2.2.1.6 A108V naturally occuring mutation 700782 2.2.1.6 A117D naturally occuring mutation 700782 2.2.1.6 A117E naturally occuring mutation 700782 2.2.1.6 A117F naturally occuring mutation 700782 2.2.1.6 A117H naturally occuring mutation 700782 2.2.1.6 A117I naturally occuring mutation 700782 2.2.1.6 A117K naturally occuring mutation 700782 2.2.1.6 A117L naturally occuring mutation 700782 2.2.1.6 A117M naturally occuring mutation 700782 2.2.1.6 A117N naturally occuring mutation 700782 2.2.1.6 A117P naturally occuring mutation 700782 2.2.1.6 A117Q naturally occuring mutation 700782 2.2.1.6 A117R naturally occuring mutation 700782 2.2.1.6 A117S naturally occuring mutation 700782 2.2.1.6 A117T naturally occuring mutation 700782 2.2.1.6 A117V naturally occuring mutation 700782 2.2.1.6 A117W naturally occuring mutation 700782 2.2.1.6 A117Y naturally occuring mutation 700782 2.2.1.6 A121T naturally occuring mutation 700782 2.2.1.6 A122V naturally occuring mutation 700782 2.2.1.6 A122V Nicotiana tabacum plants with transplastomic expression of mutant are specifically tolerant to pyrimidinylcarboxylate, imidazolinon, and sulfonylurea/pyrimidinylcarboxylate herbicides, respectively 700807 2.2.1.6 A122V reduced affinity for all Mg2+, thiamine diphosphate and FAD 395903 2.2.1.6 A200C naturally occuring mutation 700782 2.2.1.6 A200D naturally occuring mutation 700782 2.2.1.6 A200E naturally occuring mutation 700782 2.2.1.6 A200R naturally occuring mutation 700782 2.2.1.6 A200T naturally occuring mutation 700782 2.2.1.6 A200V naturally occuring mutation 700782 2.2.1.6 A200W naturally occuring mutation 700782 2.2.1.6 A200Y naturally occuring mutation 700782 2.2.1.6 A205F site-directed mutagenesis, the enzyme mutation confers resistance to imidazolinone, sulfonylurea, triazolopyrimidines, sulfonylaminocarbonyl triazolinones, and pyrimidinyl(thio)benzoate herbicides 734994 2.2.1.6 A205F the A205F substitution in acetolactate synthase, confirmed in a population of allotetraploid annual bluegrass, confers resistance to imidazolinone, sulfonylurea, triazolopyrimidines, sulfonylamino-carbonyl-triazolinones, and pyrimidinyl (thio) benzoate herbicides 734994 2.2.1.6 A205F the A205F substitution in acetolactate synthase, confirmed in a population of allotetraploid annual bluegrass, confers resistance to imidazolinone, sulfonylurea, triazolopyrimidines, sulfonylaminocarbonyl triazolinones, and pyrimidinyl(thio)benzoate herbicides 734994 2.2.1.6 A205F the mutation confers high resistance to imidazolinones, sulfonylureas, triazolopyrimidines, sulfonylamino-carbonyl-triazolinones, and pyrimidinyl (thio) benzoate herbicides 734994 2.2.1.6 A205V naturally occuring mutation 700782 2.2.1.6 A205V site-directed mutagenesis 734994 2.2.1.6 A205V the mutation confers resistance to imidazolinones, sulfonylureas, triazolopyrimidines, sulfonylamino-carbonyl-triazolinones, and pyrimidinyl (thio) benzoate herbicides 734994 2.2.1.6 A26V naturally occuring mutation 700782 2.2.1.6 A36V site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine 675377 2.2.1.6 A96T the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 A96V the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 C163S labile, readlily degraded 657718 2.2.1.6 C309S labile, readlily degraded 657718 2.2.1.6 C411A no enzymic activity, no binding of FAD 657718 2.2.1.6 C607S no significant effects 657718 2.2.1.6 C83A about 91% of wild-type activity 719466 2.2.1.6 C83S about 126% of wild-type activity 719466 2.2.1.6 C83T about 41% of wild-type activity 719466 2.2.1.6 D374A naturally occuring mutation 700782 2.2.1.6 D374A substrate inhibition at high concentrations, strong resistance to Londax and Cadre, 10fold increase in activation efficiency for thiamine diphosphate 658223 2.2.1.6 D374A/D375A strong resistance to Londax and to C, about 2fold increase in affinity for FAD, decrease in activation efficiency for thiamine diphosphate 658223 2.2.1.6 D374E greatly reduced activity, strong resistance to Londax, 8fold increase in affinity for FAD, decrease in activation efficiency for thiamine diphosphate 658223 2.2.1.6 D374E/D375E strong resistance to Londax and to C 658223 2.2.1.6 D375A about 10fold increase in Km-value, strong resistance to Londax 658223 2.2.1.6 D375A naturally occuring mutation 700782 2.2.1.6 D375E about 3fold reduction in Km-value, strong resistance to Londax, about 3fold increase in activation efficiency of FAD 658223 2.2.1.6 D375E naturally occuring mutation 700782 2.2.1.6 D376E the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate 757919 2.2.1.6 D379E naturally occuring mutation 700782 2.2.1.6 D379G naturally occuring mutation 700782 2.2.1.6 D379N naturally occuring mutation 700782 2.2.1.6 D379P naturally occuring mutation 700782 2.2.1.6 D379S naturally occuring mutation 700782 2.2.1.6 D379V naturally occuring mutation 700782 2.2.1.6 D379W naturally occuring mutation 700782 2.2.1.6 D428E 8% activity compared to wild-type 657912 2.2.1.6 D428N 8% activity compared to wild-type 657912 2.2.1.6 DELTA567 deletion of entire C-terminus including mobile loop and C-terminal lid, no enzymic activity 657852 2.2.1.6 DELTA567-582 deletion of mobile loop region 4.5% of activity compared to wild-type, increase in activation constant of thiamine diphosphate 657852 2.2.1.6 DELTA598 deletion of c-terminus maintaining mobile loop and C-terminal lid, 1.2% of activity compared to wild-type 657852 2.2.1.6 DELTA630 deletion of C-terminal lid, 4.5% of activity compared to wild-type, increase in activation constant of thiamine diphosphate 657852 2.2.1.6 DeltaQ217 mutation in subunit ilvB, mutant enzyme is activated by valine and resisitant to 3-chlorobutanoate and norleucine 698031 2.2.1.6 DeltaQ217 mutation in the beta-domain of the catalytic subunit, affecting regulation by valine. Mutation is located on the surface of the catalytic subunit dimer and lowers the interaction with the regulatory subunit 718706 2.2.1.6 E139A mutation in a conservative loop near the active center, mutant enzyme is activated by valine and resistant to 2-oxobutanoate 698031 2.2.1.6 E139A mutation in the alpha-domain of the catalytic subunit, affecting regulation by valine. Mutation is located on the surface of the catalytic subunit dimer and lowers the interaction with the regulatory subunit 718706 2.2.1.6 E47A 8% activity compared to wild-type 657912 2.2.1.6 E47A about 5% of wild-type activity 718895 2.2.1.6 E47Q 10% activity compared to wild-type 657912 2.2.1.6 E47Q about 5% of wild-type activity 718895 2.2.1.6 E49A site-directed mutagenesis, the mutant shows decreased activities and weakened thiamine diphosphate binding. The Km for substrate pyruvate is 22fold higher than that of the wild-type cALS. In addition, the E49A mutation also has a drastic effect on cofactor thiamine diphosphate activation. The half-saturating concentration (Kc) for thiamine diphosphate is 2000fold higher than that of wild-type cALS 733597 2.2.1.6 E49A the mutation causes a 190fold reduction in affinity for thiamine diphosphate 733597 2.2.1.6 E49D site-directed mutagenesis, the mutant exhibits normal substrate kinetics, with the Km for pyruvate equal to that of wild-type cALS 733597 2.2.1.6 E49D the mutation causes a 150fold reduction in affinity for thiamine diphosphate 733597 2.2.1.6 E49Q site-directed mutagenesis, the mutant shows decreased activities and weakened thiamine diphosphate binding, the Kc for ThDP that is 3600fold higher than that of wild-type cALS 733597 2.2.1.6 E49Q the mutant causes a 170fold reduction in affinity for thiamine diphosphate shows 7% of wild type activity 733597 2.2.1.6 E60A about 48% of wild-type activity 719466 2.2.1.6 E60Q about 1% of wild-type activity 719466 2.2.1.6 E85A site-directed mutagenesis, the mutation leads to severe drop in catalyticactivity with reduced affinity toward thiamine diphosphate, , the enzyme shows reduced activity compared to the wild-type enzyme -, 733747 2.2.1.6 E85A the mutation leads to severe drop in catalytic activity (0.08% of wild type activity) with reduced affinity toward thiamine diphosphate 733747 2.2.1.6 E85A the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate 733747 2.2.1.6 E85D site-directed mutagenesis, the mutation leads to severe drop in catalyticactivity with reduced affinity toward thiamine diphosphate 733747 2.2.1.6 E85D the mutation leads to severe drop in catalytic activity (2.23% of wild type activity) with reduced affinity toward thiamine diphosphate 733747 2.2.1.6 E85Q site-directed mutagenesis, the mutation leads to severe drop in catalyticactivity with reduced affinity toward thiamine diphosphate -, 733747 2.2.1.6 E85Q the mutation leads to severe drop in catalytic activity (1.2% of wild type activity) with reduced affinity toward thiamine diphosphate -, 733747 2.2.1.6 F109M both substrate affinity and kcat are significantly compromised. The specificity for 2-ketobutyrate as acceptor is not altered 718875 2.2.1.6 F147A 4fold decrease in vmax value, strong resistance to sulfonylurea inhibitors -, 719375 2.2.1.6 F147R 2.5fold decrease in vmax value, strong resistance to sulfonylurea inhibitors -, 719375 2.2.1.6 F180R the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 F204A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme 671854 2.2.1.6 F577D naturally occuring mutation 700782 2.2.1.6 F577E naturally occuring mutation 700782 2.2.1.6 F590C naturally occuring mutation 700782 2.2.1.6 F590G naturally occuring mutation 700782 2.2.1.6 F590L naturally occuring mutation 700782 2.2.1.6 F590N naturally occuring mutation 700782 2.2.1.6 F590R naturally occuring mutation 700782 2.2.1.6 G116N naturally occuring mutation 700782 2.2.1.6 G116S naturally occuring mutation 700782 2.2.1.6 G121A Nicotiana tabacum plants with transplastomic expression of mutant are specifically tolerant to pyrimidinylcarboxylate, imidazolinon, and sulfonylurea/pyrimidinylcarboxylate herbicides, respectively 700807 2.2.1.6 G14A site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine 675377 2.2.1.6 G14D site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine 675377 2.2.1.6 G16D mutation in the N-terminal part of the regulatory subunit ilvN, affecting regulation by valine. Mutation considerably reduces the interaction of the subunits 718706 2.2.1.6 G16D/E105stop no enzymic activity after in vitro reconstitution with large subunit 657717 2.2.1.6 G654D mutant isolated from Ontario population. Mutant confers resistance to herbicide imazethapyr, and cross-resistance to nicosulfuron and flucarbazone 701267 2.2.1.6 G95A the naturally occuring mutation leads to resistance against pyrimidinyl carboxy herbicides, e.g. bispyribac-sodium 700769 2.2.1.6 H111F site-directed mutagenesis, the mutant enzyme exhibits about 50fold lower specific activity with significant reduction in kcat compared to the wild-type enzyme 733987 2.2.1.6 H111F the mutant displays 26fold increase in Km value compared to the wild type enzyme 733987 2.2.1.6 H111R site-directed mutagenesis, the mutant enzyme exhibits increasedspecific activity and kcat compared to the wild-type enzyme 733987 2.2.1.6 H111R the mutant displays 17fold increase in Km value compared to the wild type enzyme 733987 2.2.1.6 H181A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme 671854 2.2.1.6 H205A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme 671854 2.2.1.6 H219A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme 671854 2.2.1.6 H28A site-directed mutagenesis, the mutant enzyme is much less able to catalyze the C-C bond formation as the wild-type enzyme, while the ability for C-C bond cleavage is still intact, the H28A variant shows an 8fold decrease in the formation of (R)-phenylacetylcarbinol (12%), but 1,2-diketone cleavage is nearly unaffected (78% conversion) -, 733089 2.2.1.6 H28A/N484A site-directed mutagenesis, the double mutant catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol, variant H28A/N484A shows acceptable formation of (R)-phenylacetylcarbinol (73%), but conversion toward the cleavage product is decreased by a factor of five (17% conversion), the mutant is also active with 1,2-diketone, e.g. cyclohexane-1,2-dione, in contrast to the wild-type enzyme, mutant substrate specificity amd enantioselectivity, overview -, 733089 2.2.1.6 H351F 5fold increase in Km-value, weak resistance to Londax and Cadre, difference in secondary structure compared to wild-type 657720 2.2.1.6 H351M 18fold increase in Km-value, strong resistance to Londax and Cadre, difference in secondary structure compared to wild-type 657720 2.2.1.6 H351Q 60fold increase in Km-value, strong resistance to Londax and Cadre, difference in secondary structure compared to wild-type 657720 2.2.1.6 H351Q naturally occuring mutation 700782 2.2.1.6 H392M no significant effects 657720 2.2.1.6 H474R site-directed mutagenesis 735039 2.2.1.6 H474R site-directed mutagenesis, the reaction specificity of acetolactate synthase from Thermus thermophilus is redirected to catalyze acetaldehyde formation to develop a thermophilic pyruvate decarboxylase. The mutation likely generates two new hydrogen bonds near the thiamine diphosphate-binding site. These hydrogen bonds might result in the better accessibility of H+ to the substrate-cofactor-enzyme intermediate and a shift in the reaction specificity of the enzyme 735039 2.2.1.6 H474R the mutant shows reduced activity compared to the wild type enzyme 735039 2.2.1.6 H487F no enzymic activity, no affinity for FAD 657720 2.2.1.6 H487L no enzymic activity, no affinity for FAD 657720 2.2.1.6 H747R mutation leads to 3fold increased acetaldehyde formation, with 30% decrease in acetolactate formation 735039 2.2.1.6 H76A site-directed mutagenesis, almost inactive mutant -, 733089 2.2.1.6 H76A/Q116A site-directed mutagenesis, inactive mutant 733089 2.2.1.6 H84A site-directed mutagenesis, the mutation leads to the loss of many hydrogen bonds among residues His84, Glu85, and Gln86 in wild-type enzyme -, 733747 2.2.1.6 H84A the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate -, 733747 2.2.1.6 H84T site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme 733747 2.2.1.6 H84T the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate 733747 2.2.1.6 I106V/A135P after in vitro reconstitution with large subunit, enzymic activity comparable to wild-type 657717 2.2.1.6 K139R site-directed mutagenesis -, 735039 2.2.1.6 K139R the mutant shows slightly reduced activity compared to the wild type enzyme -, 735039 2.2.1.6 K176G the naturally occuring mutation, substitution of two adenines to guanines in the ilvB gene, causes a cold-sensitive phenotype of mutant strain JH642. The acetolactate synthase efficiency in strain JH642 is reduced by 51fold 697972 2.2.1.6 K218A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme 671854 2.2.1.6 K219Q no residual activity, no binding of FAD 657724 2.2.1.6 K251D naturally occuring mutation 700782 2.2.1.6 K251E naturally occuring mutation 700782 2.2.1.6 K251N naturally occuring mutation 700782 2.2.1.6 K251P naturally occuring mutation 700782 2.2.1.6 K251T naturally occuring mutation 700782 2.2.1.6 K255F naturally occuring mutation 700782 2.2.1.6 K255F strong resistance to Londax, Cadre and N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide 657724 2.2.1.6 K255Q naturally occuring mutation 700782 2.2.1.6 K255Q strong resistance to Londax, Cadre and N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide 657724 2.2.1.6 K299Q no significant effects 657724 2.2.1.6 K40H site-directed mutagenesis, the half-life of the mutant at 50°C is 44 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type -, 733658 2.2.1.6 K40I site-directed mutagenesis, the half-life of the mutant at 50°C is 89 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type -, 733658 2.2.1.6 K40I the mutant shows slightly improved activity towards 2-oxoisovalerate compared to the wild type enzyme 733658 2.2.1.6 K40Y site-directed mutagenesis, the half-life of the mutant at 50°C is 110 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type 733658 2.2.1.6 L131R site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine 675377 2.2.1.6 L141A 5fold decrease in vmax value -, 719375 2.2.1.6 L16A site-directed mutagenesis of the regulatory subunit, the mutant shows increased sensitivity to valine inhibition compared to the wild-type subunit 675377 2.2.1.6 L177A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme 671854 2.2.1.6 L18F mutation in the N-terminal part of the regulatory subunit ilvN, affecting regulation by valine. Mutation does not influence the interaction of the subunits 718706 2.2.1.6 L18F no enzymic activity after in vitro reconstitution with large subunit 657717 2.2.1.6 L222A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme 671854 2.2.1.6 L476M about 34% of wild-type activity 719466 2.2.1.6 L476M/Q480W about 47% of wild-type activity 719466 2.2.1.6 L9A site-directed mutagenesis of the regulatory subunit, the mutant shows slightly decreased sensitivity to valine inhibition compared to the wild-type subunit 675377 2.2.1.6 L9H site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine 675377 2.2.1.6 L9V site-directed mutagenesis of the regulatory subunit, the mutant shows slightly decreased sensitivity to valine inhibition compared to the wild-type subunit 675377 2.2.1.6 M124E naturally occuring mutation 700782 2.2.1.6 M250A large decrease in activity, increase in Km-value 660390 2.2.1.6 M263A about 16% of wild-type activity 719466 2.2.1.6 M350C naturally occuring mutation 700782 2.2.1.6 M354C naturally occuring mutation 700782 2.2.1.6 M354K naturally occuring mutation 700782 2.2.1.6 M354V naturally occuring mutation 700782 2.2.1.6 M460N naturally occuring mutation 700782 2.2.1.6 M483N site-directed mutagenesis, the mutant is inactivated at 50°C 733658 2.2.1.6 M569C naturally occuring mutation 700782 2.2.1.6 M98E the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 M98H the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 M98I the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 additional information among 28 populations resistant to herbiced tribenuron, nine individuals have only the mutant ALS gene and are homozygous, 18 individuals have both the wild type and the mutant ALS gene and are heterozygous, whereas one individual is heterozygous but with two different mutant ALS alleles 701407 2.2.1.6 additional information cloning of a herbicide-resistant acetohydroxyacid synthase gene from Pseudomonas sp. Lm10. Sequence analysis shows that the regulatory subunit of the resisitant enzyme is identical to that of Pseudomonas putida KT2440, whereas six mutations are found in the catalytic subunit, i.e. resistant AHAS/sensitive AHAS: H134N, A135P, S136T, I210V, F264Y, and S486W -, 719329 2.2.1.6 additional information construction of a mutant with a deleted C-terminal domain in the regulatory subunit IlvN. The constructed enzyme shows altered kinetic properties, i.e., an about twofold-lower Km for the substrate pyruvate and an about fourfold-lower Vmax, a slightly increased Km for the substrate alpha-ketobutyrate with an about twofold-lower Vmax, and insensitivity against the inhibitors L-valine, L-isoleucine, and L-leucine. Introduction of the mutant into the L-lysine producers Corynebacterium glutamicum DM1729 and DM1933 increases L-lysine formation by 43% and 36%, respectively. Complete inactivation of the AHAS in Corynebacterium glutamicum DM1729 and DM1933 by deletion of the ilvB gene, encoding the catalytic subunit of AHAS, leads to L-valine, L-isoleucine, and L-leucine auxotrophy and to further-improved L-lysine production. In batch fermentations, the mutant produces about 85% more L-lysine and shows an 85%-higher substrate-specific product yield 695780 2.2.1.6 additional information engineering of a strain of Pyrococcus furiosus to contain an additional pathway for ethanol production. Enzyme ALS deletion abolishes acetoin formation and improves ethanol production in the alcohol dehydrogenase ADHA strain. High level expression of enzyme ALS uncouples the temperature-dependence of acetoin formation 734625 2.2.1.6 additional information expression of an Ilv2 variant that lacks the N-terminal mitochondrial targeting sequence leads to highly elevated diacetyl levels comparable to a petite strain. Expression of a mutant allele of the gamma-subunit of the F1-ATPase, ATP3-5, could be an attractive way to reduce diacetyl formation by petite strains 718641 2.2.1.6 additional information generation of the deletion mutants DELTAMoilv2 and DELTAMoilv6. Phenotypic analysis shows that both mutants are auxotrophic for leucine, isoleucine and valine, and are defective in conidial morphogenesis, appressorial penetration and pathogenicity -, 734734 2.2.1.6 additional information genotyping by random mutagenesis, error-prone PCR and mutant library screening leading to the identification of a quadruple mutant with 3.1fold higher acetaldehyde-forming activity than the wild-type, mutant reaction-specificity profiles -, 735039 2.2.1.6 additional information identification and phenotypes of herbicide-resistant mutant enzymes, overview 700782 2.2.1.6 additional information identification of naturally occuring mutations leading to herbicide resistance of the plants, e.g. chlorsulfuron-resistant plants, overview. ALS-inhibiting herbicides occur in Lactuca serriola within a relatively small geographical area 701265 2.2.1.6 additional information isozyme AHAS II mutants of residues Phe109, Met250, Arg276 and Trp464 are nearly inactive in (S)-2-acetolactate formation, but show increased activity with pyruvate and benzaldehyde compared to the wild-type isozyme 677228 2.2.1.6 additional information mutants with overexpression of 2-acetolactate synthase (ALS), 2-acetolactate decarboxylase, and acetoin reductase, either individually or in combination, are constructed to improve 2,3-butanediol production in Klebsiella pneumoniae. The strain (KG-rs) that overexpresses both 2-acetolactate synthase and acetoin reductase shows an improved 2,3-butanediol yield. When cultured in the media with five different carbon sources (glucose, galactose, fructose, sucrose, and lactose), the mutant exhibits higher 2,3-butanediol productivity and production than the parental strain in all the tested carbon sources except for lactose. The 2,3-butanediol production of strain KG-rs in a batch fermentation with glucose as the carbon source is 12% higher than that of the parental strain, overview -, 733547 2.2.1.6 additional information mutations of the residues M8 and M13 of the small, regulatory subunit encoded by gene ilvN result in reduced sensitivity of the mutant enzymes to feedback inhibition which leads to increased production of valine as well as of isoleucine and leucine 667251 2.2.1.6 additional information several mutations, including deletion mutations W548deletion, P171deletion and S627deletion, reduce the enzyme's sensitivity to herbicides, overview 699740 2.2.1.6 additional information shortening of the regulatory subunit to 107 residues reduces the interaction with the catalytic subunit essentially 718706 2.2.1.6 additional information structure-guided mutagenesis strategy to generate enzyme AlsS variants -, 733658 2.2.1.6 additional information substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview -, 733089 2.2.1.6 additional information the 138th (alanine) and 404th (valine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme -, 756622 2.2.1.6 additional information the 138th (valine) and 404th (alanine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme. The 138th valine of subunit IlvB is beneficial for the L-valine biosynthesis -, 756622 2.2.1.6 additional information the aspartate substitution significantly affects the activation of thiamine diphosphate. The Kc for thiamine diphosphate is determined to be 280fold higher than that of wild-type cALS 733597 2.2.1.6 additional information the truncated mutant DELTA80 is resistant to inhibition by valine 675377 2.2.1.6 N11A site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine 675377 2.2.1.6 N11D site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit 675377 2.2.1.6 N11H site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit 675377 2.2.1.6 N29D site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit 675377 2.2.1.6 N29H site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit 675377 2.2.1.6 N484A site-directed mutagenesis 733089 2.2.1.6 P126A site-directed mutagenesis, the mutant exhibits similar kinetics but significantly lower activity compared to the wild-type enzyme -, 733745 2.2.1.6 P126A, the mutant exhibits significantly lower activity than the wild type enzyme -, 733745 2.2.1.6 P126E inactive -, 733745 2.2.1.6 P126E site-directed mutagenesis, inactive mutant -, 733745 2.2.1.6 P126T site-directed mutagenesis, the mutant exhibits significantly lower activity than wild-type enzyme and a significantly decreased preference toward thiamine diphosphate as cofactor -, 733745 2.2.1.6 P126T the mutant exhibits significantly lower activity than the wild type enzyme -, 733745 2.2.1.6 P126V site-directed mutagenesis, the mutant exhibits significantly lower activity than wild-type enzyme and a significantly decreased preference toward pyruvate as substrate -, 733745 2.2.1.6 P126V the mutant exhibits significantly lower activity than the wild type enzyme -, 733745 2.2.1.6 P171A the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 P171Q the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 P171S the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 P192A naturally occuring mutation 700782 2.2.1.6 P192E naturally occuring mutation 700782 2.2.1.6 P192L naturally occuring mutation 700782 2.2.1.6 P192Q naturally occuring mutation 700782 2.2.1.6 P192R naturally occuring mutation 700782 2.2.1.6 P192S naturally occuring mutation 700782 2.2.1.6 P192V naturally occuring mutation 700782 2.2.1.6 P192W naturally occuring mutation 700782 2.2.1.6 P192Y naturally occuring mutation 700782 2.2.1.6 P197A mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding. Most common mutation among 28 populations resistant to tribenuron 701407 2.2.1.6 P197E site-directed mutagenesis, the mutation confers broad-spectrum resistance across ALS inhibitors. A subpopulation (WRR04) is generated and is individually homozygous for the Pro197Glu substitution. The WRR04 population exhibits broad-spectrum resistance to tribenuron (318fold), pyrithiobac sodium (over 197fold), pyroxsulam (81fold), florasulam (over 36fold) and imazethapyr (11fold). The ALS from WRR04 shows high resistance to all the tested ALS inhibitors 734841 2.2.1.6 P197E the mutation leads to high resistance to inhibitors tribenuron, pyrithiobac sodium, pyroxsulam (TP, 81-fold), florasulam, and imazethapyr 734841 2.2.1.6 P197H the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate 757919 2.2.1.6 P197L mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding 701407 2.2.1.6 P197L the mutation causes serious cross-resistance to most types of enzyme inhibitors 757036 2.2.1.6 P197L the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate 757919 2.2.1.6 P197R mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding 701407 2.2.1.6 P197S mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding 701407 2.2.1.6 P197S naturally occuring mutation 700782 2.2.1.6 P197S naturally occuring mutation leading to resistance against the sulfonylurea herbicide imazosulfuron 735336 2.2.1.6 P197S Nicotiana tabacum plants with transplastomic expression of mutant are specifically tolerant to pyrimidinylcarboxylate, imidazolinon, and sulfonylurea/pyrimidinylcarboxylate herbicides, respectively 700807 2.2.1.6 P197S the mutant shows increased resistance against imazosulfuron 735336 2.2.1.6 P197T mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding 701407 2.2.1.6 P197T naturally occuring mutation leading to resistance against the sulfonylurea herbicide imazosulfuron 735336 2.2.1.6 P197T the mutant shows increased resistance against imazosulfuron 735336 2.2.1.6 P197T the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate 757919 2.2.1.6 P206A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme 671854 2.2.1.6 P87A site-directed mutagenesis, the half-life of the mutant at 50°C is 33 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type 733658 2.2.1.6 Q108stop no enzymic activity after in vitro reconstitution with large subunit 657717 2.2.1.6 Q110A about 3% of wild-type activity 718895 2.2.1.6 Q110E about 1.5% of wild-type activity 718895 2.2.1.6 Q110H about 15% of wild-type activity 718895 2.2.1.6 Q110N about 8% of wild-type activity 718895 2.2.1.6 Q112E site-directed mutagenesis, the mutant enzyme exhibits about 50fold lower specific activity with significant reduction in kcat compared to the wild-type enzyme 733987 2.2.1.6 Q112E the mutant exhibits significantly lower specific activity with 70fold higher Ks for thiamine diphosphate compared to the wild type enzyme 733987 2.2.1.6 Q112N site-directed mutagenesis, the mutant enzyme exhibits about 50fold lower specific activity with significant reduction in kcat compared to the wild-type enzyme 733987 2.2.1.6 Q112N the mutant exhibits significantly lower specific activity with 15fold higher Ks for thiamine diphosphate compared to the wild type enzyme 733987 2.2.1.6 Q112V site-directed mutagenesis, the mutant enzyme exhibits about 50fold lower specific activity with significant reduction in kcat compared to the wild-type enzyme 733987 2.2.1.6 Q112V the mutant exhibits significantly lower specific activity with 10fold higher Ks for thiamine diphosphate compared to the wild type enzyme 733987 2.2.1.6 Q116A site-directed mutagenesis, inactive mutant -, 733089 2.2.1.6 Q124S site-directed mutagenesis, the half-life of the mutant at 50°C is 42 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type 733658 2.2.1.6 Q411E site-directed mutagenesis, the mutant enzyme exhibits increased specific activity and kcat compared to the wild-type enzyme 733987 2.2.1.6 Q411E the mutant shows a 10fold rise in Km and a 20fold increase in Ks for thiamine diphosphate compared to the wild type enzyme 733987 2.2.1.6 Q411N site-directed mutagenesis, the mutant enzyme has a 3fold increased Km compared to the wild-type enzyme 733987 2.2.1.6 Q411N the mutant exhibits increased specific activity and kcat compared to the wild type enzyme 733987 2.2.1.6 Q424S site-directed mutagenesis, the half-life of the mutant at 50°C is 104 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows increased activity compared to the wild-type 733658 2.2.1.6 Q424S/Q487S site-directed mutagenesis, the half-life of the mutant at 50°C is 94 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type 733658 2.2.1.6 Q480W about 22% of wild-type activity 719466 2.2.1.6 Q487A mutation diminishes decarboxylase activity but maintains the synthase activity 695784 2.2.1.6 Q487A wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity -, 695784 2.2.1.6 Q487G mutation diminishes decarboxylase activity but maintains the synthase activity 695784 2.2.1.6 Q487G wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity -, 695784 2.2.1.6 Q487I complete loss of synthase activity 695784 2.2.1.6 Q487I loss of acetolactate synthase activity, decrease in decarboxylase activity -, 695784 2.2.1.6 Q487L complete loss of synthase activity 695784 2.2.1.6 Q487L loss of acetolactate synthase activity, decrease in decarboxylase activity -, 695784 2.2.1.6 Q487S mutation diminishes decarboxylase activity but maintains the synthase activity 695784 2.2.1.6 Q487S site-directed mutagenesis, the half-life of the mutant at 50°C is 22 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type -, 733658 2.2.1.6 Q487S the mutant shows wild type activity towards 2-oxoisovalerate -, 733658 2.2.1.6 Q487S wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity -, 695784 2.2.1.6 Q86A site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme 733747 2.2.1.6 Q86A the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate 733747 2.2.1.6 Q86W site-directed mutagenesis, inactive mutant 733747 2.2.1.6 Q86W the mutation completely abolishes the enzyme's activity 733747 2.2.1.6 R141A site-directed mutagenesis, inactive mutant, unable to bind the cofactor FAD 674354 2.2.1.6 R141F site-directed mutagenesis, inactive mutant, unable to bind the cofactor FAD 674354 2.2.1.6 R141K site-directed mutagenesis, the mutant shows reduced activity and activation by thiamine diphosphate compared to the wild-type enzyme, the mutant is partially resistant to herbicides, e.g. Londax, Cadre, and/or TP 674354 2.2.1.6 R173A the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 R173E the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 R199E naturally occuring mutation 700782 2.2.1.6 R216A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme 671854 2.2.1.6 R269Q about 0.5% of wild-type activity 719466 2.2.1.6 R276K large decrease in activity, increase in Km-value 660390 2.2.1.6 R289K about 11% of wild-type activity 719466 2.2.1.6 R372F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, the mutant is partially resistant to herbicides, e.g. Londax, Cadre, and/or TP 674354 2.2.1.6 R372K site-directed mutagenesis, the mutant shows reduced activity and activation by FAD compared to the wild-type enzyme, the mutant is partially resistant to herbicides, e.g. Londax, Cadre, and/or TP 674354 2.2.1.6 R372S/F373P/D374V site-directed mutagenesis, mutation of the conserved motif 372RFDDR376 results in abolished FAD binding and highly reduced activity 672866 2.2.1.6 R372S/F373P/D374V/D375E site-directed mutagenesis, mutation of the conserved motif 372RFDDR376 results in abolished FAD binding and highly reduced activity 672866 2.2.1.6 R372S/F373P/D374V/D375E/R376Y site-directed mutagenesis, mutation of the conserved motif 372RFDDR376 results in abolished FAD binding and highly reduced activity, the mutant is resistant to herbocides 672866 2.2.1.6 R376F site-directed mutagenesis, inactive mutant, unable to bind the cofactor FAD 674354 2.2.1.6 R376K site-directed mutagenesis, the mutant shows reduced activity and activation by FAD compared to the wild-type enzyme, the mutant is partially resistant to herbicides, e.g. Londax, Cadre, and/or TP 674354 2.2.1.6 S167A 73% of wild-type activity 719010 2.2.1.6 S167F inactive, mutation abolishes the binding affinity for cofactor FAD. The far-UV spectrum is similar to wild-type 719010 2.2.1.6 S167R 250% of wild-type activity 719010 2.2.1.6 S212A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme 671854 2.2.1.6 S506A 230% of wild-type activity 719010 2.2.1.6 S506F inactive, mutation abolishes the binding affinity for cofactor FAD. The far-UV spectrum is similar to wild-type 719010 2.2.1.6 S506R 183% of wild-type activity 719010 2.2.1.6 S539A 73% of wild-type activity, strong resistance to herbicides NC-311, a sulfonylurea, Cadre, an imidazolinone, and a triazolopyrimidine 719010 2.2.1.6 S539F 171% of wild-type activity, strong resistance to herbicides NC-311, a sulfonylurea, Cadre, an imidazolinone, and a triazolopyrimidine 719010 2.2.1.6 S539R 30% of wild-type activity 719010 2.2.1.6 S627D the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 S627F the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 S627I the mutation contributes to herbicide resistance 757706 2.2.1.6 S627I the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 S627N the mutation confers tolerance against imidazolinone herbicides, including imazethapyr and imazamox. The mutant is tolerant to imidazolinone but the catalytic efficiency of the mutated enzyme decreases in its presence. Moreover, the activity of the mutated enzyme decreases more in the presence of imazethapyr than in the presence of imazamox 758092 2.2.1.6 S627N the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 S627T the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 S638N the mutant is more resistant to imidazolinone herbicides than the wild type in contrast to sulfonylurea herbicides that inhibit the mutant as well as the wild type enzyme 755711 2.2.1.6 S652T naturally occuring mutation 700782 2.2.1.6 S653F naturally occuring mutation 700782 2.2.1.6 S653I mutant isolated from Ontario population. Mutant confers resistance to herbicide imazethapyr, and cross-resistance to nicosulfuron and flucarbazone 701267 2.2.1.6 S653N binds FAD more strongly than the wild-type enzyme 395903 2.2.1.6 S653N mutant isolated from Ontario population. Mutant confers resistance to herbicide imazethapyr, and cross-resistance to nicosulfuron and flucarbazone 701267 2.2.1.6 S653N naturally occuring mutation 700782 2.2.1.6 S653T mutant isolated from Ontario population. Mutant confers resistance to herbicide imazethapyr, and cross-resistance to nicosulfuron and flucarbazone 701267 2.2.1.6 S653T naturally occuring mutation 700782 2.2.1.6 T34C site-directed mutagenesis of the regulatory subunit, the mutant shows decreased sensitivity to valine inhibition compared to the wild-type subunit 675377 2.2.1.6 T34I site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit 675377 2.2.1.6 T47C site-directed mutagenesis of the regulatory subunit, the mutant shows decreased sensitivity to valine inhibition compared to the wild-type subunit 675377 2.2.1.6 T84V site-directed mutagenesis, the half-life of the mutant at 50°C is 2.5 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type 733658 2.2.1.6 V153D site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine 675377 2.2.1.6 V172A site-directed mutagenesis 735039 2.2.1.6 V172A the mutant shows reduced activity compared to the wild type enzyme 735039 2.2.1.6 V17D mutation in the N-terminal part of the regulatory subunit ilvN, affecting regulation by valine. Mutation considerably reduces the interaction of the subunits 718706 2.2.1.6 V17D no enzymic activity after in vitro reconstitution with large subunit 657717 2.2.1.6 V17D/F30L no enzymic activity after in vitro reconstitution with large subunit 657717 2.2.1.6 V35A site-directed mutagenesis of the regulatory subunit, the mutant shows decreased sensitivity to valine inhibition compared to the wild-type subunit 675377 2.2.1.6 V375A mutation in isozyme AHAS II, allows 2-oxo-butanoate to be a good first substrate and the mutant enzyme can synthesize 2-propionyl-2-hydroxybutanoate 699604 2.2.1.6 V375A slightly reduced kcat value with a moderate increase of the apparent KM of pyruvate. The specificity for 2-ketobutyrate as acceptor is not altered 718875 2.2.1.6 V375I slightly reduced kcat value with a moderate increase of the apparent KM of pyruvate. The specificity for 2-ketobutyrate as acceptor is not altered 718875 2.2.1.6 V391A about 3% of wild-type activity 719466 2.2.1.6 V477I about 8% of wild-type activity 719466 2.2.1.6 V570Q naturally occuring mutation 700782 2.2.1.6 V583A naturally occuring mutation 700782 2.2.1.6 V583C naturally occuring mutation 700782 2.2.1.6 V583N naturally occuring mutation 700782 2.2.1.6 V583Y naturally occuring mutation 700782 2.2.1.6 V99M naturally occuring mutation 700782 2.2.1.6 W464A naturally occuring mutation 700782 2.2.1.6 W464L decrease in activity, increase in Km-value 660390 2.2.1.6 W464L naturally occuring mutation 700782 2.2.1.6 W464L the mutant of isozyme AHAS II has lost the preference for 2-ketobutyrate as second substrate 677228 2.2.1.6 W464Q naturally occuring mutation 700782 2.2.1.6 W464Y naturally occuring mutation 700782 2.2.1.6 W46F naturally occuring mutation 700782 2.2.1.6 W548C the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 W548F the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 W548L the mutation contributes to herbicide resistance 757706 2.2.1.6 W548L the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 W548L/S627I a naturally occuring mutation, the recombinant enzyme shows resistance to multiple herbicides including pyrimidinylcarboxylate, sulfonylurea and imidazolinone herbicides, and shows stronger resistance to pyrimidinylcarboxylate herbicides than to other herbicides. Bispyribac-sodium, a pyrimidinylcarboxylate herbicide, has almost no effect on the enzyme at up to 100m M, which is an approximately 10000fold higher concentration than the concentration required for 50% inhibition of the wild-type. The resistance level of the double mutant W548L/S627I BS is stronger than the additive effect predicted from the degree of resistance of each single amino acid mutated ALS, phenotype, overview 699740 2.2.1.6 W548L/S627I mutant confers resistance to multiple herbicides including pyrimidinylcarboxylate, sulfonylurea and imidazolinone herbicides, and shows stronger resistance to pyrimidinylcarboxylate herbicides than to other herbicides. Bispyribac-sodium has almost no effect on the enzyme even at 100 mM, which is an approximately 10000fold higher concentration than the concentration required for 50% inhibition of the wild-type. The resistance level of W548L/S627I is stronger than the additive effect predicted from the degree of resistance of each single amino acid mutated. Transformed rice cells carrying this gene and a regenerated rice plant express resistance to bispyribac-sodium 699740 2.2.1.6 W548L/S627I use of two-point mutated gene of acetolactate synthase from herbicide-resistant rice callus as a selectable marker gene in production of transgenic soybeans. T1 soybeans grown from one regenerated plant after selection of the acetolactate synthase targeting pyrimidinyl-carboxy herbicide bispyribacsodium exhibit herbicide resistance, and the introduction and expression of the gene is confirmed by genetic analysis. The selective culturing is applicable to the production of transgenic soybeans 700729 2.2.1.6 W548S the naturally occuring mutation reduces the enzyme's sensitivity to herbicides 699740 2.2.1.6 W557L naturally occuring mutation 700782 2.2.1.6 W561R 30fold decrease in vmax value, strong resistance to sulfonylurea inhibitors -, 719375 2.2.1.6 W563C naturally occuring mutation 700782 2.2.1.6 W563S naturally occuring mutation 700782 2.2.1.6 W573F site-directed mutagenesis, the mutant shows 69fold reduced activity compared to the wild-type enzyme, substitution of the W573 residue causes significant perturbations in the activation process and in the binding site of thiamine diphosphate 672868 2.2.1.6 W574L insensitive to sulfonurea herbicides 395903 2.2.1.6 W574L naturally occuring mutation 700782 2.2.1.6 W574L naturally occuring mutation leading to resistance against the sulfonylurea herbicide imazosulfuron 735336 2.2.1.6 W574L site-directed mutagenesis 734994 2.2.1.6 W574L the mutant shows increased resistance against imazosulfuron 735336 2.2.1.6 W574L the mutation causes herbicide resistance. The mutant enzyme is over 9000fold more resistant towards metsulfuron-methyl and imazethapyr than the wild type enzyme 757918 2.2.1.6 W574L the mutation confers resistance to imidazolinones, sulfonylureas, triazolopyrimidines, sulfonylamino-carbonyl-triazolinones, and pyrimidinyl (thio) benzoate herbicides 734994 2.2.1.6 W574L the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate 757919 2.2.1.6 W574S naturally occuring mutation 700782 2.2.1.6 W574S reduction in sensitivity to sulfonurea herbicides compared to the wild-type enzyme 395903 2.2.1.6 W586A naturally occuring mutation 700782 2.2.1.6 W586C naturally occuring mutation 700782 2.2.1.6 W586E naturally occuring mutation 700782 2.2.1.6 W586G naturally occuring mutation 700782 2.2.1.6 W586H naturally occuring mutation 700782 2.2.1.6 W586I naturally occuring mutation 700782 2.2.1.6 W586K naturally occuring mutation 700782 2.2.1.6 W586L naturally occuring mutation 700782 2.2.1.6 W586N naturally occuring mutation 700782 2.2.1.6 W586S naturally occuring mutation 700782 2.2.1.6 W586V naturally occuring mutation 700782 2.2.1.6 Y35N site-directed mutagenesis 735039 2.2.1.6 Y35N the mutant shows reduced activity compared to the wild type enzyme 735039 2.2.1.6 Y35N/K139R/V172A/H474R shows 3.1fold higher acetaldehyde-forming activity than the wild-type 735039 2.2.1.6 Y35N/K139R/V172A/H474R the mutant shows strongly reduced activity compared to the wild type enzyme 735039 2.2.1.6 Y481A site-directed mutagenesis, the half-life of the mutant at 50°C is 19 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type 733658