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Literature summary extracted from

  • Gokhale, K.; Tilak, B.
    Mechanisms of bacterial acetohydroxyacid synthase (AHAS) and specific inhibitors of Mycobacterium tuberculosis AHAS as potential drug candidates against tuberculosis (2015), Curr. Drug Targets, 16, 689-699.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.2.1.6 drug development the enzyme is a target for drug development Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 drug development the enzyme is a target for drug development Saccharomyces cerevisiae
2.2.1.6 drug development the enzyme is a target for drug development Pseudomonas aeruginosa
2.2.1.6 drug development the enzyme is a target for drug development Escherichia coli
2.2.1.6 drug development the enzyme is a target for drug development in tuberculosis treatment Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.2.1.6 genes ilvB and ilvN Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.2.1.6 2-chloro-3-oxocyclohex-1-en-1-yl 3-(trifluoromethyl)benzoate
-
 Mycobacterium tuberculosis
2.2.1.6 2-chloro-3-oxocyclohex-1-en-1-yl-3-(trifluoromethyl)benzoate
-
 Escherichia coli
2.2.1.6 2-chloro-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoate
-
 Mycobacterium tuberculosis
2.2.1.6 2-chloro-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoic acid no inhibition by bensulfuron methyl. Feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern Mycobacterium tuberculosis
2.2.1.6 2-chloro-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoic acid ester
-
 Escherichia coli
2.2.1.6 2-chloro-6-(methoxycarbonyl)-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoate
-
 Mycobacterium tuberculosis
2.2.1.6 2-chloro-6-methoxycarbonyl-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoate
-
 Escherichia coli
2.2.1.6 2-chloro-N-(4-chloro-3-[[(4-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]phenyl)acetamide
-
 Mycobacterium tuberculosis
2.2.1.6 2-chloro-N-(4-chloro-3-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]phenyl)acetamide
-
 Mycobacterium tuberculosis
2.2.1.6 2-nitro-5-(phenylsulfonyl)phenyl 4-chlorobenzoate
-
 Mycobacterium tuberculosis
2.2.1.6 2-phenyl-3-[[3-(trifluoromethyl)benzoyl]oxy]quinazolin-4(3H)-one
-
 Mycobacterium tuberculosis
2.2.1.6 2-phenyl-3-{[3-(trifluoromethyl)benzoyl]oxy}quinazolin-4-one
-
 Escherichia coli
2.2.1.6 3-[(3-bromobenzoyl)oxy]-2-phenylquinazolin-4(3H)-one
-
 Mycobacterium tuberculosis
2.2.1.6 3-[(3-bromobenzoyl)oxy]-2-phenylquinazolin-4-one
-
 Escherichia coli
2.2.1.6 3-[(4-nitrobenzoyl)oxy]quinazolin-4(3H)-one
-
 Mycobacterium tuberculosis
2.2.1.6 3-[(4-nitrobenzoyl)oxy]quinazolin-4-one
-
 Escherichia coli
2.2.1.6 bensulfuron methyl
-
 Mycobacterium tuberculosis
2.2.1.6 chlorimuron ethyl
-
 Mycobacterium tuberculosis
2.2.1.6 ethyl 4-chloro-2-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
 Mycobacterium tuberculosis
2.2.1.6 imazapyr
-
 Escherichia coli
2.2.1.6 imazapyr
-
 Mycobacterium tuberculosis
2.2.1.6 imazaquin
-
 Escherichia coli
2.2.1.6 imazaquin
-
 Mycobacterium tuberculosis
2.2.1.6 imazethapyr
-
 Escherichia coli
2.2.1.6 imazethapyr
-
 Mycobacterium tuberculosis
2.2.1.6 isoleucine feedback inhibition; feedback inhibition; feedback inhibition Escherichia coli
2.2.1.6 isoleucine feedback inhibition Mycobacterium tuberculosis
2.2.1.6 isoleucine feedback inhibition Pseudomonas aeruginosa
2.2.1.6 isoleucine feedback inhibition Saccharomyces cerevisiae
2.2.1.6 isoleucine feedback inhibition Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 KHG20612 strong inhibition Mycobacterium tuberculosis
2.2.1.6 leucine feedback inhibition; feedback inhibition; feedback inhibition Escherichia coli
2.2.1.6 leucine feedback inhibition Mycobacterium tuberculosis
2.2.1.6 leucine feedback inhibition Pseudomonas aeruginosa
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 methyl-2-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoylsulfamoyl]benzoate
-
 Mycobacterium tuberculosis
2.2.1.6 metsulfuron methyl
-
 Mycobacterium tuberculosis
2.2.1.6 additional information feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Certain imidazolinones show significant activity against the bacterial enzyme with Ki values of below 0.11 mM. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern; feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Certain imidazolinones show significant activity against the bacterial enzyme with Ki values of below 0.11 mM. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern; feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Certain imidazolinones show significant activity against the bacterial enzyme with Ki values of below 0.11 mM. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern Escherichia coli
2.2.1.6 additional information not inhibited by bensulfuron methyl Mycobacterium tuberculosis
2.2.1.6 additional information feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme Pseudomonas aeruginosa
2.2.1.6 additional information feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme Saccharomyces cerevisiae
2.2.1.6 additional information feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 N-phenyl-3-(phenyldisulfanyl)-1H-1,2,4-triazole-1-carboxamide strong inhibition Mycobacterium tuberculosis
2.2.1.6 propan-2-yl 4-bromo-3-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
 Mycobacterium tuberculosis
2.2.1.6 sulfometuron methyl
-
 Mycobacterium tuberculosis
2.2.1.6 valine feedback inhibition; feedback inhibition; feedback inhibition Escherichia coli
2.2.1.6 valine feedback inhibition Mycobacterium tuberculosis
2.2.1.6 valine feedback inhibition Pseudomonas aeruginosa
2.2.1.6 valine feedback inhibition Saccharomyces cerevisiae
2.2.1.6 valine feedback inhibition Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.2.1.6 Ca2+ activates Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 Ca2+ activates Saccharomyces cerevisiae
2.2.1.6 Ca2+ activates Pseudomonas aeruginosa
2.2.1.6 Ca2+ activates Escherichia coli
2.2.1.6 Ca2+ activates Mycobacterium tuberculosis
2.2.1.6 Cd2+ activates Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 Cd2+ activates Saccharomyces cerevisiae
2.2.1.6 Cd2+ activates Pseudomonas aeruginosa
2.2.1.6 Cd2+ activates Escherichia coli
2.2.1.6 Cd2+ activates Mycobacterium tuberculosis
2.2.1.6 Mg2+ required Mycobacterium tuberculosis
2.2.1.6 Mg2+ a bivalent metal cation is required Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 Mg2+ a bivalent metal cation is required Saccharomyces cerevisiae
2.2.1.6 Mg2+ a bivalent metal cation is required Pseudomonas aeruginosa
2.2.1.6 Mg2+ a bivalent metal cation is required Escherichia coli
2.2.1.6 Mg2+ a bivalent metal cation is required Mycobacterium tuberculosis
2.2.1.6 Mn2+ activates Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 Mn2+ activates Saccharomyces cerevisiae
2.2.1.6 Mn2+ activates Pseudomonas aeruginosa
2.2.1.6 Mn2+ activates Escherichia coli
2.2.1.6 Mn2+ activates Mycobacterium tuberculosis
2.2.1.6 additional information enzyme AHAS is not specific as far as metal ions are concerned. It is active in presence of any metal ion like Mn2+, Mg2+, Ca2+, Cd2+ Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 additional information enzyme AHAS is not specific as far as metal ions are concerned. It is active in presence of any metal ion like Mn2+, Mg2+, Ca2+, Cd2+ Saccharomyces cerevisiae
2.2.1.6 additional information enzyme AHAS is not specific as far as metal ions are concerned. It is active in presence of any metal ion like Mn2+, Mg2+, Ca2+, Cd2+ Pseudomonas aeruginosa
2.2.1.6 additional information enzyme AHAS is not specific as far as metal ions are concerned. It is active in presence of any metal ion like Mn2+, Mg2+, Ca2+, Cd2+ Mycobacterium tuberculosis
2.2.1.6 additional information enzyme AHAS is not specific as far as metal ions are concerned. It is active in presence of any metal ion like Mn2+, Mg2+, Ca2+, Cd2+. Modeling of the activity of the metal ions in the catalytic mechanism of isozyme AHAS II Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.2.1.6 2 pyruvate Mycobacterium tuberculosis
-
 2-acetolactate + CO2
-
 ?
2.2.1.6 2 pyruvate Salmonella enterica subsp. enterica serovar Typhimurium irreversible decarboxylation of pyruvate 2-acetolactate + CO2
-
 ir
2.2.1.6 2 pyruvate Saccharomyces cerevisiae irreversible decarboxylation of pyruvate 2-acetolactate + CO2
-
 ir
2.2.1.6 2 pyruvate Pseudomonas aeruginosa irreversible decarboxylation of pyruvate 2-acetolactate + CO2
-
 ir
2.2.1.6 2 pyruvate Escherichia coli irreversible decarboxylation of pyruvate 2-acetolactate + CO2
-
 ir
2.2.1.6 2 pyruvate Mycobacterium tuberculosis irreversible decarboxylation of pyruvate 2-acetolactate + CO2
-
 ir
2.2.1.6 2 pyruvate Mycobacterium tuberculosis H37Rv irreversible decarboxylation of pyruvate 2-acetolactate + CO2
-
 ir
2.2.1.6 2-oxobutyrate Escherichia coli
-
 2-ethyl-2-hydroxy-3-oxopentanoate + CO2
-
 ir
2.2.1.6 2-oxobutyrate + pyruvate Mycobacterium tuberculosis
-
 2-aceto-2-hydroxybutyrate + CO2
-
 ?
2.2.1.6 pyruvate + 2-oxobutyrate Salmonella enterica subsp. enterica serovar Typhimurium irreversible decarboxylation of pyruvate 2-aceto-2-hydroxybutyrate + CO2
-
 ir
2.2.1.6 pyruvate + 2-oxobutyrate Saccharomyces cerevisiae irreversible decarboxylation of pyruvate 2-aceto-2-hydroxybutyrate + CO2
-
 ir
2.2.1.6 pyruvate + 2-oxobutyrate Pseudomonas aeruginosa irreversible decarboxylation of pyruvate 2-aceto-2-hydroxybutyrate + CO2
-
 ir
2.2.1.6 pyruvate + 2-oxobutyrate Escherichia coli irreversible decarboxylation of pyruvate 2-aceto-2-hydroxybutyrate + CO2
-
 ir
2.2.1.6 pyruvate + 2-oxobutyrate Mycobacterium tuberculosis irreversible decarboxylation of pyruvate 2-aceto-2-hydroxybutyrate + CO2
-
 ir
2.2.1.6 pyruvate + 2-oxobutyrate Mycobacterium tuberculosis H37Rv irreversible decarboxylation of pyruvate 2-aceto-2-hydroxybutyrate + CO2
-
 ir

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.6 Escherichia coli P00892 and P0ADG1 large and small subunit of isozyme 2 encoded by genes ilvG and ilvM; isozyme AHAS I, Escherichia coli wild-type does not contain AHAS II as result of a frameshift mutation, leading to a premature stop codon in the centre of the catalytic subunit of gene ilvG, which results into a cryptic form of AHAS II found in strain K-12, normal expression can be restored by gene ilvO mutation
-
2.2.1.6 Escherichia coli P00893 and P00894 large and small subunit of isozyme 3 encoded by genes ilvI and ilvH; isozyme AHAS I, Escherichia coli wild-type does not contain AHAS II as result of a frameshift mutation, leading to a premature stop codon in the centre of the catalytic subunit of gene ilvG, which results into a cryptic form of AHAS II found in strain K-12, normal expression can be restored by gene ilvO mutation
-
2.2.1.6 Escherichia coli P08142 and P0ADF8 large and small subunit of isozyme 1 encoded by genes ilvB and ilvN; isozyme AHAS I, Escherichia coli wild-type does not contain AHAS II as result of a frameshift mutation, leading to a premature stop codon in the centre of the catalytic subunit of gene ilvG, which results into a cryptic form of AHAS II found in strain K-12, normal expression can be restored by gene ilvO mutation
-
2.2.1.6 Mycobacterium tuberculosis
-
-
-
2.2.1.6 Mycobacterium tuberculosis P9WG41 and P9WKJ3 large and small subunit encoded by genes ilvB and ilvN; two subunits encoded by genes ilvB and ilvN
-
2.2.1.6 Mycobacterium tuberculosis H37Rv P9WG41 and P9WKJ3 large and small subunit encoded by genes ilvB and ilvN; two subunits encoded by genes ilvB and ilvN
-
2.2.1.6 Pseudomonas aeruginosa
-
-
-
2.2.1.6 Saccharomyces cerevisiae
-
-
-
2.2.1.6 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 catalytic mechanism, detailed overview Salmonella enterica subsp. enterica serovar Typhimurium
a
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 catalytic mechanism, detailed overview Saccharomyces cerevisiae
a
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 catalytic mechanism, detailed overview Pseudomonas aeruginosa
a
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 catalytic mechanism, detailed overview Escherichia coli
a
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 catalytic mechanism, detailed overview. An intermediate step involves the attack of the ThDP carbanion on the pyruvate to form lactyl ThDP. The second substrate (the acceptor) carbonyl is attacked by hydroxyethylthiamine diphosphate enamine to give the product-ThDP adduct, which then dissociates to form ThDP and the free product. Direct competition that exists between the acceptor substrates for the bound HE-ThDP determines the ratio of formation of the products. The product ratio depends only on the relative amounts of the acceptor substrates in wild-type enzymes and the kcat is virtually independent of the amount of the acceptors. The rate determining step of the process is the one just before product determining carboligation step from which kcat is determined, the other steps of the process have little effect on the overall rate of reaction Mycobacterium tuberculosis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.6 2 pyruvate
-
 Mycobacterium tuberculosis 2-acetolactate + CO2
-
 ?
2.2.1.6 2 pyruvate irreversible decarboxylation of pyruvate Salmonella enterica subsp. enterica serovar Typhimurium 2-acetolactate + CO2
-
 ir
2.2.1.6 2 pyruvate irreversible decarboxylation of pyruvate Saccharomyces cerevisiae 2-acetolactate + CO2
-
 ir
2.2.1.6 2 pyruvate irreversible decarboxylation of pyruvate Pseudomonas aeruginosa 2-acetolactate + CO2
-
 ir
2.2.1.6 2 pyruvate irreversible decarboxylation of pyruvate Escherichia coli 2-acetolactate + CO2
-
 ir
2.2.1.6 2 pyruvate irreversible decarboxylation of pyruvate Mycobacterium tuberculosis 2-acetolactate + CO2
-
 ir
2.2.1.6 2 pyruvate irreversible decarboxylation of pyruvate Mycobacterium tuberculosis H37Rv 2-acetolactate + CO2
-
 ir
2.2.1.6 2-oxobutyrate
-
 Escherichia coli 2-ethyl-2-hydroxy-3-oxopentanoate + CO2
-
 ir
2.2.1.6 2-oxobutyrate + pyruvate
-
 Mycobacterium tuberculosis 2-aceto-2-hydroxybutyrate + CO2
-
 ?
2.2.1.6 additional information the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of puruvate and 2-ketobutyrate, respectively Salmonella enterica subsp. enterica serovar Typhimurium ?
-
 ?
2.2.1.6 additional information the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of puruvate and 2-ketobutyrate, respectively Saccharomyces cerevisiae ?
-
 ?
2.2.1.6 additional information the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of puruvate and 2-ketobutyrate, respectively Pseudomonas aeruginosa ?
-
 ?
2.2.1.6 additional information the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of puruvate and 2-ketobutyrate, respectively Mycobacterium tuberculosis ?
-
 ?
2.2.1.6 additional information the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of pyruvate and 2-oxobutyrate, respectively. Substrate specificities of isozymes: isozymes AHAS II and AHAS III prefer 2-oxobutyrate as the second substrate whereas such selectivity is not observed in case of isozyme AHAS I. Isozymes AHAS I and AHAS II are capable of self condensing 2-oxobutyrate to form 2-ethyl-2-hydroxy-3-oxopentanoate Escherichia coli ?
-
 ?
2.2.1.6 additional information the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of puruvate and 2-ketobutyrate, respectively Mycobacterium tuberculosis H37Rv ?
-
 ?
2.2.1.6 pyruvate + 2-oxobutyrate irreversible decarboxylation of pyruvate Salmonella enterica subsp. enterica serovar Typhimurium 2-aceto-2-hydroxybutyrate + CO2
-
 ir
2.2.1.6 pyruvate + 2-oxobutyrate irreversible decarboxylation of pyruvate Saccharomyces cerevisiae 2-aceto-2-hydroxybutyrate + CO2
-
 ir
2.2.1.6 pyruvate + 2-oxobutyrate irreversible decarboxylation of pyruvate Pseudomonas aeruginosa 2-aceto-2-hydroxybutyrate + CO2
-
 ir
2.2.1.6 pyruvate + 2-oxobutyrate irreversible decarboxylation of pyruvate Escherichia coli 2-aceto-2-hydroxybutyrate + CO2
-
 ir
2.2.1.6 pyruvate + 2-oxobutyrate irreversible decarboxylation of pyruvate Mycobacterium tuberculosis 2-aceto-2-hydroxybutyrate + CO2
-
 ir
2.2.1.6 pyruvate + 2-oxobutyrate irreversible decarboxylation of pyruvate Mycobacterium tuberculosis H37Rv 2-aceto-2-hydroxybutyrate + CO2
-
 ir

Subunits

EC Number Subunits Comment Organism
2.2.1.6 tetramer the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 tetramer the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer Pseudomonas aeruginosa
2.2.1.6 tetramer the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer Escherichia coli
2.2.1.6 tetramer the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer The catalytic subunit has a molecular weight of 60-70 kD, the regulator of 10-45 kD Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.2.1.6 acetohydroxyacid synthase
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 acetohydroxyacid synthase
-
 Saccharomyces cerevisiae
2.2.1.6 acetohydroxyacid synthase
-
 Pseudomonas aeruginosa
2.2.1.6 acetohydroxyacid synthase
-
 Mycobacterium tuberculosis
2.2.1.6 acetohydroxyacid synthase
-
 Escherichia coli
2.2.1.6 AHAS
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 AHAS
-
 Saccharomyces cerevisiae
2.2.1.6 AHAS
-
 Pseudomonas aeruginosa
2.2.1.6 AHAS
-
 Mycobacterium tuberculosis
2.2.1.6 AHAS
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.6 FAD
-
 Mycobacterium tuberculosis
2.2.1.6 FAD the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 FAD the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct Pseudomonas aeruginosa
2.2.1.6 FAD the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct Mycobacterium tuberculosis
2.2.1.6 FAD the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct, reaction mechanism molecular modeling Saccharomyces cerevisiae
2.2.1.6 FAD the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct, reaction mechanism molecular modeling Escherichia coli
2.2.1.6 thiamine diphosphate
-
 Mycobacterium tuberculosis
2.2.1.6 thiamine diphosphate dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 thiamine diphosphate dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP Saccharomyces cerevisiae
2.2.1.6 thiamine diphosphate dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP Pseudomonas aeruginosa
2.2.1.6 thiamine diphosphate dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP Escherichia coli
2.2.1.6 thiamine diphosphate dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP Mycobacterium tuberculosis

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.2.1.6 0.00177
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis KHG20612
2.2.1.6 0.00177
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis N-phenyl-3-(phenyldisulfanyl)-1H-1,2,4-triazole-1-carboxamide
2.2.1.6 0.00178
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis 2-chloro-6-(methoxycarbonyl)-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoate
2.2.1.6 0.00185
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis 3-[(3-bromobenzoyl)oxy]-2-phenylquinazolin-4(3H)-one
2.2.1.6 0.00202
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis 2-phenyl-3-[[3-(trifluoromethyl)benzoyl]oxy]quinazolin-4(3H)-one
2.2.1.6 0.00267
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis 2-chloro-3-oxocyclohex-1-en-1-yl 3-(trifluoromethyl)benzoate
2.2.1.6 0.00479
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis sulfometuron methyl
2.2.1.6 0.00596
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis metsulfuron methyl
2.2.1.6 0.00596
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis methyl-2-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoylsulfamoyl]benzoate
2.2.1.6 0.00897
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis chlorimuron ethyl
2.2.1.6 0.0141
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis 2-chloro-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoate
2.2.1.6 0.01413
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis 3-[(4-nitrobenzoyl)oxy]quinazolin-4(3H)-one

Expression

EC Number Organism Comment Expression
2.2.1.6 Escherichia coli leucine controls isozyme AHAS III production in Escherichia coli additional information

General Information

EC Number General Information Comment Organism
2.2.1.6 evolution three types of isozymes, AHAS I, II, III, are found in Enterobacteria encoded by ilvBN, ilvGMEDA, ilvIH operons, respectively. Bacterial AHAS consists of a regulatory and a catalytic subunit Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 evolution three types of isozymes, AHAS I, II, III, are found in Enterobacteria encoded by ilvBN, ilvGMEDA, ilvIH operons, respectively. Bacterial AHAS consists of a regulatory and a catalytic subunit Pseudomonas aeruginosa
2.2.1.6 evolution three types of isozymes, AHAS I, II, III, are found in Enterobacteria encoded by ilvBN, ilvGMEDA, ilvIH operons, respectively. Bacterial AHAS consists of a regulatory and a catalytic subunit Escherichia coli
2.2.1.6 evolution three types of isozymes, AHAS I, II, III, are found in Enterobacteria encoded by ilvBN, ilvGMEDA, ilvIH operons, respectively. Bacterial AHAS consists of a regulatory and a catalytic subunit Mycobacterium tuberculosis
2.2.1.6 malfunction enzyme inhibition abolishes biosynthesis of brachend chain amino acids and leads to bacteriostasis Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 malfunction enzyme inhibition abolishes biosynthesis of brachend chain amino acids and leads to bacteriostasis Pseudomonas aeruginosa
2.2.1.6 malfunction enzyme inhibition abolishes biosynthesis of brachend chain amino acids and leads to bacteriostasis Escherichia coli
2.2.1.6 malfunction enzyme inhibition abolishes biosynthesis of brachend chain amino acids and leads to bacteriostasis Mycobacterium tuberculosis
2.2.1.6 metabolism the bacterial anabolic enzyme form catalyzes the first step in biosynthesis of branched amino acids isoleucine, leucine and valine. It catalyzes the first and the most crucial step which is either the self condensation of pyruvate to form 2-acetolactate or the condensation between lactate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate. 2-acetolactate and 2-aceto-2-hydroxybutyrate serve as the precursors for the synthesis of leucine and valine while latter serves as the precursor for the synthesis of isoleucine. In some bacteria, the enzyme is responsible for the formation of butanediol and other products of fermentation Mycobacterium tuberculosis
2.2.1.6 metabolism the bacterial anabolic enzyme form catalyzes the first step in biosynthesis of branched amino acids isoleucine, leucine and valine. It catalyzes the first and the most crucial step which is either the self condensation of pyruvate to form 2-acetolactate or the condensation between lactate and 2-oxobutyrate to form 2-aceto-2-hydroxybutyrate. 2-acetolactate and 2-aceto-2-hydroxybutyrate serve as the precursors for the synthesis of leucine and valine while latter serves as the precursor for the synthesis of isoleucine. In some bacteria, the enzyme is responsible for the formation of butanediol and other products of fermentation Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 metabolism the bacterial anabolic enzyme form catalyzes the first step in biosynthesis of branched amino acids isoleucine, leucine and valine. It catalyzes the first and the most crucial step which is either the self condensation of pyruvate to form 2-acetolactate or the condensation between lactate and 2-oxobutyrate to form 2-aceto-2-hydroxybutyrate. 2-acetolactate and 2-aceto-2-hydroxybutyrate serve as the precursors for the synthesis of leucine and valine while latter serves as the precursor for the synthesis of isoleucine. In some bacteria, the enzyme is responsible for the formation of butanediol and other products of fermentation Pseudomonas aeruginosa
2.2.1.6 metabolism the bacterial anabolic enzyme form catalyzes the first step in biosynthesis of branched amino acids isoleucine, leucine and valine. It catalyzes the first and the most crucial step which is either the self condensation of pyruvate to form 2-acetolactate or the condensation between lactate and 2-oxobutyrate to form 2-aceto-2-hydroxybutyrate. 2-acetolactate and 2-aceto-2-hydroxybutyrate serve as the precursors for the synthesis of leucine and valine while latter serves as the precursor for the synthesis of isoleucine. In some bacteria, the enzyme is responsible for the formation of butanediol and other products of fermentation Escherichia coli
2.2.1.6 metabolism the enzyme catalyzes the first step in biosynthesis of branched amino acids isoleucine, leucine and valine Saccharomyces cerevisiae
2.2.1.6 additional information there exist two types of the enzyme, catabolic and anabolic AHAS. The anabolic form of the enzyme consists of two subunits out of which one is catalytic while the other is regulatory in nature. The regulatory subunit acts via feedback inhibition Salmonella enterica subsp. enterica serovar Typhimurium
2.2.1.6 additional information there exist two types of the enzyme, catabolic and anabolic AHAS. The anabolic form of the enzyme consists of two subunits out of which one is catalytic while the other is regulatory in nature. The regulatory subunit acts via feedback inhibition Pseudomonas aeruginosa
2.2.1.6 additional information there exist two types of the enzyme, catabolic and anabolic AHAS. The anabolic form of the enzyme consists of two subunits out of which one is catalytic while the other is regulatory in nature. The regulatory subunit acts via feedback inhibition Escherichia coli
2.2.1.6 additional information there exist two types of the enzyme, catabolic and anabolic AHAS. The anabolic form of the enzyme consists of two subunits out of which one is catalytic while the other is regulatory in nature. The regulatory subunit acts via feedback inhibition Mycobacterium tuberculosis