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
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2.2.1.6
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herbicide
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weed
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sulfonylurea
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als-inhibiting
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branched-chain
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imidazolinone
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biotype
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cross-resistance
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herbicide-resistant
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imazethapyr
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chlorsulfuron
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triazolopyrimidine
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4.1.3.18
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als-inhibitors
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glyphosate
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target-site
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amaranthus
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imazamox
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acetoin
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sulfometuron
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2,3-butanediol
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echinochloa
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protoporphyrinogen
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broadleaf
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2-ketobutyrate
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non-target-site
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whole-plant
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nicosulfuron
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accase
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hybridus
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rigidum
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waterhemp
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mesotrione
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postemergence
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crus-galli
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safener
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5-enolpyruvylshikimate-3-phosphate
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ilvced
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alpha-ketobutyrate
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brewing
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rudis
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dicamba
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synthesis
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agriculture
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molecular biology
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glufosinate
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thdp-dependent
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palmeri
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tuberculatus
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analysis
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alopecurus
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isomeroreductase
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pharmacology
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herbicide-binding
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drug development
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glyphosate-resistant
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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 (Engineering
Engineering on EC 2.2.1.6 - acetolactate synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A122V
A205F
site-directed mutagenesis, the enzyme mutation confers resistance to imidazolinone, sulfonylurea, triazolopyrimidines, sulfonylaminocarbonyl triazolinones, and pyrimidinyl(thio)benzoate herbicides
G121A
Nicotiana tabacum plants with transplastomic expression of mutant are specifically tolerant to pyrimidinylcarboxylate, imidazolinon, and sulfonylurea/pyrimidinylcarboxylate herbicides, respectively
P197L
-
the mutation causes serious cross-resistance to most types of enzyme inhibitors
P197S
S653N
W574L
W574S
H28A
-
site-directed mutagenesis, the mutant enzyme is much less able to catalyze the C-C bond formation as the wild-type enzyme, while the ability for C-C bond cleavage is still intact, the H28A variant shows an 8fold decrease in the formation of (R)-phenylacetylcarbinol (12%), but 1,2-diketone cleavage is nearly unaffected (78% conversion)
H28A/N484A
-
site-directed mutagenesis, the double mutant catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol, variant H28A/N484A shows acceptable formation of (R)-phenylacetylcarbinol (73%), but conversion toward the cleavage product is decreased by a factor of five (17% conversion), the mutant is also active with 1,2-diketone, e.g. cyclohexane-1,2-dione, in contrast to the wild-type enzyme, mutant substrate specificity amd enantioselectivity, overview
H28A
-
site-directed mutagenesis, the mutant enzyme is much less able to catalyze the C-C bond formation as the wild-type enzyme, while the ability for C-C bond cleavage is still intact, the H28A variant shows an 8fold decrease in the formation of (R)-phenylacetylcarbinol (12%), but 1,2-diketone cleavage is nearly unaffected (78% conversion)
-
H28A/N484A
-
site-directed mutagenesis, the double mutant catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol, variant H28A/N484A shows acceptable formation of (R)-phenylacetylcarbinol (73%), but conversion toward the cleavage product is decreased by a factor of five (17% conversion), the mutant is also active with 1,2-diketone, e.g. cyclohexane-1,2-dione, in contrast to the wild-type enzyme, mutant substrate specificity amd enantioselectivity, overview
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K176G
the naturally occuring mutation, substitution of two adenines to guanines in the ilvB gene, causes a cold-sensitive phenotype of mutant strain JH642. The acetolactate synthase efficiency in strain JH642 is reduced by 51fold
K40H
site-directed mutagenesis, the half-life of the mutant at 50°C is 44 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
K40I
K40Y
site-directed mutagenesis, the half-life of the mutant at 50°C is 110 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
P87A
site-directed mutagenesis, the half-life of the mutant at 50°C is 33 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
Q124S
site-directed mutagenesis, the half-life of the mutant at 50°C is 42 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
Q424S
site-directed mutagenesis, the half-life of the mutant at 50°C is 104 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows increased activity compared to the wild-type
Q424S/Q487S
site-directed mutagenesis, the half-life of the mutant at 50°C is 94 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type
Q487A
Q487G
Q487I
Q487L
Q487S
T84V
site-directed mutagenesis, the half-life of the mutant at 50°C is 2.5 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type
Y481A
site-directed mutagenesis, the half-life of the mutant at 50°C is 19 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type
Q487A
-
wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
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Q487G
-
wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
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Q487I
-
loss of acetolactate synthase activity, decrease in decarboxylase activity
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Q487L
-
loss of acetolactate synthase activity, decrease in decarboxylase activity
-
Q487S
-
wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
-
K40H
-
site-directed mutagenesis, the half-life of the mutant at 50°C is 44 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
-
K40I
-
site-directed mutagenesis, the half-life of the mutant at 50°C is 89 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type
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Q487S
S638N
-
the mutant is more resistant to imidazolinone herbicides than the wild type in contrast to sulfonylurea herbicides that inhibit the mutant as well as the wild type enzyme
D376E
-
the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate
P197H
-
the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate
P197L
-
the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate
P197T
-
the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate
W574L
-
the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate
E49A
E49D
E49Q
H111F
H111R
Q112E
Q112N
Q112V
Q411E
Q411N
A36V
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
E47A
E47Q
F109M
-
both substrate affinity and kcat are significantly compromised. The specificity for 2-ketobutyrate as acceptor is not altered
G14A
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
G14D
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
L131R
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
L16A
-
site-directed mutagenesis of the regulatory subunit, the mutant shows increased sensitivity to valine inhibition compared to the wild-type subunit
L9A
-
site-directed mutagenesis of the regulatory subunit, the mutant shows slightly decreased sensitivity to valine inhibition compared to the wild-type subunit
L9H
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
L9V
-
site-directed mutagenesis of the regulatory subunit, the mutant shows slightly decreased sensitivity to valine inhibition compared to the wild-type subunit
N11A
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
N11D
-
site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit
N11H
-
site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit
N29D
-
site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit
N29H
-
site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit
T34C
-
site-directed mutagenesis of the regulatory subunit, the mutant shows decreased sensitivity to valine inhibition compared to the wild-type subunit
T34I
-
site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit
T47C
-
site-directed mutagenesis of the regulatory subunit, the mutant shows decreased sensitivity to valine inhibition compared to the wild-type subunit
V153D
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
V35A
-
site-directed mutagenesis of the regulatory subunit, the mutant shows decreased sensitivity to valine inhibition compared to the wild-type subunit
V375A
V375I
-
slightly reduced kcat value with a moderate increase of the apparent KM of pyruvate. The specificity for 2-ketobutyrate as acceptor is not altered
W464L
E85A
E85D
E85Q
F147A
4fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
F147R
2.5fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
H84A
H84T
P126A
site-directed mutagenesis, the mutant exhibits similar kinetics but significantly lower activity compared to the wild-type enzyme
P126A,
the mutant exhibits significantly lower activity than the wild type enzyme
P126E
P126T
P126V
Q86A
Q86W
W561R
30fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
E85A
-
site-directed mutagenesis, the mutation leads to severe drop in catalyticactivity with reduced affinity toward thiamine diphosphate, , the enzyme shows reduced activity compared to the wild-type enzyme
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E85Q
F147A
-
4fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
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F147R
-
2.5fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
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H84A
P126A
-
site-directed mutagenesis, the mutant exhibits similar kinetics but significantly lower activity compared to the wild-type enzyme
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P126A,
-
the mutant exhibits significantly lower activity than the wild type enzyme
-
P126E
P126T
P126V
W561R
-
30fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
-
P197E
D374A
D374A/D375A
-
strong resistance to Londax and to C, about 2fold increase in affinity for FAD, decrease in activation efficiency for thiamine diphosphate
D374E
-
greatly reduced activity, strong resistance to Londax, 8fold increase in affinity for FAD, decrease in activation efficiency for thiamine diphosphate
D375A
D375E
DELTA567
-
deletion of entire C-terminus including mobile loop and C-terminal lid, no enzymic activity
DELTA567-582
-
deletion of mobile loop region 4.5% of activity compared to wild-type, increase in activation constant of thiamine diphosphate
DELTA598
-
deletion of c-terminus maintaining mobile loop and C-terminal lid, 1.2% of activity compared to wild-type
DELTA630
-
deletion of C-terminal lid, 4.5% of activity compared to wild-type, increase in activation constant of thiamine diphosphate
H351F
-
5fold increase in Km-value, weak resistance to Londax and Cadre, difference in secondary structure compared to wild-type
H351M
-
18fold increase in Km-value, strong resistance to Londax and Cadre, difference in secondary structure compared to wild-type
H351Q
K255F
K255Q
R141A
-
site-directed mutagenesis, inactive mutant, unable to bind the cofactor FAD
R141F
-
site-directed mutagenesis, inactive mutant, unable to bind the cofactor FAD
R141K
-
site-directed mutagenesis, the mutant shows reduced activity and activation by thiamine diphosphate compared to the wild-type enzyme, the mutant is partially resistant to herbicides, e.g. Londax, Cadre, and/or TP
R372F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, the mutant is partially resistant to herbicides, e.g. Londax, Cadre, and/or TP
R372K
-
site-directed mutagenesis, the mutant shows reduced activity and activation by FAD compared to the wild-type enzyme, the mutant is partially resistant to herbicides, e.g. Londax, Cadre, and/or TP
R372S/F373P/D374V
-
site-directed mutagenesis, mutation of the conserved motif 372RFDDR376 results in abolished FAD binding and highly reduced activity
R372S/F373P/D374V/D375E
-
site-directed mutagenesis, mutation of the conserved motif 372RFDDR376 results in abolished FAD binding and highly reduced activity
R372S/F373P/D374V/D375E/R376Y
-
site-directed mutagenesis, mutation of the conserved motif 372RFDDR376 results in abolished FAD binding and highly reduced activity, the mutant is resistant to herbocides
R376F
-
site-directed mutagenesis, inactive mutant, unable to bind the cofactor FAD
R376K
-
site-directed mutagenesis, the mutant shows reduced activity and activation by FAD compared to the wild-type enzyme, the mutant is partially resistant to herbicides, e.g. Londax, Cadre, and/or TP
S167F
-
inactive, mutation abolishes the binding affinity for cofactor FAD. The far-UV spectrum is similar to wild-type
S506F
-
inactive, mutation abolishes the binding affinity for cofactor FAD. The far-UV spectrum is similar to wild-type
S539A
-
73% of wild-type activity, strong resistance to herbicides NC-311, a sulfonylurea, Cadre, an imidazolinone, and a triazolopyrimidine
S539F
-
171% of wild-type activity, strong resistance to herbicides NC-311, a sulfonylurea, Cadre, an imidazolinone, and a triazolopyrimidine
W573F
-
site-directed mutagenesis, the mutant shows 69fold reduced activity compared to the wild-type enzyme, substitution of the W573 residue causes significant perturbations in the activation process and in the binding site of thiamine diphosphate
A96T
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
A96V
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
F180R
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
G95A
the naturally occuring mutation leads to resistance against pyrimidinyl carboxy herbicides, e.g. bispyribac-sodium
M98E
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
M98H
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
M98I
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
P171A
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
P171Q
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
P171S
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
R173A
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
R173E
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
S627D
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
S627F
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
S627I
S627N
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
S627T
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
W548C
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
W548F
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
W548L
W548L/S627I
W548S
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
S627N
the mutation confers tolerance against imidazolinone herbicides, including imazethapyr and imazamox. The mutant is tolerant to imidazolinone but the catalytic efficiency of the mutated enzyme decreases in its presence. Moreover, the activity of the mutated enzyme decreases more in the presence of imazethapyr than in the presence of imazamox
P197A
mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding. Most common mutation among 28 populations resistant to tribenuron
P197L
mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding
P197R
mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding
P197S
mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding
P197T
mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding
A205F
A205V
the mutation confers resistance to imidazolinones, sulfonylureas, triazolopyrimidines, sulfonylamino-carbonyl-triazolinones, and pyrimidinyl (thio) benzoate herbicides
W574L
F204A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
H181A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
H205A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
H219A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
K218A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
L177A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
L222A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
P206A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
R216A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
S212A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
P197S
P197T
W574L
G654D
-
mutant isolated from Ontario population. Mutant confers resistance to herbicide imazethapyr, and cross-resistance to nicosulfuron and flucarbazone
S653I
-
mutant isolated from Ontario population. Mutant confers resistance to herbicide imazethapyr, and cross-resistance to nicosulfuron and flucarbazone
S653N
-
mutant isolated from Ontario population. Mutant confers resistance to herbicide imazethapyr, and cross-resistance to nicosulfuron and flucarbazone
S653T
-
mutant isolated from Ontario population. Mutant confers resistance to herbicide imazethapyr, and cross-resistance to nicosulfuron and flucarbazone
DeltaQ217
E139A
G16D
mutation in the N-terminal part of the regulatory subunit ilvN, affecting regulation by valine. Mutation considerably reduces the interaction of the subunits
G16D/E105stop
no enzymic activity after in vitro reconstitution with large subunit
I106V/A135P
after in vitro reconstitution with large subunit, enzymic activity comparable to wild-type
L18F
Q108stop
no enzymic activity after in vitro reconstitution with large subunit
V17D
V17D/F30L
no enzymic activity after in vitro reconstitution with large subunit
H474R
H747R
mutation leads to 3fold increased acetaldehyde formation, with 30% decrease in acetolactate formation
K139R
V172A
Y35N
Y35N/K139R/V172A/H474R
K139R
additional information
A122V
Nicotiana tabacum plants with transplastomic expression of mutant are specifically tolerant to pyrimidinylcarboxylate, imidazolinon, and sulfonylurea/pyrimidinylcarboxylate herbicides, respectively
P197S
Nicotiana tabacum plants with transplastomic expression of mutant are specifically tolerant to pyrimidinylcarboxylate, imidazolinon, and sulfonylurea/pyrimidinylcarboxylate herbicides, respectively
W574S
-
reduction in sensitivity to sulfonurea herbicides compared to the wild-type enzyme
K40I
site-directed mutagenesis, the half-life of the mutant at 50°C is 89 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type
K40I
the mutant shows slightly improved activity towards 2-oxoisovalerate compared to the wild type enzyme
Q487A
mutation diminishes decarboxylase activity but maintains the synthase activity
Q487A
wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
Q487G
mutation diminishes decarboxylase activity but maintains the synthase activity
Q487G
wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
Q487I
loss of acetolactate synthase activity, decrease in decarboxylase activity
Q487L
loss of acetolactate synthase activity, decrease in decarboxylase activity
Q487S
mutation diminishes decarboxylase activity but maintains the synthase activity
Q487S
site-directed mutagenesis, the half-life of the mutant at 50°C is 22 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
Q487S
wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
Q487S
-
site-directed mutagenesis, the half-life of the mutant at 50°C is 22 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
-
E49A
-
site-directed mutagenesis, the mutant shows decreased activities and weakened thiamine diphosphate binding. The Km for substrate pyruvate is 22fold higher than that of the wild-type cALS. In addition, the E49A mutation also has a drastic effect on cofactor thiamine diphosphate activation. The half-saturating concentration (Kc) for thiamine diphosphate is 2000fold higher than that of wild-type cALS
E49A
-
the mutation causes a 190fold reduction in affinity for thiamine diphosphate
E49D
-
site-directed mutagenesis, the mutant exhibits normal substrate kinetics, with the Km for pyruvate equal to that of wild-type cALS
E49D
-
the mutation causes a 150fold reduction in affinity for thiamine diphosphate
E49Q
-
site-directed mutagenesis, the mutant shows decreased activities and weakened thiamine diphosphate binding, the Kc for ThDP that is 3600fold higher than that of wild-type cALS
E49Q
-
the mutant causes a 170fold reduction in affinity for thiamine diphosphate shows 7% of wild type activity
H111F
site-directed mutagenesis, the mutant enzyme exhibits about 50fold lower specific activity with significant reduction in kcat compared to the wild-type enzyme
H111F
the mutant displays 26fold increase in Km value compared to the wild type enzyme
H111R
site-directed mutagenesis, the mutant enzyme exhibits increasedspecific activity and kcat compared to the wild-type enzyme
H111R
the mutant displays 17fold increase in Km value compared to the wild type enzyme
Q112E
site-directed mutagenesis, the mutant enzyme exhibits about 50fold lower specific activity with significant reduction in kcat compared to the wild-type enzyme
Q112E
the mutant exhibits significantly lower specific activity with 70fold higher Ks for thiamine diphosphate compared to the wild type enzyme
Q112N
site-directed mutagenesis, the mutant enzyme exhibits about 50fold lower specific activity with significant reduction in kcat compared to the wild-type enzyme
Q112N
the mutant exhibits significantly lower specific activity with 15fold higher Ks for thiamine diphosphate compared to the wild type enzyme
Q112V
site-directed mutagenesis, the mutant enzyme exhibits about 50fold lower specific activity with significant reduction in kcat compared to the wild-type enzyme
Q112V
the mutant exhibits significantly lower specific activity with 10fold higher Ks for thiamine diphosphate compared to the wild type enzyme
Q411E
site-directed mutagenesis, the mutant enzyme exhibits increased specific activity and kcat compared to the wild-type enzyme
Q411E
the mutant shows a 10fold rise in Km and a 20fold increase in Ks for thiamine diphosphate compared to the wild type enzyme
Q411N
site-directed mutagenesis, the mutant enzyme has a 3fold increased Km compared to the wild-type enzyme
Q411N
the mutant exhibits increased specific activity and kcat compared to the wild type enzyme
V375A
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mutation in isozyme AHAS II, allows 2-oxo-butanoate to be a good first substrate and the mutant enzyme can synthesize 2-propionyl-2-hydroxybutanoate
V375A
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slightly reduced kcat value with a moderate increase of the apparent KM of pyruvate. The specificity for 2-ketobutyrate as acceptor is not altered
W464L
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the mutant of isozyme AHAS II has lost the preference for 2-ketobutyrate as second substrate
E85A
site-directed mutagenesis, the mutation leads to severe drop in catalyticactivity with reduced affinity toward thiamine diphosphate, , the enzyme shows reduced activity compared to the wild-type enzyme
E85A
the mutation leads to severe drop in catalytic activity (0.08% of wild type activity) with reduced affinity toward thiamine diphosphate
E85A
the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate
E85D
site-directed mutagenesis, the mutation leads to severe drop in catalyticactivity with reduced affinity toward thiamine diphosphate
E85D
the mutation leads to severe drop in catalytic activity (2.23% of wild type activity) with reduced affinity toward thiamine diphosphate
E85Q
site-directed mutagenesis, the mutation leads to severe drop in catalyticactivity with reduced affinity toward thiamine diphosphate
E85Q
the mutation leads to severe drop in catalytic activity (1.2% of wild type activity) with reduced affinity toward thiamine diphosphate
H84A
site-directed mutagenesis, the mutation leads to the loss of many hydrogen bonds among residues His84, Glu85, and Gln86 in wild-type enzyme
H84A
the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate
H84T
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
H84T
the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate
P126T
site-directed mutagenesis, the mutant exhibits significantly lower activity than wild-type enzyme and a significantly decreased preference toward thiamine diphosphate as cofactor
P126T
the mutant exhibits significantly lower activity than the wild type enzyme
P126V
site-directed mutagenesis, the mutant exhibits significantly lower activity than wild-type enzyme and a significantly decreased preference toward pyruvate as substrate
P126V
the mutant exhibits significantly lower activity than the wild type enzyme
Q86A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
Q86A
the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate
Q86W
the mutation completely abolishes the enzyme's activity
E85Q
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site-directed mutagenesis, the mutation leads to severe drop in catalyticactivity with reduced affinity toward thiamine diphosphate
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E85Q
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the mutation leads to severe drop in catalytic activity (1.2% of wild type activity) with reduced affinity toward thiamine diphosphate
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H84A
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site-directed mutagenesis, the mutation leads to the loss of many hydrogen bonds among residues His84, Glu85, and Gln86 in wild-type enzyme
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H84A
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the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate
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P126T
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site-directed mutagenesis, the mutant exhibits significantly lower activity than wild-type enzyme and a significantly decreased preference toward thiamine diphosphate as cofactor
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P126T
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the mutant exhibits significantly lower activity than the wild type enzyme
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P126V
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site-directed mutagenesis, the mutant exhibits significantly lower activity than wild-type enzyme and a significantly decreased preference toward pyruvate as substrate
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P126V
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the mutant exhibits significantly lower activity than the wild type enzyme
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P197E
site-directed mutagenesis, the mutation confers broad-spectrum resistance across ALS inhibitors. A subpopulation (WRR04) is generated and is individually homozygous for the Pro197Glu substitution. The WRR04 population exhibits broad-spectrum resistance to tribenuron (318fold), pyrithiobac sodium (over 197fold), pyroxsulam (81fold), florasulam (over 36fold) and imazethapyr (11fold). The ALS from WRR04 shows high resistance to all the tested ALS inhibitors
P197E
the mutation leads to high resistance to inhibitors tribenuron, pyrithiobac sodium, pyroxsulam (TP, 81-fold), florasulam, and imazethapyr
D374A
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substrate inhibition at high concentrations, strong resistance to Londax and Cadre, 10fold increase in activation efficiency for thiamine diphosphate
D375E
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about 3fold reduction in Km-value, strong resistance to Londax, about 3fold increase in activation efficiency of FAD
H351Q
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60fold increase in Km-value, strong resistance to Londax and Cadre, difference in secondary structure compared to wild-type
K255F
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strong resistance to Londax, Cadre and N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
K255Q
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strong resistance to Londax, Cadre and N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
S627I
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
W548L
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
W548L/S627I
a naturally occuring mutation, the recombinant enzyme shows resistance to multiple herbicides including pyrimidinylcarboxylate, sulfonylurea and imidazolinone herbicides, and shows stronger resistance to pyrimidinylcarboxylate herbicides than to other herbicides. Bispyribac-sodium, a pyrimidinylcarboxylate herbicide, has almost no effect on the enzyme at up to 100m M, which is an approximately 10000fold higher concentration than the concentration required for 50% inhibition of the wild-type. The resistance level of the double mutant W548L/S627I BS is stronger than the additive effect predicted from the degree of resistance of each single amino acid mutated ALS, phenotype, overview
W548L/S627I
mutant confers resistance to multiple herbicides including pyrimidinylcarboxylate, sulfonylurea and imidazolinone herbicides, and shows stronger resistance to pyrimidinylcarboxylate herbicides than to other herbicides. Bispyribac-sodium has almost no effect on the enzyme even at 100 mM, which is an approximately 10000fold higher concentration than the concentration required for 50% inhibition of the wild-type. The resistance level of W548L/S627I is stronger than the additive effect predicted from the degree of resistance of each single amino acid mutated. Transformed rice cells carrying this gene and a regenerated rice plant express resistance to bispyribac-sodium
W548L/S627I
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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
A205F
the A205F substitution in acetolactate synthase, confirmed in a population of allotetraploid annual bluegrass, confers resistance to imidazolinone, sulfonylurea, triazolopyrimidines, sulfonylamino-carbonyl-triazolinones, and pyrimidinyl (thio) benzoate herbicides
A205F
the A205F substitution in acetolactate synthase, confirmed in a population of allotetraploid annual bluegrass, confers resistance to imidazolinone, sulfonylurea, triazolopyrimidines, sulfonylaminocarbonyl triazolinones, and pyrimidinyl(thio)benzoate herbicides
A205F
the mutation confers high resistance to imidazolinones, sulfonylureas, triazolopyrimidines, sulfonylamino-carbonyl-triazolinones, and pyrimidinyl (thio) benzoate herbicides
W574L
the mutation confers resistance to imidazolinones, sulfonylureas, triazolopyrimidines, sulfonylamino-carbonyl-triazolinones, and pyrimidinyl (thio) benzoate herbicides
W574L
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the mutation causes herbicide resistance. The mutant enzyme is over 9000fold more resistant towards metsulfuron-methyl and imazethapyr than the wild type enzyme
P197S
naturally occuring mutation leading to resistance against the sulfonylurea herbicide imazosulfuron
P197S
the mutant shows increased resistance against imazosulfuron
P197T
naturally occuring mutation leading to resistance against the sulfonylurea herbicide imazosulfuron
P197T
the mutant shows increased resistance against imazosulfuron
W574L
naturally occuring mutation leading to resistance against the sulfonylurea herbicide imazosulfuron
W574L
the mutant shows increased resistance against imazosulfuron
DeltaQ217
mutation in subunit ilvB, mutant enzyme is activated by valine and resisitant to 3-chlorobutanoate and norleucine
DeltaQ217
mutation in the beta-domain of the catalytic subunit, affecting regulation by valine. Mutation is located on the surface of the catalytic subunit dimer and lowers the interaction with the regulatory subunit
E139A
mutation in a conservative loop near the active center, mutant enzyme is activated by valine and resistant to 2-oxobutanoate
E139A
mutation in the alpha-domain of the catalytic subunit, affecting regulation by valine. Mutation is located on the surface of the catalytic subunit dimer and lowers the interaction with the regulatory subunit
L18F
no enzymic activity after in vitro reconstitution with large subunit
L18F
mutation in the N-terminal part of the regulatory subunit ilvN, affecting regulation by valine. Mutation does not influence the interaction of the subunits
V17D
no enzymic activity after in vitro reconstitution with large subunit
V17D
mutation in the N-terminal part of the regulatory subunit ilvN, affecting regulation by valine. Mutation considerably reduces the interaction of the subunits
H474R
the mutant shows reduced activity compared to the wild type enzyme
H474R
site-directed mutagenesis, the reaction specificity of acetolactate synthase from Thermus thermophilus is redirected to catalyze acetaldehyde formation to develop a thermophilic pyruvate decarboxylase. The mutation likely generates two new hydrogen bonds near the thiamine diphosphate-binding site. These hydrogen bonds might result in the better accessibility of H+ to the substrate-cofactor-enzyme intermediate and a shift in the reaction specificity of the enzyme
K139R
the mutant shows slightly reduced activity compared to the wild type enzyme
V172A
the mutant shows reduced activity compared to the wild type enzyme
Y35N
the mutant shows reduced activity compared to the wild type enzyme
Y35N/K139R/V172A/H474R
the mutant shows strongly reduced activity compared to the wild type enzyme
Y35N/K139R/V172A/H474R
shows 3.1fold higher acetaldehyde-forming activity than the wild-type
K139R
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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the mutant shows slightly reduced activity compared to the wild type enzyme
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additional information
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identification and phenotypes of herbicide-resistant mutant enzymes, overview
additional information
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substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview
additional information
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substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview
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additional information
structure-guided mutagenesis strategy to generate enzyme AlsS variants
additional information
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structure-guided mutagenesis strategy to generate enzyme AlsS variants
additional information
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structure-guided mutagenesis strategy to generate enzyme AlsS variants
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additional information
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identification and phenotypes of herbicide-resistant mutant enzymes, overview
additional information
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mutations of the residues M8 and M13 of the small, regulatory subunit encoded by gene ilvN result in reduced sensitivity of the mutant enzymes to feedback inhibition which leads to increased production of valine as well as of isoleucine and leucine
additional information
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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
additional information
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the 138th (alanine) and 404th (valine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme
additional information
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the 138th (valine) and 404th (alanine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme. The 138th valine of subunit IlvB is beneficial for the L-valine biosynthesis
additional information
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the 138th (alanine) and 404th (valine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme
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additional information
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the 138th (valine) and 404th (alanine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme. The 138th valine of subunit IlvB is beneficial for the L-valine biosynthesis
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additional information
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the 138th (alanine) and 404th (valine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme
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additional information
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the 138th (valine) and 404th (alanine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme. The 138th valine of subunit IlvB is beneficial for the L-valine biosynthesis
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additional information
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the aspartate substitution significantly affects the activation of thiamine diphosphate. The Kc for thiamine diphosphate is determined to be 280fold higher than that of wild-type cALS
additional information
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isozyme AHAS II mutants of residues Phe109, Met250, Arg276 and Trp464 are nearly inactive in (S)-2-acetolactate formation, but show increased activity with pyruvate and benzaldehyde compared to the wild-type isozyme
additional information
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the truncated mutant DELTA80 is resistant to inhibition by valine
additional information
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identification and phenotypes of herbicide-resistant mutant enzymes, overview
additional information
identification and phenotypes of herbicide-resistant mutant enzymes, overview
additional information
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identification and phenotypes of herbicide-resistant mutant enzymes, overview
additional information
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mutants with overexpression of 2-acetolactate synthase (ALS), 2-acetolactate decarboxylase, and acetoin reductase, either individually or in combination, are constructed to improve 2,3-butanediol production in Klebsiella pneumoniae. The strain (KG-rs) that overexpresses both 2-acetolactate synthase and acetoin reductase shows an improved 2,3-butanediol yield. When cultured in the media with five different carbon sources (glucose, galactose, fructose, sucrose, and lactose), the mutant exhibits higher 2,3-butanediol productivity and production than the parental strain in all the tested carbon sources except for lactose. The 2,3-butanediol production of strain KG-rs in a batch fermentation with glucose as the carbon source is 12% higher than that of the parental strain, overview
additional information
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mutants with overexpression of 2-acetolactate synthase (ALS), 2-acetolactate decarboxylase, and acetoin reductase, either individually or in combination, are constructed to improve 2,3-butanediol production in Klebsiella pneumoniae. The strain (KG-rs) that overexpresses both 2-acetolactate synthase and acetoin reductase shows an improved 2,3-butanediol yield. When cultured in the media with five different carbon sources (glucose, galactose, fructose, sucrose, and lactose), the mutant exhibits higher 2,3-butanediol productivity and production than the parental strain in all the tested carbon sources except for lactose. The 2,3-butanediol production of strain KG-rs in a batch fermentation with glucose as the carbon source is 12% higher than that of the parental strain, overview
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additional information
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mutants with overexpression of 2-acetolactate synthase (ALS), 2-acetolactate decarboxylase, and acetoin reductase, either individually or in combination, are constructed to improve 2,3-butanediol production in Klebsiella pneumoniae. The strain (KG-rs) that overexpresses both 2-acetolactate synthase and acetoin reductase shows an improved 2,3-butanediol yield. When cultured in the media with five different carbon sources (glucose, galactose, fructose, sucrose, and lactose), the mutant exhibits higher 2,3-butanediol productivity and production than the parental strain in all the tested carbon sources except for lactose. The 2,3-butanediol production of strain KG-rs in a batch fermentation with glucose as the carbon source is 12% higher than that of the parental strain, overview
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additional information
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identification of naturally occuring mutations leading to herbicide resistance of the plants, e.g. chlorsulfuron-resistant plants, overview. ALS-inhibiting herbicides occur in Lactuca serriola within a relatively small geographical area
additional information
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identification and phenotypes of herbicide-resistant mutant enzymes, overview
additional information
several mutations, including deletion mutations W548deletion, P171deletion and S627deletion, reduce the enzyme's sensitivity to herbicides, overview
additional information
among 28 populations resistant to herbiced tribenuron, nine individuals have only the mutant ALS gene and are homozygous, 18 individuals have both the wild type and the mutant ALS gene and are heterozygous, whereas one individual is heterozygous but with two different mutant ALS alleles
additional information
cloning of a herbicide-resistant acetohydroxyacid synthase gene from Pseudomonas sp. Lm10. Sequence analysis shows that the regulatory subunit of the resisitant enzyme is identical to that of Pseudomonas putida KT2440, whereas six mutations are found in the catalytic subunit, i.e. resistant AHAS/sensitive AHAS: H134N, A135P, S136T, I210V, F264Y, and S486W
additional information
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cloning of a herbicide-resistant acetohydroxyacid synthase gene from Pseudomonas sp. Lm10. Sequence analysis shows that the regulatory subunit of the resisitant enzyme is identical to that of Pseudomonas putida KT2440, whereas six mutations are found in the catalytic subunit, i.e. resistant AHAS/sensitive AHAS: H134N, A135P, S136T, I210V, F264Y, and S486W
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additional information
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generation of the deletion mutants DELTAMoilv2 and DELTAMoilv6. Phenotypic analysis shows that both mutants are auxotrophic for leucine, isoleucine and valine, and are defective in conidial morphogenesis, appressorial penetration and pathogenicity
additional information
G4NC97; G4MMK2
generation of the deletion mutants DELTAMoilv2 and DELTAMoilv6. Phenotypic analysis shows that both mutants are auxotrophic for leucine, isoleucine and valine, and are defective in conidial morphogenesis, appressorial penetration and pathogenicity
additional information
Pyricularia oryzae Guy11
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generation of the deletion mutants DELTAMoilv2 and DELTAMoilv6. Phenotypic analysis shows that both mutants are auxotrophic for leucine, isoleucine and valine, and are defective in conidial morphogenesis, appressorial penetration and pathogenicity
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additional information
engineering of a strain of Pyrococcus furiosus to contain an additional pathway for ethanol production. Enzyme ALS deletion abolishes acetoin formation and improves ethanol production in the alcohol dehydrogenase ADHA strain. High level expression of enzyme ALS uncouples the temperature-dependence of acetoin formation
additional information
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engineering of a strain of Pyrococcus furiosus to contain an additional pathway for ethanol production. Enzyme ALS deletion abolishes acetoin formation and improves ethanol production in the alcohol dehydrogenase ADHA strain. High level expression of enzyme ALS uncouples the temperature-dependence of acetoin formation
additional information
identification and phenotypes of herbicide-resistant mutant enzymes, overview
additional information
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expression of an Ilv2 variant that lacks the N-terminal mitochondrial targeting sequence leads to highly elevated diacetyl levels comparable to a petite strain. 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
additional information
shortening of the regulatory subunit to 107 residues reduces the interaction with the catalytic subunit essentially
additional information
shortening of the regulatory subunit to 107 residues reduces the interaction with the catalytic subunit essentially
additional information
genotyping by random mutagenesis, error-prone PCR and mutant library screening leading to the identification of a quadruple mutant with 3.1fold higher acetaldehyde-forming activity than the wild-type, mutant reaction-specificity profiles
additional information
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genotyping by random mutagenesis, error-prone PCR and mutant library screening leading to the identification of a quadruple mutant with 3.1fold higher acetaldehyde-forming activity than the wild-type, mutant reaction-specificity profiles
additional information
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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genotyping by random mutagenesis, error-prone PCR and mutant library screening leading to the identification of a quadruple mutant with 3.1fold higher acetaldehyde-forming activity than the wild-type, mutant reaction-specificity profiles
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