given at 2.8 Å resolution. The structure, which shows that the inhibitor contacts multiple residues and blocks access to the active site, provides a starting point for rational design of further herbicidal compounds.
17. J.A. McCourt, S.S. Pang, L.W. Guddat, and R.G. Duggleby Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase Biochemistry 44 2005 2330 2338 Crystal structures of yeast AHAS in complexes with chlorsulfuron, sulfometuronmethyl, metsulfuron methyl and tribenuron methyl provide clues about the differential effects of mutations in the active site tunnel on various inhibitors. The bent conformation of the isoalloxazine ring would account for its ability to accept electrons from the hydroxyethyl-ThDP intermediate.
18. N. Nemeria, K. Tittmann, E. Joseph, L. Zhou, M. Vazquez-Coll, P. Arjunan, G. Hübner, W. Furey, and F. Jordan Glutamate 636 of the Escherichia coli pyruvate dehydrogenase-E1 participates in active center communication and behaves as an engineered acetolactate synthase with unusual stereselectivity J Biol Chem 280 2005 21473 21478
19. 1H NMR spectroscopy. The quantitative analysis of their concentrations allows the determination of the microscopic rate constants of individual catalytic steps.
20. K. Tittmann, M. Vyazmensky, G. Hübner, Z. Barak, and D.M. Chipman The carboligation reaction of acetohydroxyacid synthase II: steady state intermediate distributions in wild-type and mutants by NMR Proc Natl Acad Sci USA 102 2005 553 558 Detailed NMR analysis was used to determine microscopic rate constants for elementary steps in the reactions of AHAS II and mutants altered at conserved residues Arg276, Trp464 and Met250.
21. Y. Lindqvist, G. Schneider, U. Ermler, and M. Sundstrom Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution EMBO J 11 1992 2373 2379
22. D. Kern, G. Kern, H. Neef, K. Tittmann, M. Killenberg Jabs, C. Wikner, G. Schneider, and G. Huebner How thiamine diphosphate is activated in enzymes Science 275 1997 67 70
23. A. Bar-Ilan, V. Balan, K. Tittmann, R. Golbik, M. Vyazmensky, G. Hübner, Z. Barak, and D.M. Chipman Binding and activation of thiamin diphosphate in acetohydroxyacid synthase Biochemistry 40 2001 11946 11954
24. N. Nemeria, A. Baykal, E. Joseph, S. Zhang, Y. Yan, W. Furey, and F. Jordan Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1′,4′-imino tautomeric form of the coenzyme, unlike the michaelis complex or the free coenzyme Biochemistry 43 2004 6565 6575 Two circular dichroism signals observed in ThDP-dependent enzymes were investigated. The authors suggest that all tetrahedral ThDP-bound covalent complexes will prefer the 1′,4′-iminopyrimidine tautomer, and that the 4′-aminopyrimidine of ThDP participates in multiple steps of acid-base catalysis.
25. J. Kim, D.G. Beak, Y.T. Kim, J.D. Choi, and M.Y. Yoon Effects of deletions at the C-terminus of tobacco acetohydroxyacid synthase on the enzyme activity and cofactor binding Biochem J 384 2004 59 68 Mutants of tobacco AHAS with serial deletions in two disordered regions, a 'mobile loop' and a C-terminal 'lid', were constructed. From the properties of mutants without the C-terminal lid, and the internal deletion mutant without the mobile loop 567-582, the authors suggest that these regions are involved in the binding/stabilization of the active dimer and ThDP binding.
26. D.T. Le, M.Y. Yoon, Y.T. Kim, and J.D. Choi Homology modeling of the structure of tobacco acetohydroxy acid synthase and examination of the active site by site-directed mutagenesis Biochem Biophys Res Commun 317 2004 930 938
27. M.Y. Yoon, J.H. Hwang, M.K. Choi, D.K. Baek, J. Kim, Y.T. Kim, and J.D. Choi The active site and mechanism of action of recombinant acetohydroxy acid synthase from tobacco FEBS Lett 555 2003 185 191
28. S. Engel, M. Vyazmensky, S. Geresh, Z. Barak, and D.M. Chipman Acetoxydroxyacid synthase: a new enzyme for chiral synthesis of R-phenylacetylcarbinol Biotechnol Bioeng 83 2003 833 840
29. S. Engel, M. Vyazmensky, M. Vinogradov, D. Berkovich, A. Bar-Ilan, U. Qimron, Y. Rosiansky, Z. Barak, and D.M. Chipman Role of a conserved arginine in the mechanism of acetohydroxyacid synthase. Catalysis of condensation with a specific ketoacid substrate J Biol Chem 279 2004 24803 24812 Mutagenesis of four different residues in the active site of AHAS II support a critical role for conserved residue Arg276 in stabilizing the transition states for ligation of the second substrate to HEThDP and for breaking of the product-ThDP bond.
30. S.S. Pang, R.G. Duggleby, R.L. Schowen, and L.W. Guddat The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate J Biol Chem 279 2004 2242 2253 The structure of Klebsiella pneumoniae ALS is similar to AHAS except that the FAD groove in AHAS is filled by the protein residues in ALS. Another complex has a tricyclic structure that has not been observed in any ThDP-dependent enzyme, and probably results from an intramolecular proton transfer within a tricyclic carbanion that is proposed as the true reaction intermediate.
31. M.T. Tse, and J.V. Schloss The oxygenase reaction of acetolactate synthase Biochemistry 32 1993 10398 10403
32. T. Ray Site of action of chlorsulfuron: inhibition of valine and isoleucine biosynthesis of plants Plant Physiol 75 1984 827 831
33. M. Muhitch, D. Shaner, and M. Stidham Imidazolinones and acetohydroxyacid synthase from higher plants. Properties of the enzyme from maize suspension culture cells and evidence for the binding of imazapyr to acetohydroxyacid synthase in vivo Plant Physiol 83 1987 451 456
34. R. LaRossa, and J. Schloss The sulfonylurea herbicide sulfometuron methyl is an extremely potent and selective inhibitor of acetolactate synthase in Salmonella typhimurium J Biol Chem 259 1984 8753 8757
35. A.K. Chang, and R.G. Duggleby Expression purification and characterization of Arabidopsis thaliana acetohydroxyacid synthase Biochem J 327 1997 161 169
36. J. Durner, V. Gailus, and P. Böger New aspects on inhibition of plant acetolactate synthase by chlorsulfuron and imazaquin Plant Physiol 95 1991 1144 1149
37. C.M. Hill, S.S. Pang, and R.G. Duggleby Purification of Escherichia coli acetohydroxyacid synthase isoenzyme II and reconstitution of active enzyme from its individual pure subunits Biochem J 327 1997 891 898
38. J. Schloss Acetolactate synthase mechanism of action and its herbicide binding site Pestic Sci 29 1990 283 292
39. T. Ahan, D. Kim, and J. Choi Inhibition of acetohydroxyacid synthase by sulfonylureas and imidazolinones Korean Biochem J 25 1992 636 641
40. J. Schloss, L. Ciskanik, and D. Van Dyk Origin of the herbicide binding site of acetolactate synthase Nature 311 1988 360 366
41. D. Shaner, P. Anderson, and M. Stidham Imidazolinones: potent inhibitors of acetohydroxyacid synthase Plant Physiol 76 1984 545 546
42. D. Landstein, S. Arad, Z. Barak, and D. Chipman Relationships among the herbicide and functional sites of acetohydroxy acid synthase from Chlorella emersonii Planta 191 1993 1 6
43. D. Shaner, B. Singh, and M. Stidham Interaction of imidazolinone with plant acetohydroxy acid synthase: evidence for in vivo binding and competition with sulfometuron methyl J Agric Food Chem 38 1990 1279 1282
44. F. Ortéga, J. Bastide, and T. Hawkes Comparison between thifensulfuron methyl-induced inactivation of barley acetohydroxyacid synthase and Escherichia coli acetohydroxyacid synthase isozyme II Pestic Biochem Physio 56 1996 231 242
45. J. Schloss Recent advances in understanding the mechanism and inhibition of acetolactate synthase J. Stetter Herbicides Inhibiting Branched Chain Amino Acid Biosynthesis 1994 Springer-Verlag 4 14
46. K. Ott, J. Kwagh, G. Stockton, V. Sidorov, and G. Kakefuda Rational molecular design and genetic engineering of herbicide resistant crops by structure modeling and site-directed mutagenesis of acetohydroxyacid synthase J Mol Biol 263 1996 359 368
47. M. Ibdah, A. Bar-Ilan, O. Livnah, J. Schloss, Z. Barak, and D. Chipman Homology modeling of the structure of bacterial acetohydroxy acid synthase and examination of the active site by site-directed mutagenesis Biochemistry 35 1996 16282 16291
48. Y. Muller, and G. Schulz Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase Science 259 1993 965 967
49. S. Falco, R. McDevitt, C.-F. Chui, M. Hartnett, S. Knowlton, C. Mauvais, J. Smith, and B. Mazur Engineering herbicide-resistant acetolactate synthase Dev Ind Microbiol 30 1989 187 194
50. R.G. Duggleby, S.S. Pang, H. Yu, and L.W. Guddat Systematic characterization of mutations in yeast acetohydroxyacid synthase Eur J Biochem 270 2003 2895 2904