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Literature summary extracted from

  • Duggleby, R.G.; McCourt, J.A.; Guddat, L.W.
    Structure and mechanism of inhibition of plant acetohydroxyacid synthase (2008), Plant Physiol. Biochem., 46, 309-324.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.2.1.6 drug development the enzyme is a target for development of herbicides, overview Nicotiana tabacum
2.2.1.6 drug development the enzyme is a target for development of herbicides, overview Arabidopsis thaliana
2.2.1.6 drug development the enzyme is a target for development of herbicides, overview Brassica napus
2.2.1.6 drug development the enzyme is a target for development of herbicides, overview Helianthus annuus
2.2.1.6 drug development the enzyme is a target for development of herbicides, overview Gossypium hirsutum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.2.1.6 resolution of the diffraction data for herbicide-AHAS complexes varies between 2.2 A for the chlorsulfuron-bound structure to 2.8 A for the chlorimuron ethyl-bound structure, between 2.5 and 2.9 A for other catalytic subunit-herbicide complexes, overview Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
2.2.1.6 A108V naturally occuring mutation Escherichia coli
2.2.1.6 A117D naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117E naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117F naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117H naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117I naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117K naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117L naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117M naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117N naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117P naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117Q naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117R naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117S naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117T naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117V naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117W naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A117Y naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A121T naturally occuring mutation Nicotiana tabacum
2.2.1.6 A122V naturally occuring mutation Arabidopsis thaliana
2.2.1.6 A200C naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A200D naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A200E naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A200R naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A200T naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A200V naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A200W naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A200Y naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 A205V naturally occuring mutation Helianthus annuus
2.2.1.6 A26V naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 D374A naturally occuring mutation Nicotiana tabacum
2.2.1.6 D375A naturally occuring mutation Nicotiana tabacum
2.2.1.6 D375E naturally occuring mutation Nicotiana tabacum
2.2.1.6 D379E naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 D379G naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 D379N naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 D379P naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 D379S naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 D379V naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 D379W naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 F577D naturally occuring mutation Nicotiana tabacum
2.2.1.6 F577E naturally occuring mutation Nicotiana tabacum
2.2.1.6 F590C naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 F590G naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 F590L naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 F590N naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 F590R naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 G116N naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 G116S naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 H351Q naturally occuring mutation Nicotiana tabacum
2.2.1.6 K251D naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 K251E naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 K251N naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 K251P naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 K251T naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 K255F naturally occuring mutation Nicotiana tabacum
2.2.1.6 K255Q naturally occuring mutation Nicotiana tabacum
2.2.1.6 M124E naturally occuring mutation Arabidopsis thaliana
2.2.1.6 M350C naturally occuring mutation Nicotiana tabacum
2.2.1.6 M354C naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 M354K naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 M354V naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 M460N naturally occuring mutation Escherichia coli
2.2.1.6 M569C naturally occuring mutation Nicotiana tabacum
2.2.1.6 additional information identification and phenotypes of herbicide-resistant mutant enzymes, overview Escherichia coli
2.2.1.6 additional information identification and phenotypes of herbicide-resistant mutant enzymes, overview Nicotiana tabacum
2.2.1.6 additional information identification and phenotypes of herbicide-resistant mutant enzymes, overview Arabidopsis thaliana
2.2.1.6 additional information identification and phenotypes of herbicide-resistant mutant enzymes, overview Brassica napus
2.2.1.6 additional information identification and phenotypes of herbicide-resistant mutant enzymes, overview Helianthus annuus
2.2.1.6 additional information identification and phenotypes of herbicide-resistant mutant enzymes, overview Gossypium hirsutum
2.2.1.6 additional information identification and phenotypes of herbicide-resistant mutant enzymes, overview Saccharomyces cerevisiae
2.2.1.6 P192A naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 P192E naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 P192L naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 P192Q naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 P192R naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 P192S naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 P192V naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 P192W naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 P192Y naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 P197S naturally occuring mutation Arabidopsis thaliana
2.2.1.6 R199E naturally occuring mutation Arabidopsis thaliana
2.2.1.6 S652T naturally occuring mutation Nicotiana tabacum
2.2.1.6 S653F naturally occuring mutation Arabidopsis thaliana
2.2.1.6 S653N naturally occuring mutation Arabidopsis thaliana
2.2.1.6 S653T naturally occuring mutation Arabidopsis thaliana
2.2.1.6 V570Q naturally occuring mutation Nicotiana tabacum
2.2.1.6 V583A naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 V583C naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 V583N naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 V583Y naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 V99M naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 W464A naturally occuring mutation Escherichia coli
2.2.1.6 W464L naturally occuring mutation Escherichia coli
2.2.1.6 W464Q naturally occuring mutation Escherichia coli
2.2.1.6 W464Y naturally occuring mutation Escherichia coli
2.2.1.6 W46F naturally occuring mutation Escherichia coli
2.2.1.6 W557L naturally occuring mutation Brassica napus
2.2.1.6 W563C naturally occuring mutation Gossypium hirsutum
2.2.1.6 W563S naturally occuring mutation Gossypium hirsutum
2.2.1.6 W574L naturally occuring mutation Arabidopsis thaliana
2.2.1.6 W574S naturally occuring mutation Arabidopsis thaliana
2.2.1.6 W586A naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 W586C naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 W586E naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 W586G naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 W586H naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 W586I naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 W586K naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 W586L naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 W586N naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 W586S naturally occuring mutation Saccharomyces cerevisiae
2.2.1.6 W586V naturally occuring mutation Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.2.1.6 chlorimuron ethyl a sulfonylurea herbicide, complex inhibition, binding structure, overview Arabidopsis thaliana
2.2.1.6 chlorimuron ethyl a sulfonylurea herbicide, complex inhibition, overview Brassica napus
2.2.1.6 chlorimuron ethyl a sulfonylurea herbicide, complex inhibition, overview Gossypium hirsutum
2.2.1.6 chlorimuron ethyl a sulfonylurea herbicide, complex inhibition, overview Helianthus annuus
2.2.1.6 chlorimuron ethyl a sulfonylurea herbicide, complex inhibition, overview Nicotiana tabacum
2.2.1.6 chlorsulfuron
-
 Arabidopsis thaliana
2.2.1.6 chlorsulfuron
-
 Brassica napus
2.2.1.6 chlorsulfuron
-
 Gossypium hirsutum
2.2.1.6 chlorsulfuron
-
 Helianthus annuus
2.2.1.6 chlorsulfuron
-
 Nicotiana tabacum
2.2.1.6 imazapyr an imidazolinone herbicide, complex inhibition, overview Arabidopsis thaliana
2.2.1.6 imazapyr an imidazolinone herbicide, complex inhibition, overview Brassica napus
2.2.1.6 imazapyr an imidazolinone herbicide, complex inhibition, overview Gossypium hirsutum
2.2.1.6 imazapyr an imidazolinone herbicide, complex inhibition, overview Helianthus annuus
2.2.1.6 imazapyr a imidazolinone herbicide, complex inhibition, overview Nicotiana tabacum
2.2.1.6 imazaquin an imidazolinone herbicide, complex inhibition, binding structure, overview Arabidopsis thaliana
2.2.1.6 imazaquin an imidazolinone herbicide, complex inhibition, overview Brassica napus
2.2.1.6 imazaquin an imidazolinone herbicide, complex inhibition, overview Gossypium hirsutum
2.2.1.6 imazaquin an imidazolinone herbicide, complex inhibition, overview Helianthus annuus
2.2.1.6 imazaquin a imidazolinone herbicide, complex inhibition, overview Nicotiana tabacum
2.2.1.6 leucine feedback inhibition Arabidopsis thaliana
2.2.1.6 leucine feedback inhibition Brassica napus
2.2.1.6 leucine feedback inhibition Escherichia coli
2.2.1.6 leucine feedback inhibition Gossypium hirsutum
2.2.1.6 leucine feedback inhibition Helianthus annuus
2.2.1.6 leucine feedback inhibition Nicotiana tabacum
2.2.1.6 leucine feedback inhibition Nitrosomonas europaea
2.2.1.6 leucine feedback inhibition Saccharomyces cerevisiae
2.2.1.6 leucine feedback inhibition Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 leucine feedback inhibition Thermotoga maritima
2.2.1.6 metsulfuron methyl a sulfonylurea herbicide, complex inhibition, overview Arabidopsis thaliana
2.2.1.6 metsulfuron methyl a sulfonylurea herbicide, complex inhibition, overview Brassica napus
2.2.1.6 metsulfuron methyl a sulfonylurea herbicide, complex inhibition, overview Gossypium hirsutum
2.2.1.6 metsulfuron methyl a sulfonylurea herbicide, complex inhibition, overview Helianthus annuus
2.2.1.6 metsulfuron methyl a sulfonylurea herbicide, complex inhibition, overview Nicotiana tabacum
2.2.1.6 additional information ligand binding structures, and inhibition mechanism, overview Arabidopsis thaliana
2.2.1.6 additional information ligand binding structures, and inhibition mechanism, overview Brassica napus
2.2.1.6 additional information ligand binding structures, and inhibition mechanism, overview Gossypium hirsutum
2.2.1.6 additional information ligand binding structures, and inhibition mechanism, overview Helianthus annuus
2.2.1.6 additional information ligand binding structures, and inhibition mechanism, overview Nicotiana tabacum
2.2.1.6 sulfometuron methyl
-
 Arabidopsis thaliana
2.2.1.6 sulfometuron methyl
-
 Brassica napus
2.2.1.6 sulfometuron methyl
-
 Gossypium hirsutum
2.2.1.6 sulfometuron methyl
-
 Helianthus annuus
2.2.1.6 sulfometuron methyl
-
 Nicotiana tabacum
2.2.1.6 tribenuron methyl
-
 Arabidopsis thaliana
2.2.1.6 tribenuron methyl
-
 Brassica napus
2.2.1.6 tribenuron methyl
-
 Gossypium hirsutum
2.2.1.6 tribenuron methyl
-
 Helianthus annuus
2.2.1.6 tribenuron methyl
-
 Nicotiana tabacum
2.2.1.6 valine feedback inhibition Arabidopsis thaliana
2.2.1.6 valine feedback inhibition Brassica napus
2.2.1.6 valine feedback inhibition Escherichia coli
2.2.1.6 valine feedback inhibition Gossypium hirsutum
2.2.1.6 valine feedback inhibition Helianthus annuus
2.2.1.6 valine feedback inhibition Nicotiana tabacum
2.2.1.6 valine feedback inhibition Nitrosomonas europaea
2.2.1.6 valine feedback inhibition, the inhibition by valine is uniquely in fungi reversed by MgATP Saccharomyces cerevisiae
2.2.1.6 valine feedback inhibition Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 valine feedback inhibition Thermotoga maritima

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.2.1.6 chloroplast an N-terminal peptide, which is subsequently removed, is required to direct the protein to chloroplasts in plants Nicotiana tabacum 9507
-
2.2.1.6 chloroplast an N-terminal peptide, which is subsequently removed, is required to direct the protein to chloroplasts in plants Arabidopsis thaliana 9507
-
2.2.1.6 chloroplast an N-terminal peptide, which is subsequently removed, is required to direct the protein to chloroplasts in plants Brassica napus 9507
-
2.2.1.6 chloroplast an N-terminal peptide, which is subsequently removed, is required to direct the protein to chloroplasts in plants Helianthus annuus 9507
-
2.2.1.6 chloroplast an N-terminal peptide, which is subsequently removed, is required to direct the protein to chloroplasts in plants Gossypium hirsutum 9507
-
2.2.1.6 mitochondrion an N-terminal peptide, which is subsequently removed, is required to direct the protein to mitochondria in fungi Saccharomyces cerevisiae 5739
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.2.1.6 Al3+ activates Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 Ba2+ activates Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 Ca2+ activates Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 Cd2+ activates Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 Co2+ activates Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 Mg2+ the enzyme requires a divalent metal ion Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 Mg2+ the enzyme requires a divalent metal ion Gossypium hirsutum
2.2.1.6 Mg2+ the enzyme requires a divalent metal ion Saccharomyces cerevisiae
2.2.1.6 Mg2+ the enzyme requires a divalent metal ion, involved in anchoring the cofactor thiamine diphosphate in the active site Arabidopsis thaliana
2.2.1.6 Mg2+ the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site Escherichia coli
2.2.1.6 Mg2+ the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site Nicotiana tabacum
2.2.1.6 Mg2+ the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site Brassica napus
2.2.1.6 Mg2+ the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site Nitrosomonas europaea
2.2.1.6 Mg2+ the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site Helianthus annuus
2.2.1.6 Mg2+ the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site Thermotoga maritima
2.2.1.6 Mn2+ the activity is about 133% for Mn2+ as compared to Mg2+ Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 additional information AHASII is active in the presence of Mn2+, Mg2+, Ca2+, Cd2+, Co2+, Zn2+, Cu2+, Al3+, Ba2+ or Ni2+, the activity is about 50% for Ni2+ and 133% for Mn2+ as compared to Mg2+ Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 Ni2+ the activity is about 50% for Ni2+ as compared to Mg2+ Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 Zn2+ activates Salmonella enterica subsp. enterica serovar Typhimurium

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.2.1.6 34000
-
 1 * 59000-66000, catalytic subunit + 1 * 34000, regulatory subunit Saccharomyces cerevisiae
2.2.1.6 50000
-
 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Nicotiana tabacum
2.2.1.6 50000
-
 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Arabidopsis thaliana
2.2.1.6 50000
-
 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Brassica napus
2.2.1.6 50000
-
 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Helianthus annuus
2.2.1.6 50000
-
 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Gossypium hirsutum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.2.1.6 additional information Salmonella enterica subsp. enterica serovar Typhimurium AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate ?
-
 ?
2.2.1.6 additional information Escherichia coli AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate ?
-
 ?
2.2.1.6 additional information Nicotiana tabacum AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate ?
-
 ?
2.2.1.6 additional information Arabidopsis thaliana AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate ?
-
 ?
2.2.1.6 additional information Brassica napus AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate ?
-
 ?
2.2.1.6 additional information Nitrosomonas europaea AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate ?
-
 ?
2.2.1.6 additional information Helianthus annuus AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate ?
-
 ?
2.2.1.6 additional information Thermotoga maritima AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate ?
-
 ?
2.2.1.6 additional information Gossypium hirsutum AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate ?
-
 ?
2.2.1.6 additional information Saccharomyces cerevisiae AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.6 Arabidopsis thaliana
-
 three isoenzymes AHASI-AHASIII
-
2.2.1.6 Brassica napus
-
-
-
2.2.1.6 Escherichia coli
-
-
-
2.2.1.6 Gossypium hirsutum Q42768
-
-
2.2.1.6 Helianthus annuus
-
-
-
2.2.1.6 Nicotiana tabacum
-
-
-
2.2.1.6 Nitrosomonas europaea
-
-
-
2.2.1.6 Saccharomyces cerevisiae P07342 catalytic aubunit
-
2.2.1.6 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
2.2.1.6 Thermotoga maritima
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.2.1.6 proteolytic modification the N-terminal peptide of the precursor protein is removed Nicotiana tabacum
2.2.1.6 proteolytic modification the N-terminal peptide of the precursor protein is removed Arabidopsis thaliana
2.2.1.6 proteolytic modification the N-terminal peptide of the precursor protein is removed Brassica napus
2.2.1.6 proteolytic modification the N-terminal peptide of the precursor protein is removed Helianthus annuus
2.2.1.6 proteolytic modification the N-terminal peptide of the precursor protein is removed Gossypium hirsutum
2.2.1.6 proteolytic modification the N-terminal peptide of the precursor protein is removed Saccharomyces cerevisiae

Reaction

EC Number Reaction Comment Organism Reaction ID
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 catalytic mechanism of the catalytic subunit involving the thiamine diphopshtae cofactor, overview Arabidopsis thaliana
a
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 catalytic mechanism of the catalytic subunit involving the thiamine diphosphate cofactor, overview Gossypium hirsutum
a
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 catalytic mechanism of the catalytic subunit involving the thiamine diphosphtae cofactor, overview Nicotiana tabacum
a
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 catalytic mechanism of the catalytic subunit involving the thiamine diphosphtae cofactor, overview Brassica napus
a
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 catalytic mechanism of the catalytic subunit involving the thiamine diphosphtae cofactor, overview Helianthus annuus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.6 additional information AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate Salmonella enterica subsp. enterica serovar Typhimurium ?
-
 ?
2.2.1.6 additional information AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate Escherichia coli ?
-
 ?
2.2.1.6 additional information AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate Nicotiana tabacum ?
-
 ?
2.2.1.6 additional information AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate Arabidopsis thaliana ?
-
 ?
2.2.1.6 additional information AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate Brassica napus ?
-
 ?
2.2.1.6 additional information AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate Nitrosomonas europaea ?
-
 ?
2.2.1.6 additional information AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate Helianthus annuus ?
-
 ?
2.2.1.6 additional information AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate Thermotoga maritima ?
-
 ?
2.2.1.6 additional information AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate Gossypium hirsutum ?
-
 ?
2.2.1.6 additional information AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.2.1.6 dimer 1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 dimer 1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit Escherichia coli
2.2.1.6 dimer 1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit Nitrosomonas europaea
2.2.1.6 dimer 1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit Thermotoga maritima
2.2.1.6 dimer 1 * 59000-66000, catalytic subunit + 1 * 34000, regulatory subunit Saccharomyces cerevisiae
2.2.1.6 dimer 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Nicotiana tabacum
2.2.1.6 dimer 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Arabidopsis thaliana
2.2.1.6 dimer 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Brassica napus
2.2.1.6 dimer 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Helianthus annuus
2.2.1.6 dimer 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Gossypium hirsutum
2.2.1.6 More the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 More the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview Escherichia coli
2.2.1.6 More the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview Nicotiana tabacum
2.2.1.6 More the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview Arabidopsis thaliana
2.2.1.6 More the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview Brassica napus
2.2.1.6 More the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview Nitrosomonas europaea
2.2.1.6 More the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview Helianthus annuus
2.2.1.6 More the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview Thermotoga maritima
2.2.1.6 More the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview Gossypium hirsutum
2.2.1.6 More the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
2.2.1.6 acetohydroxyacid synthase
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 acetohydroxyacid synthase
-
 Escherichia coli
2.2.1.6 acetohydroxyacid synthase
-
 Nicotiana tabacum
2.2.1.6 acetohydroxyacid synthase
-
 Arabidopsis thaliana
2.2.1.6 acetohydroxyacid synthase
-
 Brassica napus
2.2.1.6 acetohydroxyacid synthase
-
 Nitrosomonas europaea
2.2.1.6 acetohydroxyacid synthase
-
 Helianthus annuus
2.2.1.6 acetohydroxyacid synthase
-
 Thermotoga maritima
2.2.1.6 acetohydroxyacid synthase
-
 Gossypium hirsutum
2.2.1.6 acetohydroxyacid synthase
-
 Saccharomyces cerevisiae
2.2.1.6 AHAS
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 AHAS
-
 Escherichia coli
2.2.1.6 AHAS
-
 Nicotiana tabacum
2.2.1.6 AHAS
-
 Arabidopsis thaliana
2.2.1.6 AHAS
-
 Brassica napus
2.2.1.6 AHAS
-
 Nitrosomonas europaea
2.2.1.6 AHAS
-
 Helianthus annuus
2.2.1.6 AHAS
-
 Thermotoga maritima
2.2.1.6 AHAS
-
 Gossypium hirsutum
2.2.1.6 AHAS
-
 Saccharomyces cerevisiae
2.2.1.6 More the enzyme belongs to the ThDP-dependent family of enzymes Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 More the enzyme belongs to the ThDP-dependent family of enzymes Escherichia coli
2.2.1.6 More the enzyme belongs to the ThDP-dependent family of enzymes Nicotiana tabacum
2.2.1.6 More the enzyme belongs to the ThDP-dependent family of enzymes Arabidopsis thaliana
2.2.1.6 More the enzyme belongs to the ThDP-dependent family of enzymes Brassica napus
2.2.1.6 More the enzyme belongs to the ThDP-dependent family of enzymes Nitrosomonas europaea
2.2.1.6 More the enzyme belongs to the ThDP-dependent family of enzymes Helianthus annuus
2.2.1.6 More the enzyme belongs to the ThDP-dependent family of enzymes Thermotoga maritima
2.2.1.6 More the enzyme belongs to the ThDP-dependent family of enzymes Gossypium hirsutum
2.2.1.6 More the enzyme belongs to the ThDP-dependent family of enzymes Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.6 FAD required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 FAD required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes Escherichia coli
2.2.1.6 FAD required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes Nitrosomonas europaea
2.2.1.6 FAD required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes Thermotoga maritima
2.2.1.6 FAD required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes Saccharomyces cerevisiae
2.2.1.6 FAD required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview Nicotiana tabacum
2.2.1.6 FAD required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview Arabidopsis thaliana
2.2.1.6 FAD required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview Brassica napus
2.2.1.6 FAD required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview Helianthus annuus
2.2.1.6 FAD required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview Gossypium hirsutum
2.2.1.6 thiamine diphosphate required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+ Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 thiamine diphosphate required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+ Escherichia coli
2.2.1.6 thiamine diphosphate required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+ Nicotiana tabacum
2.2.1.6 thiamine diphosphate required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+ Arabidopsis thaliana
2.2.1.6 thiamine diphosphate required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+ Brassica napus
2.2.1.6 thiamine diphosphate required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+ Nitrosomonas europaea
2.2.1.6 thiamine diphosphate required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+ Helianthus annuus
2.2.1.6 thiamine diphosphate required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+ Thermotoga maritima
2.2.1.6 thiamine diphosphate required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+ Gossypium hirsutum
2.2.1.6 thiamine diphosphate required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+ Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.2.1.6 additional information
-
 additional information inhibition kinetics Arabidopsis thaliana
2.2.1.6 additional information
-
 leucine/valine an equimolar mixture of leucine and valine Arabidopsis thaliana
2.2.1.6 0.000011
-
 chlorimuron ethyl about Arabidopsis thaliana
2.2.1.6 0.003
-
 imazaquin about Arabidopsis thaliana
2.2.1.6 0.231
-
 valine
-
 Arabidopsis thaliana
2.2.1.6 0.336
-
 leucine
-
 Arabidopsis thaliana