Literature summary for 2.2.1.6 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.

Application

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

Cloned(Commentary)

Cloned (Comment)	Organism
genes ilvB and ilvN	Mycobacterium tuberculosis

Inhibitors

Inhibitors	Comment	Organism
2-chloro-3-oxocyclohex-1-en-1-yl 3-(trifluoromethyl)benzoate	-	Mycobacterium tuberculosis
2-chloro-3-oxocyclohex-1-en-1-yl-3-(trifluoromethyl)benzoate	-	Escherichia coli
2-chloro-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoate	-	Mycobacterium tuberculosis
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-chloro-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoic acid ester	-	Escherichia coli
2-chloro-6-(methoxycarbonyl)-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoate	-	Mycobacterium tuberculosis
2-chloro-6-methoxycarbonyl-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoate	-	Escherichia coli
2-chloro-N-(4-chloro-3-[[(4-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]phenyl)acetamide	-	Mycobacterium tuberculosis
2-chloro-N-(4-chloro-3-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]phenyl)acetamide	-	Mycobacterium tuberculosis
2-nitro-5-(phenylsulfonyl)phenyl 4-chlorobenzoate	-	Mycobacterium tuberculosis
2-phenyl-3-[[3-(trifluoromethyl)benzoyl]oxy]quinazolin-4(3H)-one	-	Mycobacterium tuberculosis
2-phenyl-3-{[3-(trifluoromethyl)benzoyl]oxy}quinazolin-4-one	-	Escherichia coli
3-[(3-bromobenzoyl)oxy]-2-phenylquinazolin-4(3H)-one	-	Mycobacterium tuberculosis
3-[(3-bromobenzoyl)oxy]-2-phenylquinazolin-4-one	-	Escherichia coli
3-[(4-nitrobenzoyl)oxy]quinazolin-4(3H)-one	-	Mycobacterium tuberculosis
3-[(4-nitrobenzoyl)oxy]quinazolin-4-one	-	Escherichia coli
bensulfuron methyl	-	Mycobacterium tuberculosis
chlorimuron ethyl	-	Mycobacterium tuberculosis
ethyl 4-chloro-2-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate	-	Mycobacterium tuberculosis
imazapyr	-	Escherichia coli
imazapyr	-	Mycobacterium tuberculosis
imazaquin	-	Escherichia coli
imazaquin	-	Mycobacterium tuberculosis
imazethapyr	-	Escherichia coli
imazethapyr	-	Mycobacterium tuberculosis
isoleucine	feedback inhibition; feedback inhibition; feedback inhibition	Escherichia coli
isoleucine	feedback inhibition	Mycobacterium tuberculosis
isoleucine	feedback inhibition	Pseudomonas aeruginosa
isoleucine	feedback inhibition	Saccharomyces cerevisiae
isoleucine	feedback inhibition	Salmonella enterica subsp. enterica serovar Typhimurium
KHG20612	strong inhibition	Mycobacterium tuberculosis
leucine	feedback inhibition; feedback inhibition; feedback inhibition	Escherichia coli
leucine	feedback inhibition	Mycobacterium tuberculosis
leucine	feedback inhibition	Pseudomonas aeruginosa
leucine	feedback inhibition	Saccharomyces cerevisiae
leucine	feedback inhibition	Salmonella enterica subsp. enterica serovar Typhimurium
methyl-2-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoylsulfamoyl]benzoate	-	Mycobacterium tuberculosis
metsulfuron methyl	-	Mycobacterium tuberculosis
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
additional information	not inhibited by bensulfuron methyl	Mycobacterium tuberculosis
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
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
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
N-phenyl-3-(phenyldisulfanyl)-1H-1,2,4-triazole-1-carboxamide	strong inhibition	Mycobacterium tuberculosis
propan-2-yl 4-bromo-3-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate	-	Mycobacterium tuberculosis
sulfometuron methyl	-	Mycobacterium tuberculosis
valine	feedback inhibition; feedback inhibition; feedback inhibition	Escherichia coli
valine	feedback inhibition	Mycobacterium tuberculosis
valine	feedback inhibition	Pseudomonas aeruginosa
valine	feedback inhibition	Saccharomyces cerevisiae
valine	feedback inhibition	Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

Metals/Ions	Comment	Organism
Ca2+	activates	Salmonella enterica subsp. enterica serovar Typhimurium
Ca2+	activates	Saccharomyces cerevisiae
Ca2+	activates	Pseudomonas aeruginosa
Ca2+	activates	Escherichia coli
Ca2+	activates	Mycobacterium tuberculosis
Cd2+	activates	Salmonella enterica subsp. enterica serovar Typhimurium
Cd2+	activates	Saccharomyces cerevisiae
Cd2+	activates	Pseudomonas aeruginosa
Cd2+	activates	Escherichia coli
Cd2+	activates	Mycobacterium tuberculosis
Mg2+	required	Mycobacterium tuberculosis
Mg2+	a bivalent metal cation is required	Salmonella enterica subsp. enterica serovar Typhimurium
Mg2+	a bivalent metal cation is required	Saccharomyces cerevisiae
Mg2+	a bivalent metal cation is required	Pseudomonas aeruginosa
Mg2+	a bivalent metal cation is required	Escherichia coli
Mg2+	a bivalent metal cation is required	Mycobacterium tuberculosis
Mn2+	activates	Salmonella enterica subsp. enterica serovar Typhimurium
Mn2+	activates	Saccharomyces cerevisiae
Mn2+	activates	Pseudomonas aeruginosa
Mn2+	activates	Escherichia coli
Mn2+	activates	Mycobacterium tuberculosis
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
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
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
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
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)

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

Organism

Organism	UniProt	Comment	Textmining
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	-
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	-
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	-
Mycobacterium tuberculosis	-	-	-
Mycobacterium tuberculosis	P9WG41 and P9WKJ3	large and small subunit encoded by genes ilvB and ilvN; two subunits encoded by genes ilvB and ilvN	-
Mycobacterium tuberculosis H37Rv	P9WG41 and P9WKJ3	large and small subunit encoded by genes ilvB and ilvN; two subunits encoded by genes ilvB and ilvN	-
Pseudomonas aeruginosa	-	-	-
Saccharomyces cerevisiae	-	-	-
Salmonella enterica subsp. enterica serovar Typhimurium	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
2 pyruvate = 2-acetolactate + CO2	catalytic mechanism, detailed overview	Salmonella enterica subsp. enterica serovar Typhimurium	a
2 pyruvate = 2-acetolactate + CO2	catalytic mechanism, detailed overview	Saccharomyces cerevisiae	a
2 pyruvate = 2-acetolactate + CO2	catalytic mechanism, detailed overview	Pseudomonas aeruginosa	a
2 pyruvate = 2-acetolactate + CO2	catalytic mechanism, detailed overview	Escherichia coli	a
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)

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

Subunits

Subunits	Comment	Organism
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
tetramer	the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer	Pseudomonas aeruginosa
tetramer	the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer	Escherichia coli
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

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

Cofactor

Cofactor	Comment	Organism
FAD	-	Mycobacterium tuberculosis
FAD	the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct	Salmonella enterica subsp. enterica serovar Typhimurium
FAD	the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct	Pseudomonas aeruginosa
FAD	the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct	Mycobacterium tuberculosis
FAD	the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct, reaction mechanism molecular modeling	Saccharomyces cerevisiae
FAD	the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct, reaction mechanism molecular modeling	Escherichia coli
thiamine diphosphate	-	Mycobacterium tuberculosis
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
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
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
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
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

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

Expression

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

General Information

General Information	Comment	Organism
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
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
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
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
malfunction	enzyme inhibition abolishes biosynthesis of brachend chain amino acids and leads to bacteriostasis	Salmonella enterica subsp. enterica serovar Typhimurium
malfunction	enzyme inhibition abolishes biosynthesis of brachend chain amino acids and leads to bacteriostasis	Pseudomonas aeruginosa
malfunction	enzyme inhibition abolishes biosynthesis of brachend chain amino acids and leads to bacteriostasis	Escherichia coli
malfunction	enzyme inhibition abolishes biosynthesis of brachend chain amino acids and leads to bacteriostasis	Mycobacterium tuberculosis
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
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
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
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
metabolism	the enzyme catalyzes the first step in biosynthesis of branched amino acids isoleucine, leucine and valine	Saccharomyces cerevisiae
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
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
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
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