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 |
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 |
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 |
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 |
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 | - |
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 |
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 |
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 | ? | - |
? |
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 | - |
- |
- |
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 |
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 | |
2.2.1.6 | 2 pyruvate = 2-acetolactate + CO2 | catalytic mechanism of the catalytic subunit involving the thiamine diphosphate cofactor, overview | Gossypium hirsutum | |
2.2.1.6 | 2 pyruvate = 2-acetolactate + CO2 | catalytic mechanism of the catalytic subunit involving the thiamine diphosphtae cofactor, overview | Nicotiana tabacum | |
2.2.1.6 | 2 pyruvate = 2-acetolactate + CO2 | catalytic mechanism of the catalytic subunit involving the thiamine diphosphtae cofactor, overview | Brassica napus | |
2.2.1.6 | 2 pyruvate = 2-acetolactate + CO2 | catalytic mechanism of the catalytic subunit involving the thiamine diphosphtae cofactor, overview | Helianthus annuus |
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 | ? | - |
? |
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 |
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 |
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 |
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 |