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Literature summary for 2.2.1.6 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

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Inhibitors

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

Localization

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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

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

Posttranslational Modification

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

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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

Subunits Comment Organism
dimer 1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit Salmonella enterica subsp. enterica serovar Typhimurium
dimer 1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit Escherichia coli
dimer 1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit Nitrosomonas europaea
dimer 1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit Thermotoga maritima
dimer 1 * 59000-66000, catalytic subunit + 1 * 34000, regulatory subunit Saccharomyces cerevisiae
dimer 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Nicotiana tabacum
dimer 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Arabidopsis thaliana
dimer 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Brassica napus
dimer 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Helianthus annuus
dimer 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit Gossypium hirsutum
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
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
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
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
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
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
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
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
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
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

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

Cofactor

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

Ki Value [mM]

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