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 (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 | 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 | 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 | 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 | 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 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 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 |