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Information on EC 2.2.1.6 - acetolactate synthase and Organism(s) Oryza sativa and UniProt Accession Q6K2E8
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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
-
herbicide
-
weed
- sulfonylurea
-
als-inhibiting
-
branched-chain
- imidazolinone
-
biotype
-
cross-resistance
-
herbicide-resistant
- imazethapyr
- chlorsulfuron
- triazolopyrimidine
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4.1.3.18
-
als-inhibitors
- glyphosate
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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
The taxonomic range for the selected organisms is: Oryza sativa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetohydroxy acid synthase
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acetohydroxy acid synthetase
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acetohydroxyacid synthase
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acetolactate pyruvate-lyase (carboxylating)
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acetolactate synthetase
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acetolactic synthetase
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AHAS
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alpha-acetohydroxy acid synthetase
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alpha-acetohydroxyacid synthase
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alpha-acetolactate synthase
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alpha-acetolactate synthetase
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alpha-ALS
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GST-mALS
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GST-wALS
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synthase, acetolactate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
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C-C bond formation
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-
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PATHWAY SOURCE
PATHWAYS
KEGG
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-, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
pyruvate:pyruvate acetaldehydetransferase (decarboxylating)
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.
CAS REGISTRY NUMBER
COMMENTARY
9027-45-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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acetolactate synthase is the first common enzyme in the biosynthetic pathway of branched-chain amino acids
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?
additional information
?
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acetolactate synthase is the first common enzyme in the biosynthetic pathway of branched-chain amino acids
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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acetolactate synthase is the first common enzyme in the biosynthetic pathway of branched-chain amino acids
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-
?
additional information
?
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acetolactate synthase is the first common enzyme in the biosynthetic pathway of branched-chain amino acids
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bispyribac-sodium
almost no effect on the mutant W548L/S627I even at 100 mM, which is an approximately 10000fold higher concentration than the concentration required for 50% inhibition of the wild-type
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00002
ethyl 5-[(4,6-dimethoxy-2-pyrimidinyl)aminocarbonylaminosulfonyl]-1-methyl-1H-pyrazole-4-carboxylate
Oryza sativa
wild-type, pH 7.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
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
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
W548L/S627I
W548S
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
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
additional information
several mutations, including deletion mutations W548deletion, P171deletion and S627deletion, reduce the enzyme's sensitivity to herbicides, overview
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain JM105 by glutathione affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ALS gene, DNA and amino acid sequence determination and analysis, expression of GST-tagged ALS wild-type and mutant enzymes in Escherichia coli strain JM105. expression in transgenic Oryza sativa var. Nipponbare plants using the Agrobacterium tumefaciens transfection method
gene ALS, DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes, the ALS gene exists as a single copy gene in rice and contains no introns
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
agriculture
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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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kawai, K.; Kaku, K.; Izawa, N.; Shimizu, T.; Fukuda, A.; Tanaka, Y.
A novel mutant acetolactate synthase gene from rice cells, which confers resistance to ALS-inhibiting herbicides
J. Pestic. Sci.
32
89-98
2007
Oryza sativa (Q6K2E8)
-
Tougou, M.; Yamagishi, N.; Furutani, N.; Kaku, K.; Shimizu, T.; Takahata, Y.; Sakai, J.; Kanematsu, S.; Hidaka, S.
The application of the mutated acetolactate synthase gene from rice as the selectable marker gene in the production of transgenic soybeans
Plant Cell Rep.
28
769-776
2009
Oryza sativa
Okuzaki, A.; Shimizu, T.; Kaku, K.; Kawai, K.; Toriyama, K.
A novel mutated acetolactate synthase gene conferring specific resistance to pyrimidinyl carboxy herbicides in rice
Plant Mol. Biol.
64
219-224
2007
Oryza sativa (Q6K2E8), Oryza sativa
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