2.2.1.6: acetolactate synthase
This is an abbreviated version!
For detailed information about acetolactate synthase, go to the full flat file.
Word Map on EC 2.2.1.6
-
2.2.1.6
-
herbicide
-
weed
-
sulfonylurea
-
als-inhibiting
-
branched-chain
-
imidazolinone
-
biotype
-
cross-resistance
-
herbicide-resistant
-
imazethapyr
-
chlorsulfuron
-
triazolopyrimidine
-
4.1.3.18
-
als-inhibitors
-
glyphosate
-
target-site
-
amaranthus
-
imazamox
-
acetoin
-
sulfometuron
-
2,3-butanediol
-
echinochloa
-
protoporphyrinogen
-
broadleaf
-
2-ketobutyrate
-
non-target-site
-
whole-plant
-
nicosulfuron
-
accase
-
hybridus
-
rigidum
-
waterhemp
-
mesotrione
-
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
-
glyphosate-resistant
-
kochia
-
biotechnology
- 2.2.1.6
-
herbicide
-
weed
- sulfonylurea
-
als-inhibiting
-
branched-chain
- imidazolinone
-
biotype
-
cross-resistance
-
herbicide-resistant
- imazethapyr
- chlorsulfuron
- triazolopyrimidine
-
4.1.3.18
-
als-inhibitors
- glyphosate
-
target-site
- amaranthus
- imazamox
- acetoin
- sulfometuron
- 2,3-butanediol
- echinochloa
- protoporphyrinogen
-
broadleaf
- 2-ketobutyrate
-
non-target-site
-
whole-plant
- nicosulfuron
- accase
- hybridus
- rigidum
-
waterhemp
- mesotrione
-
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
-
glyphosate-resistant
- kochia
- biotechnology
Reaction
2 pyruvate
=
Synonyms
aceto-hydroxy acid synthase, acetohydroxy acid synthase, acetohydroxy acid synthase I, acetohydroxy acid synthetase, acetohydroxyacid synthase, acetolactate pyruvate-lyase (carboxylating), acetolactate synthase, acetolactate synthetase, acetolactate-synthase, acetolactic synthetase, AHAS, AHAS II, AHAS1, AHAS2, AHAS3, AHASL, AHASS, alpha-acetohydroxy acid synthetase, alpha-acetohydroxyacid synthase, alpha-acetolactate synthase, alpha-acetolactate synthetase, alpha-ALS, ALS, ALS1, ALS1R, ALS2, AlsS, CalS, catabolic acetolactate synthase, EC 4.1.3.18, GST-mALS, GST-wALS, Ilv2, Ilv6, ilvB, ilvB1, ilvB2, ilvG, IlvN, ilvX, Moilv2, Moilv6, More, PF0935, sll1981, synthase, acetolactate, TM_0548, TM_0549, TTHA1213
ECTree
2.2.1.6 acetolactate synthaseAdvanced search results
results (
results (Application
Application on EC 2.2.1.6 - acetolactate synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
agriculture
analysis
-
Vis/NIR spectroscopy combined with LS-SVM, i.e. least squares-support vector machine, can be successfully applied for the determination of acetolactate synthase activity and protein content of rapeseed leaves. Vis/NIR spectroscopy is a promising detection technique for the on field applications in oilseed rape
biotechnology
brewing
-
unpleasant butterscotch-like flavor in beer due to accumulation of 2,3-butanedione derives from accumulation of mitochondrial matrix-targeted acetohydroxyacid synthase Ilv2 preprotein in the cytosol. Ilv2 preprotein accumulates in the cytosol of petite yeasts. Expression of a mutant allele of the gamma-subunit of the F1-ATPase, ATP3-5, could be an attractive way to reduce diacetyl formation by petite strains
drug development
molecular biology
pharmacology
synthesis
agriculture
-
inhibitor ZJ0273, i.e. propyl 4-(2-(4,6-dimethoxypyrimidin-2-yloxy)benzylamino)benzoate at 100 mg/l is the optimal dose of herbicide for rapeseed field
agriculture
Nicotiana tabacum plants with transplastomic expression of mutants G121A, A122V, or P197S are specifically tolerant to pyrimidinylcarboxylate, imidazolinon, and sulfonylurea/pyrimidinylcarboxylate herbicides, respectively
agriculture
-
use of two-point mutated gene of acetolactate synthase from herbicide-resistant rice callus as a selectable marker gene in production of transgenic soybeans. T1 soybeans grown from one regenerated plant after selection of the acetolactate synthase targeting pyrimidinyl-carboxy herbicide bispyribacsodium exhibit herbicide resistance, and the introduction and expression of the gene is confirmed by genetic analysis. The selective culturing is applicable to the production of transgenic soybeans
biotechnology
construction of a vector system for chloroplast transformation with acetolactate synthase, generation of a series of Arabidopsis thaliana mutated acetolactate synthase genes and introduction of constructs with the aminoglycoside 3'-adenyltransferase gene into the Nicotiana tabacum chloroplast genome by particle bombardment
biotechnology
the reaction specificity of acetolactate synthase from Thermus thermophilus can be redirected to catalyze acetaldehyde formation to develop a thermophilic pyruvate decarboxylase. Quadruple mutant Y35N/K139R/V172A/H474R shows 3.1fold higher acetaldehyde-forming activity than the wild-type mainly because of H474R amino acid substitution, which likely generates two new hydrogen bonds near the thiamine diphosphate-binding site
biotechnology
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the reaction specificity of acetolactate synthase from Thermus thermophilus can be redirected to catalyze acetaldehyde formation to develop a thermophilic pyruvate decarboxylase. Quadruple mutant Y35N/K139R/V172A/H474R shows 3.1fold higher acetaldehyde-forming activity than the wild-type mainly because of H474R amino acid substitution, which likely generates two new hydrogen bonds near the thiamine diphosphate-binding site
-
drug development
-
the enzyme is a target for drug development
drug development
the enzyme is a target for drug development
drug development
-
AHAS is the target of the sulfonylurea and imidazolinone herbicides
drug development
AHAS is the target of the sulfonylurea and imidazolinone herbicides
drug development
-
the enzyme is an important target for design of environmental-benign herbicides
drug development
-
the enzyme is the target of several herbicides, sulfonylureas, imidazolinones and other herbicides, structures of inhibitor-enzyme complexes explain the herbicide-enzyme interaction
drug development
-
the enzyme is a target for development of herbicides, overview
drug development
-
the enzyme is a target for development of herbicides, overview
drug development
-
the enzyme is a target for development of herbicides, overview
drug development
-
the enzyme is a target for development of herbicides, overview
drug development
the enzyme is a target for development of herbicides, overview
drug development
acetohydroxyacid synthase (AHAS) of Mycobacterium tuberculosis is a promising target for the development of anti-tuberculosis agents
drug development
the enzyme is a target for drug development in tuberculosis treatment
drug development
the enzyme is a target for the development of anti-tuberculosis agents
drug development
-
acetohydroxyacid synthase (AHAS) of Mycobacterium tuberculosis is a promising target for the development of anti-tuberculosis agents
-
drug development
-
the enzyme is a target for the development of anti-tuberculosis agents
-
drug development
-
the enzyme is a target for drug development in tuberculosis treatment
-
molecular biology
the G95A mutation of the ALS gene confers highly specific resistance to pyrimidinyl carboxy herbicides and can be used as a selection marker for transformations
molecular biology
the gene is useful as a selectable marker for introducing foreign traits into rice when used with pyrimidinylcarboxylate herbicides. The double-mutant W548L/S627I of the ALS gene from rice is not only helpful for introducing useful rice genes into rice by self-cloning as a host-derived selectable marker gene but also can extinguish the scientific concern for antibiotic-resistant genes, leading to minimize public concern for this issue in transgenic plants
pharmacology
-
AHAS might be a target protein for the development of anti-tuberculosis therapeutics
pharmacology
-
AHAS might be a target protein for the development of anti-tuberculosis therapeutics
-
synthesis
-
co-expression of acetolactate synthase and omega-transaminase in Escherichia coli as a whole-cell biocatalyst for production of (S)-alpha-benzylamine. Product (S)-alpha-benzylamine can be moved into the extraction solution via an organic solvent
synthesis
-
construction of a mutant with a deleted C-terminal domain in the regulatory subunit IlvN. The constructed enzyme shows altered kinetic properties, i.e., an about twofold-lower Km for the substrate pyruvate and an about fourfold-lower Vmax, a slightly increased Km for the substrate alpha-ketobutyrate with an about twofold-lower Vmax, and insensitivity against the inhibitors L-valine, L-isoleucine, and L-leucine. Introduction of the mutant into the L-lysine producers Corynebacterium glutamicum DM1729 and DM1933 increases L-lysine formation by 43% and 36%, respectively. Complete inactivation of the AHAS in Corynebacterium glutamicum DM1729 and DM1933 by deletion of the ilvB gene, encoding the catalytic subunit of AHAS, leads to L-valine, L-isoleucine, and L-leucine auxotrophy and to further-improved L-lysine production. In batch fermentations, the mutant produces about 85% more L-lysine and shows an 85%-higher substrate-specific product yield
synthesis
-
transformation of a H+-ATPase defective strain with a C-terminal truncation of acetohydroxyacid synthase gene ilvBN results in increased valine production from 21.7 mM for wild-type to 46.7 mM and increase in the valine intermediate acetoin. Inserting acetohydroxyacid isomeroreductase gene into the ilvBN plasmid further increases valine producion
synthesis
Bacillus subtilis acetolactate synthase can act as key biocatalyst in the formation of isobutanol which is deemed to be a next-generation biofuel and a renewable platform chemical. The enzyme AlsS catalyzes the conversion of 2-ketoisovalerate into isobutyraldehyde, the immediate precursor of isobutanol
synthesis
the enzyme in Pyrococcus furiosus is a potential platform for the biological production of acetoin at temperatures in the 70-80°C range. Acetoin, or 3-hydroxybutanone, is an important four-carbon compound that serves as a building block for valuable bio-based chemical compounds and is a common flavor additive and preservative in the food industry
synthesis
acetoin (i.e. 3-hydroxybutanone), is a major product at temperatures below 80 °C. Acetolactate synthase ALS, which is involved in branched-chain amino acid biosynthesis, is responsible and deletion of the Als gene abolishes acetoin production. Deletion of Als in a strain of Pyrococcus furiosus heterologously expressing an alcohol dehydrogenase gene from Thermoanaerobacter sp. X514 for ethanol production significantly improves the yield of ethanol
synthesis
construction of isobutanol production systems by overexpression of effective 2-oxoacid decarboxylase KivD and combinatorial overexpression of valine biosynthetic enzymes in Saccharomyces cerevisiae D452-2. Isobutanol production by the engineered strain is assessed in micro-aerobic batch fermentations using glucose as a sole carbon source, leading to production of 93 mg/l isobutanol, which corresponds to a fourfold improvement as compared with the control strain. Isobutanol production is further enhanced to 151 mg/l by additional overexpression of acetolactate synthase Ilv2p, acetohydroxyacid reductoisomerase Ilv5p, and dihydroxyacid dehydratase Ilv3p in the cytosol
synthesis
engineering of the wild type of Corynebacterium glutamicum for the growth-decoupled production of 2-ketoisovalerate from glucose by deletion of the aceE gene encoding the E1p subunit of the pyruvate dehydrogenase complex, deletion of the transaminase B gene ilvE, and additional overexpression of the ilvBNCD genes, encoding the L-valine biosynthetic enzymes acetohydroxyacid synthase (AHAS), acetohydroxyacid isomeroreductase, and dihydroxyacid dehydratase. 2-Ketoisovalerate production is further improved by deletion of the pyruvate:quinone oxidoreductase gene pqo. In fed-batch fermentations at high cell densities, the newly constructed strains produce up to 188 mM (21.8 g/liter) 2-ketoisovalerate and showd a product yield of about 0.47 mol per mol (0.3 g/g) of glucose and a volumetric productivity of about 4.6 mM (0.53 g/liter) 2-ketoisovalerate per h in the overall production phase
synthesis
overexpression of the als gene leads to high levels of 2,3-butanediol
synthesis
-
Bacillus subtilis acetolactate synthase can act as key biocatalyst in the formation of isobutanol which is deemed to be a next-generation biofuel and a renewable platform chemical. The enzyme AlsS catalyzes the conversion of 2-ketoisovalerate into isobutyraldehyde, the immediate precursor of isobutanol
-
synthesis
-
overexpression of the als gene leads to high levels of 2,3-butanediol
-
synthesis
-
engineering of the wild type of Corynebacterium glutamicum for the growth-decoupled production of 2-ketoisovalerate from glucose by deletion of the aceE gene encoding the E1p subunit of the pyruvate dehydrogenase complex, deletion of the transaminase B gene ilvE, and additional overexpression of the ilvBNCD genes, encoding the L-valine biosynthetic enzymes acetohydroxyacid synthase (AHAS), acetohydroxyacid isomeroreductase, and dihydroxyacid dehydratase. 2-Ketoisovalerate production is further improved by deletion of the pyruvate:quinone oxidoreductase gene pqo. In fed-batch fermentations at high cell densities, the newly constructed strains produce up to 188 mM (21.8 g/liter) 2-ketoisovalerate and showd a product yield of about 0.47 mol per mol (0.3 g/g) of glucose and a volumetric productivity of about 4.6 mM (0.53 g/liter) 2-ketoisovalerate per h in the overall production phase
-
