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Information on EC 2.2.1.6 - acetolactate synthase
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2.2.1.6 acetolactate synthaseIUBMB Comments
This enzyme requires thiamine diphosphate. The reaction shown is in the pathway of biosynthesis of valine; the enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine.
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Word Map
- 2.2.1.6
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herbicide
-
weed
- sulfonylurea
-
als-inhibiting
-
branched-chain
- imidazolinone
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biotype
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cross-resistance
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herbicide-resistant
- imazethapyr
- chlorsulfuron
- triazolopyrimidine
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4.1.3.18
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als-inhibitors
- glyphosate
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target-site
- amaranthus
- imazamox
- acetoin
- sulfometuron
- 2,3-butanediol
- echinochloa
- protoporphyrinogen
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broadleaf
- 2-ketobutyrate
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non-target-site
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whole-plant
- nicosulfuron
- accase
- hybridus
- rigidum
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waterhemp
- mesotrione
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postemergence
- crus-galli
-
safener
- 5-enolpyruvylshikimate-3-phosphate
-
ilvced
- alpha-ketobutyrate
- brewing
- rudis
- dicamba
- synthesis
- agriculture
- molecular biology
- glufosinate
-
thdp-dependent
- palmeri
- tuberculatus
- analysis
-
alopecurus
-
isomeroreductase
- pharmacology
-
herbicide-binding
- drug development
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glyphosate-resistant
- kochia
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
acetolactate synthase, acetohydroxy acid synthase, alpha-acetolactate synthase, ahas1, ahass, ahas2, ahas ii, acetohydroxy acid synthetase, acetohydroxy acid synthase i, ahas3, 
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
2 pyruvate = 2-acetolactate + CO2
specificity of carboligation and product liberation may be cumulative if the former is not completely committed
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2 pyruvate = 2-acetolactate + CO2
action model for the regulatory subunit
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2 pyruvate = 2-acetolactate + CO2
catalytic mechanism and active site structure, covalent intermediates
2 pyruvate = 2-acetolactate + CO2
catalytic mechanism via thiamine diphosphate-bound intermediates, structure-activity relationship of isozyme AHAS II
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2 pyruvate = 2-acetolactate + CO2
catalytic mechanism, covalent intermediates
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2 pyruvate = 2-acetolactate + CO2
residue W573 is structurally important for FAD binding, the maintainance of the active site structure, and catalysis
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2 pyruvate = 2-acetolactate + CO2
residues R141, R372, and R376 are located in the active site and are essential for cofactor binding and activity
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2 pyruvate = 2-acetolactate + CO2
the enzyme catalyzes the decarboxylation of bound pyruvate to form a hydroxyethyl-thiamine diphosphate anion/enamine intermediate, which normally reacts with a second molecule of an alpha-ketoacid to form an acetohydroxyacid, but can also perform several side reactions proceeding through the hydroxyethyl-thiamine diphosphate anion/enamine intermediate
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2 pyruvate = 2-acetolactate + CO2
catalytic mechanism of the catalytic subunit involving the thiamine diphopshtae cofactor, overview
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2 pyruvate = 2-acetolactate + CO2
catalytic mechanism of the catalytic subunit involving the thiamine diphosphate cofactor, overview
2 pyruvate = 2-acetolactate + CO2
catalytic mechanism of the catalytic subunit involving the thiamine diphosphtae cofactor, overview
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2 pyruvate = 2-acetolactate + CO2
catalytic mechanism of the catalytic subunit involving the thiamine diphosphtae cofactor, overview
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2 pyruvate = 2-acetolactate + CO2
catalytic mechanism of the catalytic subunit involving the thiamine diphosphtae cofactor, overview
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2 pyruvate = 2-acetolactate + CO2
catalytic mechanism, detailed overview
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2 pyruvate = 2-acetolactate + CO2
catalytic mechanism, detailed overview
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2 pyruvate = 2-acetolactate + CO2
catalytic mechanism, detailed overview
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2 pyruvate = 2-acetolactate + CO2
catalytic mechanism, detailed overview
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
2 pyruvate = 2-acetolactate + CO2
the reaction proceeds via the formation of a common substrate-cofactor-enzyme complex. The carbonyl addition of pyruvate to thiamine diphosphate yields a predecarboxylation intermediate followed by the elimination of carbon dioxide, resulting in the formation of a central and highly reactive intermediate, 2-hydroxyethyl-thiamine diphosphate. The carboligation between 2-hydroxyethyl-TPP and the second pyruvate molecule leads to the liberation of the reaction product, acetolactate, and the catalytic cycle is completed
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
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2 pyruvate = 2-acetolactate + CO2
the reaction proceeds via the formation of a common substrate-cofactor-enzyme complex. The carbonyl addition of pyruvate to thiamine diphosphate yields a predecarboxylation intermediate followed by the elimination of carbon dioxide, resulting in the formation of a central and highly reactive intermediate, 2-hydroxyethyl-thiamine diphosphate. The carboligation between 2-hydroxyethyl-TPP and the second pyruvate molecule leads to the liberation of the reaction product, acetolactate, and the catalytic cycle is completed
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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2 pyruvate = 2-acetolactate + CO2
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PATHWAY SOURCE
PATHWAYS
KEGG