Information on EC 2.2.1.6 - acetolactate synthase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
2.2.1.6
-
RECOMMENDED NAME
GeneOntology No.
acetolactate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
Breslow's mechanism
-
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
acid-base chemical mechanism
-
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
specificity of carboligation and product liberation may be cumulative if the former is not completely committed
-
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
structural model of enzyme
-
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
uni uni ping pong bi bi mechanism
-
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
action model for the regulatory subunit
-
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
catalytic mechanism and active site structure, covalent intermediates
-
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
catalytic mechanism via thiamine diphosphate-bound intermediates, structure-activity relationship of isozyme AHAS II
-
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
catalytic mechanism, covalent intermediates
-
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
residue W573 is structurally important for FAD binding, the maintainance of the active site structure, and catalysis
-
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
residues R141, R372, and R376 are located in the active site and are essential for cofactor binding and activity
-
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
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
-
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
catalytic mechanism of the catalytic subunit involving the thiamine diphopshtae cofactor, overview
-
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
catalytic mechanism of the catalytic subunit involving the thiamine diphosphate cofactor, overview
Q42768
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
catalytic mechanism of the catalytic subunit involving the thiamine diphosphtae cofactor, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-C bond formation
-
-
-
-
decarboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(R)-acetoin biosynthesis I
-
-
(R)-acetoin biosynthesis II
-
-
(S)-acetoin biosynthesis
-
-
acetoin degradation
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Butanoate metabolism
-
-
C5-Branched dibasic acid metabolism
-
-
isoleucine metabolism
-
-
L-isoleucine biosynthesis I (from threonine)
-
-
L-isoleucine biosynthesis II
-
-
L-isoleucine biosynthesis III
-
-
L-isoleucine biosynthesis IV
-
-
L-valine biosynthesis
-
-
Metabolic pathways
-
-
Pantothenate and CoA biosynthesis
-
-
pyruvate fermentation to isobutanol (engineered)
-
-
valine metabolism
-
-
Valine, leucine and isoleucine biosynthesis
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetohydroxy acid synthase
-
-
-
-
acetohydroxy acid synthase
-
-
acetohydroxy acid synthase
-
-
acetohydroxy acid synthase
-
-
acetohydroxy acid synthase
Haloferax volcanii DSM 3757
-
-
-
acetohydroxy acid synthase
-
-
acetohydroxy acid synthase
-
-
-
acetohydroxy acid synthase
-
-
acetohydroxy acid synthase
-
-
acetohydroxy acid synthase I
-
-
acetohydroxy acid synthetase
-
-
-
-
acetohydroxyacid synthase
-
-
-
-
acetohydroxyacid synthase
-
-
acetohydroxyacid synthase
-
-
acetohydroxyacid synthase
-
-
acetohydroxyacid synthase
-
-
acetohydroxyacid synthase
-
-
acetohydroxyacid synthase
Q42768
-
acetohydroxyacid synthase
P45261
-
acetohydroxyacid synthase
-
-
acetohydroxyacid synthase
-
-
acetohydroxyacid synthase
-
-
-
acetohydroxyacid synthase
-
-
acetohydroxyacid synthase
-
-
acetohydroxyacid synthase
P07342
-
acetolactate pyruvate-lyase (carboxylating)
-
-
-
-
acetolactate synthetase
-
-
-
-
acetolactic synthetase
-
-
-
-
AHAS
-
-
-
-
AHAS
Q42768
-
AHAS
Haloferax volcanii DSM 3757
-
-
-
AHAS II
-
-
alpha-acetohydroxy acid synthetase
-
-
-
-
alpha-acetohydroxyacid synthase
-
-
-
-
alpha-acetolactate synthase
-
-
-
-
alpha-acetolactate synthetase
-
-
-
-
alpha-ALS
-
-
-
-
EC 4.1.3.18
-
-
formerly
-
GST-mALS
-
-
-
-
GST-wALS
-
-
-
-
sll1981
Synechocystis sp. PCC6803
-
-
-
synthase, acetolactate
-
-
-
-
additional information
-
the enzyme belongs to the ThDP-dependent family of enzymes
additional information
Q42768
the enzyme belongs to the ThDP-dependent family of enzymes
additional information
-
the enzyme belongs to the ThDP-dependent family of enzymes
additional information
P07342
the enzyme belongs to the ThDP-dependent family of enzymes
additional information
-
the enzyme belongs to the ThDP-dependent family of enzymes
CAS REGISTRY NUMBER
COMMENTARY
9027-45-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
chloroplast enzyme
UniProt
Manually annotated by BRENDA team
herbicide sensitive cell line
-
-
Manually annotated by BRENDA team
mutant enzymes A122V, W574S, W574L and S653N
-
-
Manually annotated by BRENDA team
three isoenzymes AHASI-AHASIII
-
-
Manually annotated by BRENDA team
large subunit; wild-type strain MR168 and mutant strain JH642, gene ilvB
UniProt
Manually annotated by BRENDA team
strain RH33::[pRB63]n, gene alsS
-
-
Manually annotated by BRENDA team
Bacillus subtilis RH33::[pRB63]n
strain RH33::[pRB63]n, gene alsS
-
-
Manually annotated by BRENDA team
2 enzyme forms
-
-
Manually annotated by BRENDA team
genes ilvBN of the ilvBNC operon, genes ilvB and ilvN encode the catalytic and the small, regulatory subunits, respectively
-
-
Manually annotated by BRENDA team
pH 6 acetolactate forming enzyme
-
-
Manually annotated by BRENDA team
strain 1-12, 3 types of enzyme: sensitive pH 8.0 enzyme, insensitive pH 6.0 enzyme, insensitive pH 8.0 enzyme
-
-
Manually annotated by BRENDA team
Enterobacter aerogenes 01. Dez
strain 1-12, 3 types of enzyme: sensitive pH 8.0 enzyme, insensitive pH 6.0 enzyme, insensitive pH 8.0 enzyme
-
-
Manually annotated by BRENDA team
2 enzyme form AHS I and AHS II
-
-
Manually annotated by BRENDA team
3 isoenzymes: I, II, and III
-
-
Manually annotated by BRENDA team
3 isoenzymes: I, II, and III; isoenzyme I and III are expressed in wild type cells, isoenzyme II is cryptic; K-12
-
-
Manually annotated by BRENDA team
acetohydroxy acid synthase isozyme II
-
-
Manually annotated by BRENDA team
AHAS isoenzyme II
-
-
Manually annotated by BRENDA team
isoenzyme AHS III; K-12
-
-
Manually annotated by BRENDA team
isoenzyme I
-
-
Manually annotated by BRENDA team
isoenzyme I; isoenzyme III; K-12
-
-
Manually annotated by BRENDA team
isoenzyme I; K-12
-
-
Manually annotated by BRENDA team
isoenzyme II
-
-
Manually annotated by BRENDA team
isoform acetohydroxyacid synthase I
-
-
Manually annotated by BRENDA team
isoform AHAS II
-
-
Manually annotated by BRENDA team
isozyme AHAS I
-
-
Manually annotated by BRENDA team
isozyme AHAS II
-
-
Manually annotated by BRENDA team
isozyme I
-
-
Manually annotated by BRENDA team
isozyme III
-
-
Manually annotated by BRENDA team
isozymes AHAS I, AHAS II, AHAS III
-
-
Manually annotated by BRENDA team
isozymes AHAS I-III
-
-
Manually annotated by BRENDA team
isozymes I-III
-
-
Manually annotated by BRENDA team
isozymes I-III, subunit-encoding genes ilvB and ilvN
-
-
Manually annotated by BRENDA team
K-12; wild type and two isogenic strains PS1035, containing only acetohydroxy acid synthase III, and strain PS1036, containing only acetohydroxy acid synthase I
-
-
Manually annotated by BRENDA team
strain MG1655, gene ilvBN
-
-
Manually annotated by BRENDA team
large subunit
UniProt
Manually annotated by BRENDA team
Haloferax volcanii DSM 3757
-
-
-
Manually annotated by BRENDA team
two isozymes
-
-
Manually annotated by BRENDA team
subsp. lactis bv, diacetylactis
-
-
Manually annotated by BRENDA team
collected in South Australia
-
-
Manually annotated by BRENDA team
strain NCW1
-
-
Manually annotated by BRENDA team
strain NCW1, overexpression in Escherichia coli
-
-
Manually annotated by BRENDA team
Leuconostoc lactis NCW1
strain NCW1
-
-
Manually annotated by BRENDA team
Leuconostoc lactis NCW1
strain NCW1, overexpression in Escherichia coli
-
-
Manually annotated by BRENDA team
subsp. cremonis
-
-
Manually annotated by BRENDA team
var. dubia and var. major, collected in Daisen, Japan
-
-
Manually annotated by BRENDA team
collected in Daisen, Japan
-
-
Manually annotated by BRENDA team
collected in Daisen, Japan
-
-
Manually annotated by BRENDA team
Malachium aquaticum
-
-
-
Manually annotated by BRENDA team
catalytic subunit
UniProt
Manually annotated by BRENDA team
catalytic subunit ilvB1
UniProt
Manually annotated by BRENDA team
catalytic subunit ilvB2
UniProt
Manually annotated by BRENDA team
catalytic subunit ilvG
UniProt
Manually annotated by BRENDA team
catalytic subunit ilvX
UniProt
Manually annotated by BRENDA team
regulatory subunit
-
-
Manually annotated by BRENDA team
wild-type strain H37Rv, ATCC 27294
-
-
Manually annotated by BRENDA team
catalytic subunit
UniProt
Manually annotated by BRENDA team
catalytic subunit ilvB1
UniProt
Manually annotated by BRENDA team
catalytic subunit ilvG
UniProt
Manually annotated by BRENDA team
small subunit
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
; var. Kinmaze
UniProt
Manually annotated by BRENDA team
var. japonica, strain Taichung 65
UniProt
Manually annotated by BRENDA team
catalytic subunit
UniProt
Manually annotated by BRENDA team
catalytic subunit
UniProt
Manually annotated by BRENDA team
catalytic aubunit
UniProt
Manually annotated by BRENDA team
expression of both small and catalytic subunit in Escherichia coli
-
-
Manually annotated by BRENDA team
petite mutant
-
-
Manually annotated by BRENDA team
3 isoenzymes: I, II, and III; isoenzyme I and II are expressed in wild type cells, isoenzyme III is cryptic
-
-
Manually annotated by BRENDA team
isoenzyme II, recombinantly produced in Escherichia coli HB101/pDU9
-
-
Manually annotated by BRENDA team
a sulfonylurea-resistant biotype, isozyme ALS1
UniProt
Manually annotated by BRENDA team
a sulfonylurea-resistant biotype, isozyme ALS2
UniProt
Manually annotated by BRENDA team
collected in Daisen, Japan
-
-
Manually annotated by BRENDA team
Roxb. var. ohwianus T. Koyama, sulfonylurea-resistant and sulfonylurea-susceptible biotype
-
-
Manually annotated by BRENDA team
sulfonylurea-resistant biotypes collected from Nakafurano, Shiwa, Matsuyama, and Yurihonjyo in Japan, isozyme ALS1; sulfonylurea-resistant biotypes collected from Nakafurano, Shiwa, Matsuyama, and Yurihonjyo in Japan, isozyme ALS2
-
-
Manually annotated by BRENDA team
ATCC 25419
-
-
Manually annotated by BRENDA team
catalytic subunit ilvB
UniProt
Manually annotated by BRENDA team
small subunit, expression in Escherichia coli
Swissprot
Manually annotated by BRENDA team
strain PCC6803, enzyme sll1981, ORF sll1981, an acetolactate synthase homologue
-
-
Manually annotated by BRENDA team
Synechocystis sp. PCC6803
strain PCC6803, enzyme sll1981, ORF sll1981, an acetolactate synthase homologue
-
-
Manually annotated by BRENDA team
black mexican sweet, two enzyme forms: AHAS I and AHAS II
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
complete inactivation of the acetolactate synthase in Corynebacterium glutamicum DM1729 and DM1933 by deletion of the ilvB gene, encoding the catalytic subunit, leads to L-valine, L-isoleucine, and L-leucine auxotrophy and to improved L-lysine production
physiological function
-
deletion of gene ilv2 encoding acetolactate synthase results in loss of viability during isoleucine and valine starvation due to 2-oxobutanoate accumulation. Rapamycin further decreases vialbility of the mutant. Recovery from starvation is influenced by the carbon source present during recovery
physiological function
-
deletion of gene ilv2 encoding acetolactate synthase results in significant attenuation of virulence and a grater than 100fold reduction in viability after only four hours of isoleucine and valine starvation due to 2-oxobutanoate accumulation. Rapamycin increases vialbility of both ilv1 and ilv2 mutants. Recovery from starvation is influenced by the carbon source present during starvation
physiological function
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
P9WG41
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
Q6K2E8
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
O06335, O53554, P9WG39, P9WG41
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
G0ZSE6
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
acetohydroxyacid synthase is the enzyme that catalyses the first step in the common pathway of the biosynthesis of the branched chain amino acids, valine, leucine and isoleucine
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
P45261
AHAS catalyzes the first common step in the biosynthetic pathway of the branched-amino acids leucine, isoleucine, and valine
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
P45261
condensation reaction
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
60fold higher specificity for 2-ketobutyrate over pyruvate as acceptor
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
O06335, O53554, P9WG39, P9WG41
catalytic subunit ilvG shows positive cooperativity towards substrate and cofactors
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
P9WG39, P9WG41
catalytic subunit ilvG shows positive cooperativity towards substrate and cofactors
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
P9WG41
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
P9WG39, P9WG41
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
G0ZSE6
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
Haloferax volcanii DSM 3757
-
-
-
-
?
2-oxobutanoate + lactylthiamine diphosphate
acetohydroxybutanoate + ?
show the reaction diagram
-
-
-
-
2-oxobutanoate + pyruvate
2-hydroxy-2-methyl-3-oxopentanoate + CO2
show the reaction diagram
-
-
-
-
?
2-oxobutanoate + pyruvate
2-hydroxy-2-methyl-3-oxopentanoate + CO2
show the reaction diagram
-
-
-
-
?
2-oxobutanoate + pyruvate
2-hydroxy-2-methyl-3-oxopentanoate + CO2
show the reaction diagram
-
-
-
-
?
2-oxobutanoate + pyruvate
2-hydroxy-2-methyl-3-oxopentanoate + CO2
show the reaction diagram
-
60fold higher specificity for 2-ketobutyrate over pyruvate as acceptor
-
-
?
2-oxobutanoate + pyruvate
2-propionyl-2-hydroxybutanoate + ?
show the reaction diagram
-
reaction catalyzed by mutant V375A
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
r
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
r
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
first committed step in the biosynthesis of valine and leucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
first step in the biosynthesis of valine, overview
-
-
r
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
r
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine, overview
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine, regulation, overview
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
Enterobacter aerogenes 01. Dez
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
first committed step in the biosynthesis of valine and leucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
Leuconostoc lactis NCW1
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
Leuconostoc lactis NCW1
-
-
-
-
?
pyruvate
?
show the reaction diagram
-
-
-
-
-
pyruvate
?
show the reaction diagram
-
-
-
-
-
pyruvate
?
show the reaction diagram
-
-
-
-
-
pyruvate
?
show the reaction diagram
-
isoenzyme II is regulated by Leu, Ile and Val
-
-
-
pyruvate
?
show the reaction diagram
-
isoenzyme II is regulated by Leu
-
-
-
pyruvate
?
show the reaction diagram
-
the enzyme plays a role in not only preventing intracellular acidification but also supplying alpha-acetolactate as an intermediate of branched chain amino acids biosynthesis
-
-
-
pyruvate
?
show the reaction diagram
-
production of isoenzyme AHS I is under multivalent control by Val and Leu, production of isoenzyme AHS II is under multivalent control by Ile, Val and Leu
-
-
-
pyruvate
?
show the reaction diagram
-
isoenzyme AHAS I enables a bacterium to cope with poor carbon sources, which lead to low endogenous pyruvate concentrations
-
-
-
pyruvate
?
show the reaction diagram
-
constitutive high expression, the enzyme is active only under conditions of pyruvate excess
-
-
-
pyruvate
?
show the reaction diagram
-
the expression is negatively controlled by Val. Leu and Ile slightly stimulate the enzyme production
-
-
-
pyruvate
?
show the reaction diagram
-
catabolic enzyme is involved in 2,3-butanediol pathway
-
-
-
pyruvate
?
show the reaction diagram
-
catabolic enzyme is involved in 2,3-butanediol pathway
-
-
-
pyruvate
?
show the reaction diagram
-
key enzyme in synthesis of branched-chain amino acids
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
isoenzyme I is regulated by Leu and Val
-
-
-
pyruvate
(S)-2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
(S)-2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
(S)-2-acetolactate + CO2
show the reaction diagram
-
stereospecific reaction
-
-
?
pyruvate
(S)-2-acetolactate + CO2
show the reaction diagram
P07342
stereospecific reaction
-
-
?
pyruvate
(S)-2-acetolactate + CO2
show the reaction diagram
-
the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview
-
-
?
pyruvate
(S)-2-acetolactate + CO2
show the reaction diagram
P07342
the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview
-
-
?
pyruvate + 2-ketobutyrate
2-aceto-2-hydroxybutyrate
show the reaction diagram
-
first committed step in the biosynthesis of isoleucine
-
-
?
pyruvate + 2-ketobutyrate
2-aceto-2-hydroxybutyrate
show the reaction diagram
-
first committed step in the biosynthesis of isoleucine
-
-
?
pyruvate + 2-ketobutyrate
acetohydroxybutyrate
show the reaction diagram
-
-
-
-
?
pyruvate + 2-oxobutanoate
acetohydroxybutanoate
show the reaction diagram
-
-
-
?
pyruvate + 2-oxobutanoate
acetohydroxybutanoate
show the reaction diagram
-
no activity
-
-
-
pyruvate + 2-oxobutanoate
acetohydroxybutanoate
show the reaction diagram
-
isoenzyme I shows no product preference, isoenzymes II and III form acetohydroxybutanoate at 180fold and 60fold faster rates, respectively than acetolactate
-
?
pyruvate + 2-oxobutanoate
acetohydroxybutanoate
show the reaction diagram
-
much higher affinity for 2-oxobutanoate than for pyruvate
-
?
pyruvate + 2-oxobutanoate
acetohydroxybutanoate
show the reaction diagram
-
preference for 2-ketobutanoate at the second substrate site
-
?
pyruvate + 2-oxobutyrate
(S)-acetohydroxybutyrate + CO2
show the reaction diagram
-
stereospecific reaction
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
-
stereospecific reaction
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
-
stereospecific reaction, benzaldehyde is an artificial substrate, especially of mutants of isozyme AHAS II residues Phe109, Met250, Arg276 and Trp464
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
-
stereospecific reaction, isozymes AHAS I and II
-
-
?
pyruvate + O2
peracetate + CO2
show the reaction diagram
-
isozymes AHAS II and AHAS III, oxygen-consuming side reaction
-
-
?
hydroxypyruvate
? + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
mechanism of expression regulation, overview
-
-
-
additional information
?
-
-
regulatory role of the proteins of the phosphoenolpyruvate:carbohydrate phosphotransferase system, requirement of the dephospho-form of enzyme IIANtr, encoded by gene ptsN, for derepression of Escherichia coli K-12 ilvBN expression, overview
-
-
-
additional information
?
-
-
the enzyme can act in anabolic or in catabolic function, the first enzyme contains the conserved motif 372RFDDR376, while the latter does not, the conserved motif 372RFDDR376 is a possible determinant of the FAD-dependent and herbicide-resistant properties of tobacco, overview
-
-
-
additional information
?
-
-
acetohydroxybutyrate is preferably formed, isozyme AHAS I can also form peracetate from synthetic acetolactate
-
-
-
additional information
?
-
-
sll1981 functions as L-myo-inositol 1-phosphate synthase, MIPS, EC 5.5.1.4, overview
-
-
-
additional information
?
-
-
substrate specificity ratios of isozymes I-III, substrate recognition mechanism, overview
-
-
-
additional information
?
-
Q6K2E8
acetolactate synthase is the first common enzyme in the biosynthetic pathway of branched-chain amino acids
-
-
-
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
-
additional information
?
-
Q42768
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
-
additional information
?
-
P07342
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
-
additional information
?
-
-
enzyme additionallly displays 2-ketoisovalerate decarboxylase activity
-
-
-
additional information
?
-
-
the specificity of AHAS for 2-ketoacids as acceptor substrates is due to an arginine residue which probably interacts with the carboxylate of the second substrate, e.g., Arg276 in AHAS II. Mutants altered at this arginine can utilize aromatic aldehydes as second substrate and form chiral arylacyl carbinols. Mechanistically, carboligation occurs after rate-determining formation of hydroxyethyl-thiamine diphosphate. A faster rate constant for product release when the alkyl group derived from the acceptor substrate is ethyl compared to methyl plays a major role in product specificity. The crucial role of a Trp residue, i.e. Trp 464 in AHAS II, in determining specificity may be due to control of a conformational change involved in product release rather than to affinity for 2-ketobutyrate
-
-
-
additional information
?
-
-
a valine and a phenylalanine residue hydrophobically interact with the methyl substituent of pyruvate. A mutation of either Val375 or Phe109 is detrimental for unimolecular catalytic steps in which tetrahedral intermediates are involved, such as substrate addition to the cofactor and product liberation. Val375 and Phe109 to not only conjointly mediate substrate binding and specificity but moreover to ensure a proper orientation of the donor substrate and intermediates for correct orbital alignment in multiple transition states
-
-
-
additional information
?
-
-
isozyme I is not specific for 2-oxobutanoate over pyruvate as an acceptor substrate. Residues Gln480 and Met476 in AHAS I replace the Trp and Leu residues conserved in other acetohydroxyacid synthases and lead to accelerated ligation and product release steps. This difference in kinetics accounts for the unique specificity, reversibility and allosteric response of AHAS I
-
-
-
additional information
?
-
-
residue Glu47 has a crucial catalytic role for it in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation. Either the transient oxyanion on the acceptor carbonyl is stabilized by H-bonding to the glutamine side chain, or carboligation involves glutamine tautomerization and the elementary reactions of addition and protonation occur in a concerted manner. Gln110 and Glu47 have global catalytic roles, being engaged in all major bond-breaking and bond-making steps. Lys159 has a minor effect on the kinetics and specificity of isoform AHAS II, far less than does Arg276,which influences the specificity for a 2-ketoacid as a second substrate. His251 has a large effect on donor substrate binding, but this effect masks any other effects of replacement of His251
-
-
-
additional information
?
-
Synechocystis sp. PCC6803
-
sll1981 functions as L-myo-inositol 1-phosphate synthase, MIPS, EC 5.5.1.4, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
Q6K2E8
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
acetohydroxyacid synthase is the enzyme that catalyses the first step in the common pathway of the biosynthesis of the branched chain amino acids, valine, leucine and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
first committed step in the biosynthesis of valine and leucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
first step in the biosynthesis of valine, overview
-
-
r
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
r
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine, overview
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine, regulation, overview
-
-
?
pyruvate
?
show the reaction diagram
-
-
-
-
-
pyruvate
?
show the reaction diagram
-
-
-
-
-
pyruvate
?
show the reaction diagram
-
-
-
-
-
pyruvate
?
show the reaction diagram
-
isoenzyme II is regulated by Leu, Ile and Val
-
-
-
pyruvate
?
show the reaction diagram
-
isoenzyme II is regulated by Leu
-
-
-
pyruvate
?
show the reaction diagram
-
the enzyme plays a role in not only preventing intracellular acidification but also supplying alpha-acetolactate as an intermediate of branched chain amino acids biosynthesis
-
-
-
pyruvate
?
show the reaction diagram
-
production of isoenzyme AHS I is under multivalent control by Val and Leu, production of isoenzyme AHS II is under multivalent control by Ile, Val and Leu
-
-
-
pyruvate
?
show the reaction diagram
-
isoenzyme AHAS I enables a bacterium to cope with poor carbon sources, which lead to low endogenous pyruvate concentrations
-
-
-
pyruvate
?
show the reaction diagram
-
constitutive high expression, the enzyme is active only under conditions of pyruvate excess
-
-
-
pyruvate
?
show the reaction diagram
-
the expression is negatively controlled by Val. Leu and Ile slightly stimulate the enzyme production
-
-
-
pyruvate
?
show the reaction diagram
-
catabolic enzyme is involved in 2,3-butanediol pathway
-
-
-
pyruvate
?
show the reaction diagram
-
catabolic enzyme is involved in 2,3-butanediol pathway
-
-
-
pyruvate
?
show the reaction diagram
-
key enzyme in synthesis of branched-chain amino acids
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
-
pyruvate
?
show the reaction diagram
-
isoenzyme I is regulated by Leu and Val
-
-
-
pyruvate
(S)-2-acetolactate + CO2
show the reaction diagram
-
the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview
-
-
?
pyruvate
(S)-2-acetolactate + CO2
show the reaction diagram
P07342
the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
first committed step in the biosynthesis of valine and leucine
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate + 2-ketobutyrate
2-aceto-2-hydroxybutyrate
show the reaction diagram
-
first committed step in the biosynthesis of isoleucine
-
-
?
pyruvate + 2-ketobutyrate
acetohydroxybutyrate
show the reaction diagram
-
-
-
-
?
pyruvate + 2-ketobutyrate
2-aceto-2-hydroxybutyrate
show the reaction diagram
-
first committed step in the biosynthesis of isoleucine
-
-
?
pyruvate + 2-oxobutyrate
(S)-acetohydroxybutyrate + CO2
show the reaction diagram
-
stereospecific reaction
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
P45261
AHAS catalyzes the first common step in the biosynthetic pathway of the branched-amino acids leucine, isoleucine, and valine
-
-
?
additional information
?
-
-
mechanism of expression regulation, overview
-
-
-
additional information
?
-
-
regulatory role of the proteins of the phosphoenolpyruvate:carbohydrate phosphotransferase system, requirement of the dephospho-form of enzyme IIANtr, encoded by gene ptsN, for derepression of Escherichia coli K-12 ilvBN expression, overview
-
-
-
additional information
?
-
-
the enzyme can act in anabolic or in catabolic function, the first enzyme contains the conserved motif 372RFDDR376, while the latter does not, the conserved motif 372RFDDR376 is a possible determinant of the FAD-dependent and herbicide-resistant properties of tobacco, overview
-
-
-
additional information
?
-
Q6K2E8
acetolactate synthase is the first common enzyme in the biosynthetic pathway of branched-chain amino acids
-
-
-
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
-
additional information
?
-
Q42768
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
-
additional information
?
-
P07342
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
activates
FAD
-
0.005 mM, 35-40% enhancement of activity
FAD
-
contains bound FAD, 0.88 mol per mol of protomer of 69000 Da
FAD
-
absolutly required for isoenzyme I and II, no requirement for isoenzyme III
FAD
-
partial requirement for isoenzyme III
FAD
-
Km: 0.0003 mM; required
FAD
-
Km: 0.00016 mM for isoenzyme I; required by isoenzyme I, no requirement by isoenzyme III
FAD
-
no stimulation
FAD
-
no requirement
FAD
-
required
FAD
-
required as cofactor
FAD
-
no requirement
FAD
-
Km: 0.0003 mM; required
FAD
-
Km: 0.0004 mM
FAD
-
required
FAD
-
required for the enzyme in anabolic function, but not in catabolic function, the conserved motif 372RFDDR376 is a possible determinant of the FAD-dependent and herbicide-resistant properties of tobacco, overview
FAD
-
residues W573 is structurally important for FAD binding
FAD
-
the flavin plays a crucial role in the structural integrity, and is reduced in the course of catalysis as a result of an internal redox side reaction
FAD
P45261
dependent on
FAD
-
the secondary structure of the FAD binding domain of large subunit ilvB is similar to the structure of this domain in the catalytic subunit of yeast AHAS. The regulatory subunit ilvN interacts with ilvBalpha and ilvBbeta domains of the catalytic subunit and not with the ilvBgamma domain. ilvN binds close to the FAD binding site in ilvBbeta and proximal to the intrasubunit ilvBalpha/ilvBbeta domain interface
FAD
Q6K2E8
-
FAD
-
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview
FAD
-
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes
FAD
Q42768
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview
FAD
-
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview
FAD
-
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes
FAD
P07342
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes
FAD
-
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes
FAD
-
Km value 0.061 microM
FAD
G0ZSE6
Km value 0.00033 mM
riboflavin
-
plus 10 mM phosphate, stimulates
thiamine diphosphate
-
required as cofactor; saturated at 0.5 mM thiamine diphosphate
thiamine diphosphate
-
required after dialysis; required as cofactor
thiamine diphosphate
-
Km: 0.0033 mM; required after dialysis; required as cofactor
thiamine diphosphate
-
Km: 0.0031 mM; required after dialysis; required as cofactor
thiamine diphosphate
-
required as cofactor
thiamine diphosphate
-
Km: 0.0015 mM; required as cofactor
thiamine diphosphate
-
Km: 0.0012 mM; required as cofactor
thiamine diphosphate
-
-
thiamine diphosphate
-
Km: 0.0087 mM for isoenzyme I, 0.026 mM for isoenzyme III; required as cofactor
thiamine diphosphate
-
stimulates
thiamine diphosphate
-
required as cofactor
thiamine diphosphate
-
required as cofactor
thiamine diphosphate
-
required as cofactor
thiamine diphosphate
-
required as cofactor
thiamine diphosphate
-
Km: 0.0012 mM; required as cofactor
thiamine diphosphate
-
Km: 0.11 mM; required as cofactor
thiamine diphosphate
-
Km: 0.0016; required as cofactor
thiamine diphosphate
-
Km: 0.0032 mM; required as cofactor
thiamine diphosphate
-
-
thiamine diphosphate
-
dependent on
thiamine diphosphate
-
-
thiamine diphosphate
-
-
thiamine diphosphate
-
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
thiamine diphosphate
-
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
thiamine diphosphate
-
binding kinetics
thiamine diphosphate
-
-
thiamine diphosphate
P45261
dependent on
thiamine diphosphate
-
-
thiamine diphosphate
-
-
thiamine diphosphate
Q6K2E8
-
thiamine diphosphate
-
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
Q42768
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
-
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
P07342
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
-
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
-
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
thiamine diphosphate
-
Km value 0.2 mM
thiamine diphosphate
G0ZSE6
Km value 0.0092 mM
thiamine diphosphate
P9WG41
Km value 0.027 mM; Km value 0.036 mM
thiamine diphosphate
O06335, O53554, P9WG39, P9WG41
Ks value 0.042 mM; Ks value 0.042 mM
thiamine diphosphate
-
required cofactor, apparent Km: 0.0088 mM
FMN
-
stimulates, Km: 0.0013 mM
additional information
-
spectral analysis and kinetics of cofactor binding, overview
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
stimulates
K+
-
mutant D428N, Km-value 19 mM, mutant D428E, Km-value 35 mM
KCl
-
maximal activity required KCl concentrations of greater than 3.5 M
Mg2+
-
saturated at 1 mM MgCl2
Mg2+
-
strong requirement
Mg2+
-
Km: 0.06 mM; required
Mg2+
-
Km: 1.01 mM; required
Mg2+
-
Km: 0.3 mM for isoenzyme I, 0.4 mM for isoenzyme III; required
Mg2+
-
required; stimulates
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
required
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
Km: 0.28 mM; required
Mg2+
-
Km: 0.3 mM MgCl2; Mn2+ or Mg2+ required
Mg2+
-
required
Mg2+
-
wild-type, Km-value 0.01 mM, mutant D428N, Km-value 0.21 mM, mutant D428E, Km-value 0.36 mM
Mg2+
-
required
Mg2+
-
required, spectral analysis and kinetics of Mg2+ binding, overview
Mg2+
-
a divalent metal ion is required
Mg2+
-
the enzyme requires a divalent metal ion
Mg2+
-
activates, binding structure at the regulatory subunit
Mg2+
-
K0.5 is 1.160 mM
Mg2+
P37251
-
Mg2+
Q6K2E8
-
Mg2+
-
the enzyme requires a divalent metal ion, involved in anchoring the cofactor thiamine diphosphate in the active site
Mg2+
-
the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site
Mg2+
Q42768
the enzyme requires a divalent metal ion
Mg2+
-
the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site
Mg2+
P07342
the enzyme requires a divalent metal ion
Mg2+
-
the enzyme requires a divalent metal ion
Mg2+
-
the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site
Mg2+
-
Km value 1.26 mM
Mg2+
G0ZSE6
Km value 0.00012 mM
Mg2+
O06335, O53554, P9WG39, P9WG41
Ks value 0.183 mM; Ks value 0.183 mM
Mg2+
-
Mg2 is probably the natural cofactor of the enzyme. Halofgerax volcanii is thought to contain a high intracellular Mg2+ concentration, as its native habitat, the Dead Sea, contains 1.4 M MgCl2. The endogenous metal is apparently tightly-enough bound so that added Mg2+ does not stimulate the activity
MgATP2-
-
activates
Mn2+
-
can substitute for Mg2+
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
stimulates
Mn2+
-
Km: 0.016 mM MnCl2; Mn2+ or Mg2+ required
Mn2+
-
the enzyme requires a divalent metal ion
Mn2+
-
the activity is about 133% for Mn2+ as compared to Mg2+
NaCl
-
while raising the NaCl concentration from 1.5 to 3.5 M leads to an increase in enzyme activity, this increase is 3fold lower than that detected in the presence of optimal KCl levels
Ni2+
-
stimulates
Ni2+
-
the activity is about 50% for Ni2+ as compared to Mg2+
Zn2+
-
stimulates
Mn2+
-
activates, high concentrations inhibit
additional information
-
the enzyme does not require a divalent cation for activity
additional information
-
no effect: Mg2+
additional information
-
no effect: Mn2+, Mg2+, Ca2+
additional information
-
AHASII is active in the presence of Mn2+, Mg2+, Ca2+, Cd2+, Co2+, Zn2+, Cu2+, Al3+, Ba2+ or Ni2+, the activity is about 50% for Ni2+ and 133% for Mn2+ as compared to Mg2+
additional information
-
a divalent ion is required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-3,3'-dioxo-1,1',3,3'-tetrahydro-2,2'-biindole-5,5'-disulfonate
-
inhibition profile and inhibition of root growth, overview
(5-bromo-2-[[([2-[(2-chloroethoxy)methyl]phenyl]sulfonyl)carbamoyl]amino]pyrimidin-4-yl)methyl benzoate
-
-
(5-bromo-2-[[([2-[(2-chloroethoxy)methyl]phenyl]sulfonyl)carbamoyl]amino]pyrimidin-4-yl)methyl phenylacetate
-
-
(5-bromo-2-[[([2-[(2-chloroethoxy)methyl]phenyl]sulfonyl)carbamoyl]amino]pyrimidin-4-yl)methyl prop-2-enoate
-
-
1-(4,6-dimethoxypyrimidin-2-yl)-5-methoxymethyl-N-(2-isopropyl-6-nitrophenyl)-1H-1,2,4-triazole-3-sulfonamide
-
-
1-(4,6-dimethoxypyrimidin-2-yl)-5-methyl-N-(2-isopropyl-6-nitrophenyl)-1H-1,2,4-triazole-3-sulfonamide
-
-
1-(4,6-dimethoxypyrimidin-2-yl)-5-methylthio-N-(2-chloro-6-fluorophenyl)-1H-1,2,4-triazole-3-sulfonamide
-
-
1-(4-chloro-6-methoxypyrimidin-2-yl)-5-methoxy-N-(2-methyl-6-nitrophenyl)-1H-1,2,4-triazole-3-sulfonamide
-
-
2,3-dichloro-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
2-(1,1-dihydroxyethyl)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
2-(2-bromobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
-
2-(2-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
-
2-(2-chloroethoxy)-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-(2-chloroethoxy)-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-(3-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
-
2-(4-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
-
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
wild-type, 50% inhibition at 0.00318 mM, mutant C411S, 50% inhibition at 0.00426 mM, mutant C607S, 50% inhibition at 0.00099 mM
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
-
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
i.e. Cadre
2-(difluoromethoxy)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
2-acetyl-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
2-acetyl-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
-
2-amino-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
2-bromo-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
2-bromo-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
-
2-bromopyruvate
-
-
2-butoxy-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
2-butyl-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
-
2-chloro-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
2-chloro-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
-
2-chloro-N-([4-(methylamino)-6-[(1-methylethyl)sulfanyl]-1,3,5-triazin-2-yl]carbamoyl)benzenesulfonamide
-
-
2-chloro-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[[4-(ethylsulfanyl)-6-(methylamino)-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[[4-(ethylsulfanyl)-6-methoxy-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[[4-(ethylsulfanyl)-6-methylpyrimidin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[[4-(methylamino)-6-(methylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[[4-methoxy-6-(methylsulfanyl)pyrimidin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[[4-methoxy-6-(propylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[[4-methyl-6-(propylsulfanyl)pyrimidin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-oxobutanoate
-
inhibits formation of acetolactate from pyruvate
2-oxobutanoate
-
isoenzyme I has lower sensitivity to inhibition than isoenzyme III
2-oxobutanoate
-
-
2-substituted-8-(4,6-dimethoxypyrimidin-2-yloxy)-4-methylphthalazin-1-one derivatives
-
synthesis of diverse derivatives and inhibitory potency, overview
-
2-[(2-chloroethoxy)methyl]-N-[(4-chloropyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-[(2-chloroethoxy)methyl]-N-[(4-methylpyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3-fluorobenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3-methylbenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-(methylsulfanyl)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-ethylbenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-ethynylbenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-fluorobenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-hydroxybenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-iodobenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methoxybenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-nitrobenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(1-methylethoxy)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(1H-pyrrol-1-yl)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(ethylsulfanyl)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(methylsulfanyl)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(methylsulfonyl)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(phenylcarbonyl)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(propylsulfanyl)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(trifluoromethoxy)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-ethoxybenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-ethylbenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-fluorobenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-iodobenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-methoxybenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-methylbenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-nitrobenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-phenoxybenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-propoxybenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-propylbenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(1-methylethoxy)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(ethylsulfanyl)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(methylsulfanyl)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(phenylcarbonyl)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(propylsulfanyl)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(trifluoromethyl)benzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-ethoxybenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-fluorobenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-iodobenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-methoxybenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-methylbenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-nitrobenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-phenoxybenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-propoxybenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
-
2-[[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]-N,N-dimethylbenzamide
-
-
3-(7H-cyclopenta[b]pyridin-5-yl)-N-[(2-nitrophenyl)sulfanyl]alanine
-
inhibition profile and inhibition of root growth, overview
3-Bromopyruvate
-
competitive to 2-oxobutanoate
3-phosphoglycerate
-
noncompetitive
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]biphenyl-2-carboxylic acid
-
-
4-(cyclopropylcarbonyl)-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-1-methyl-1H-pyrazole-5-sulfonamide
-
i.e. K13030
4-acetyl-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-1-methyl-1H-pyrazole-5-sulfonamide
-
i.e. K13010
5-amino-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
5-benzyl-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
5-bromo-2-([[(2-chlorophenyl)sulfonyl]carbamoyl]amino)pyrimidin-4-yl benzoate
-
-
5-bromo-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
5-chloro-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
5-cyano-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
6,6'-disulfanediyldipyridine-3-carboxylic acid
-
inhibition profile and inhibition of root growth, overview
8-(4,6-dimethoxypyrimidin-2-yloxy)-4-methylphthalazin-1(2H)-one
-
-
8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
-
Ag+
-
0.1 mM, 98% residual activity
ATP
-
noncompetitive
AVS-2087
P45261
-
bensulfuron-methyl
Q6K2E8
a sulfonylurea herbicide; mutant W548L/S627I, 22% inhibition at 0.1 nM
benzaldehyde
-
inhibits isozyme AHAS II, not isozyme AHAS I
bispyribac-sodium
Q6K2E8
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; a pyrimidinylcarboxylate herbicide
bispyribac-sodium
Q6K2E8
a pyrimidinyl carboxy herbicide
bispyribacsodium
-
-
branched-chain amino acids
-
feedback inhibition, differential inhibition of isozymes, overview
-
Cadre
-
imidazolinone
Cadre
-
an imidazole herbicide, no inhibition of mutant R372S/F373P/D374V/D375E/R376Y
Cadre
-
an imidazole herbicide, wild-type enzyme IC50: 0.0041 mM
Cadre
-
an imidazolinone herbicide
Cadre
-
imidazolinone inhibitor
chlorimuron ethyl
-
-
chlorimuron ethyl
-
a sulfonylurea herbicide
chlorimuron ethyl
-
IC50: 0.009 mM, over 80% inhibition at 0.04 mM
chlorimuron ethyl
-
-
chlorimuron ethyl
-
a sulfonylurea herbicide, complex inhibition, binding structure, overview
chlorimuron ethyl
-
a sulfonylurea herbicide, complex inhibition, overview
chlorimuron ethyl
Q42768
a sulfonylurea herbicide, complex inhibition, overview
chlorimuron ethyl
-
a sulfonylurea herbicide, complex inhibition, overview
chlorimuron-ethyl
-
binding conformation
chlorimuronethyl
-
noncompetitive, lowest total interaction energy and highest MolDock score of 140054 kcal/mol and -141.52, respectively, of the compounds analyzed
chlorsulfuron
Q6K2E8
; a sulfonylurea herbicide
chlorsulfuron
Q42768
-
chlorsulphuron
-
-
chlorsulphuron
-
-
chlorsulphuron
-
-
chlorsulphuron
-
-
chlorsulphuron
-
inhibition of the enzyme from Arabidopsis thaliana and of the enzyme expressed in E. coli
Co2+
-
0.1 mM, 44% residual activity
EDTA
-
20 mM, no residual activity
EDTA
-
dialysis against EDTA leads to an irreversible loss of activity
ethyl 2-([(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl)benzoate
-
compound binds within a pocket of the enzyme formed by amino acid residues Met351, Asp375, Arg377, Gly509, Met570 and Val571
ethyl 2-([(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl)benzoate
-
compound binds within a pocket of the enzyme formed by amino acid residues Met351, Asp375, Arg377, Gly509, Met570 and Val571
ethyl 2-([[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
ethyl 2-([[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
ethyl 2-([[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
ethyl 2-[(pyrimidin-2-ylcarbamoyl)sulfamoyl]benzoate
-
-
ethyl 2-[([4-[(acryloyloxy)methyl]-5-bromopyrimidin-2-yl]carbamoyl)sulfamoyl]benzoate
-
-
ethyl 2-[[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(4,6-dimethylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(4-chloro-6-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(5-bromo-4,6-dimethylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(5-bromo-4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
FAD
-
0.01 mM, 92% inhibition
flucarbazone
-
-
flumetsulam
G0ZSE6
herbicide-resistant enzyme variant from Pseudomonas sp. Lm10 shows 6.5fold higher resistance than the sensitive variant from Pseudomonas putida KT2440
-
glyoxylate
-
isozyme AHAS II
Hg2+
-
0.1 mM, 43% residual activity
Hydroxypyruvate
-
progressive inactivation of enzyme with kinetics of suicide inhibition, mechanism
Ile
-
enzyme form AHS I is inhibited. Enzyme form AHS II is not inhibited
Ile
-
no inhibition
Ile
-
5 mM, 32% inhibition
Ile
-
mild inhibition of isoenzyme I and III
Ile
-
inhibition of isoenzyme I, no inhibition of isoenzyme II
Ile
-
less potent, noncompetitive
Ile
-
isoenzyme AHS I is sensitive to feed-back inhibition, isoenzyme AHS II is insensitive
Ile
-
insensitive to
Ile
-
no inhibition
Ile
-
slight
Ile
-
1 mM, 50% inhibition
imazapyr
-
enzyme form AHS I and AHS II
imazapyr
-
slow, tight-binding inhibitor
imazapyr
-
-
imazapyr
-
-
imazapyr
-
an imidazolinone herbicide
imazapyr
-
i.e. 2-(4-isopropyl-4-methyl-5-oxo-2-imidazolin-2-yl)nicotinic acid
imazapyr
-
-
imazapyr
Q6K2E8
an imidazolinon herbicide; mutant W548L/S627I, 27% inhibition at 0.1 nM
imazapyr
-
an imidazolinone herbicide, complex inhibition, overview
imazapyr
Q42768
an imidazolinone herbicide, complex inhibition, overview
imazapyr
-
an imidazolinone herbicide, complex inhibition, overview
imazapyr
-
a imidazolinone herbicide, complex inhibition, overview
imazaquin
-
-
imazaquin
-
1 mM, 50% inhibition
imazaquin
-
uncompetitive
imazaquin
Q6K2E8
; an imidazolinon herbicide
imazaquin
-
an imidazolinone herbicide, complex inhibition, binding structure, overview
imazaquin
-
an imidazolinone herbicide, complex inhibition, overview
imazaquin
Q42768
an imidazolinone herbicide, complex inhibition, overview
imazaquin
-
an imidazolinone herbicide, complex inhibition, overview
imazaquin
-
a imidazolinone herbicide, complex inhibition, overview
imazaquinammonium
-
-
imazethapyr
-
-
imazethapyr
-
-
imazethapyr
G0ZSE6
herbicide-resistant enzyme variant from Pseudomonas sp. Lm10 shows 12.6fold higher resistance than the sensitive variant from Pseudomonas putida KT2440
imazosulfuron
-
sulfonylurea-resistant biotype, 50% inhibition above 3000 nM, sulfonylurea-susceptible biotype, 50% inhibition at 15 nM
imazosulfuron
Q6K2E8
; a sulfonylurea herbicide
imidazolinone
-
-
imidazolinones
-
potent
imidazolinones
-
the imidazolinones behave as non-competitive or uncompetitive inhibitors
Isoleucine
-
1 mM, about 90% residual activity in both sulfonylurea-susceptible and sulfonylurea-resistant biotype
Isoleucine
-
feedback inhibition of wild-type enzyme about 50% at 10 mM, M8 and M13 mutants are resistant
KHG20612
-
inhibition kinetics and antimycobacterial activity, overview
KHG20612
P45261
-
KIH-6127
-
i.e. pyriminobac-methyl
KSW30191
P45261
-
L-2-aminobutanoate
-
5 mM, 21% inhibition
L-isoleucine
P9WG41
-
L-isoleucine
-
weakly
L-leucine
P9WG41
-
L-Thr
-
5 mM, 6.6% inhibition
L-valine
-
not inhibitory for catalytic subunit alone, inhibitory for catalytic subunit plus small subunit
L-valine
G0ZSE6
-
L-valine
-
inhibits to a maximal activity of approximately 50% at concentrations higher than 0.5 mM
Leu
-
enzyme form AHS I is inhibited. Enzyme form AHS II is not inhibited
Leu
-
no inhibition
Leu
-
no inhibition
Leu
-
cooperative effect with Val
Leu
-
mixed noncompetitive inhibition of isoenzyme, pH-independent inhibition of isoenzyme III
Leu
-
5 mM, 23% inhibition
Leu
-
no inhibition of isoenzyme I and III
Leu
-
inhibition of isoenzyme I, no inhibition of isoenzyme II
Leu
-
no inhibition
Leu
-
isoenzyme AHS I is sensitive to feed-back inhibition, isoenzyme AHS II is insensitive
Leu
-
insensitive to
Leu
-
inhibition of the enzyme from Arabidopsis thaliana, no inhibition of the enzyme expressed in E. coli
Leu
-
no inhibition
Leu
-
1 mM, 50% inhibition
leucine
-
1 mM, about 50% residual activity in both sulfonylurea-susceptible and sulfonylurea-resistant biotype
leucine
-
feedback inhibition of wild-type enzyme about 50% at 10 mM, M8 and M13 mutants are resistant
leucine
Q42768
feedback inhibition
leucine
P07342
feedback inhibition
Londax
-
a sulfonylurea herbicide, no inhibition of mutant R372S/F373P/D374V/D375E/R376Y
Londax
-
a sulfonylurea herbicide, wild-type enzyme IC50: 0.013 mM
Londax
-
a sulfonylurea herbicide
methyl 2-([(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl)benzoate
P17597
-
methyl 2-([[4-(ethylsulfanyl)-6-methoxypyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[4-(methylamino)-6-(propylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[4-chloro-6-(methylamino)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[4-chloro-6-(methylsulfanyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[4-ethoxy-6-(methylamino)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[4-methoxy-6-(methylsulfanyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[4-methoxy-6-(propylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[5-bromo-4-(dibromomethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-[[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
methyl 2-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
methyl 2-[[(5-bromo-4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
metsulfuron methyl
-
IC50: 0.006 mM, over 80% inhibition at 0.04 mM
metsulfuron methyl
-
a sulfonylurea herbicide, complex inhibition, overview
metsulfuron methyl
Q42768
a sulfonylurea herbicide, complex inhibition, overview
metsulfuron methyl
-
a sulfonylurea herbicide, complex inhibition, overview
metsulfuron-methyl
-
-
metsulfuron-methyl
-
-
metsulfuron-methyl
G0ZSE6
herbicide-resistant enzyme variant from Pseudomonas sp. Lm10 shows 56fold higher resistance than the sensitive variant from Pseudomonas putida KT2440
metsulfuronmethyl
-
-
Mg2+
-
0.5 mM, 80% residual activity
Mn2+
-
0.5 mM, 28% residual activity
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
-
wild-type, 50% inhibition at 0.00262 mM, mutant C411S, 50% inhibition at 0.00668 mM, mutant C607S, 50% inhibition at 0.00887 mM
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
-
i.e. TP
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
-
-
N-([4-[(benzyloxy)methyl]-5-bromopyrimidin-2-yl]carbamoyl)-2-chlorobenzenesulfonamide
-
-
N-([5-bromo-4-[(prop-2-en-1-yloxy)methyl]pyrimidin-2-yl]carbamoyl)-2-(2-chloroethoxy)benzenesulfonamide
-
-
N-phthalyl anilide
-
and related compounds
-
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-(ethylsulfanyl)-6-(2-fluoro-1-hydroxyethyl)benzenesulfonamide
-
i.e. K12147
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
P17597
-
N-[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-chlorobenzenesulfonamide
-
-
N-[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[(5-bromo-4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[(5-bromo-4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[(5-bromo-4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-2-chlorobenzenesulfonamide
-
-
N-[(5-bromo-4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[(5-bromo-4-methoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[(5-bromo-4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[(5-bromopyrimidin-2-yl)carbamoyl]-2-chlorobenzenesulfonamide
-
-
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
ratio 1:1
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
ratio 1:1, i.e. Londax
N-[[5-bromo-4-(1-methylethoxy)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[[5-bromo-4-(dibromomethyl)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[[5-bromo-4-(dibromomethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[[5-bromo-4-(ethenyloxy)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]-2-chlorobenzenesulfonamide
-
-
N-[[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]-2-chlorobenzenesulfonamide
-
-
N-[[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[[5-bromo-4-(tribromomethyl)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
-
NADP+
-
0.01 mM, 63% inhibition
NADPH
-
0.01 mM, 100% inhibition
NC-311
-
sulfonylurea derivative, wild-type, 50% inhibition at 9.39 nM, mutant C411S, 50% inhibition at 16.83 nM, mutant C607S, 50% inhibition at 20.25 nM
NC-311
-
sulfonylurea inhibitor
nicosulfuron
-
-
phosphate
-
inhibits activity of enzyme assayed in acetate buffer
phosphoenolpyruvate
-
noncompetitive
primisulfuron methyl
-
IC50: 0.0042 mM, over 80% inhibition at 0.04 mM
primisulfuron-methyl
-
1 mM, 50% inhibition
propyl 4-(2-(4,6-dimethoxypyrimidin-2-yloxy)benzylamino)benzoate
-
i.e.ZJ0273
propyl 4-(2-(4,6-dimethoxypyrimidin-2-yloxy)benzylamino)benzoate
-
i.e. ZJ0273. Moderate susceptibility of plants
propyl 4-(2-(4,6-dimethoxypyrimidin-2-yloxy)benzylamino)benzoate
-
i.e. ZJ0273. ALS activity in vivo is hardly affected by ZJ0273 at 100 mg/l
propyl 4-(2-(4,6-dimethoxypyrimidin-2-yloxy)benzylamino)benzoate
-
i.e. ZJ0273. Decline of ALS activity and lower biomass production at a rate of 10 mg/l of ZJ0273
propyl 4-(2-(4,6-dimethoxypyrimidin-2-yloxy)benzylamino)benzoate
Malachium aquaticum
-
i.e. ZJ0273. Moderate susceptibility of plants
pyrazosulfuron ethyl
-
IC50: 87 nM, over 80% inhibition at 0.04 mM
pyrazosulfuron ethyl
-
IC50: 870 nM
pyrazosulfuron-ethyl
Q6K2E8
; a sulfonylurea herbicide
pyrazosulfuronethyl
-
-
pyriftalid
-
-
pyrimidylsalicylate
-
0.025 mM, 60% inhibition
-
pyriminobac
Q6K2E8
a pyrimidinylcarboxylate herbicide; mutant W548L/S627I, 13% inhibition at 0.1 nM
pyriminobac-methyl
G0ZSE6
herbicide-resistant enzyme variant from Pseudomonas sp. Lm10 shows 9.2fold higher resistance than the sensitive variant from Pseudomonas putida KT2440
-
pyrithiobac-sodium
Q6K2E8
a pyrimidinylcarboxylate herbicide; mutant W548L/S627I, 32% inhibition at 0.1 nM
SO42-
-
competitive when assayed in phosphate buffer, mixed type, when assayed in acetate buffer
Sodium acetate
-
-
Sodium formate
-
-
sodium propionate
-
-
sulfometuron methyl
-
IC50: 0.0048 mM, over 80% inhibition at 0.04 mM
sulfometuron methyl
P45261
-
sulfometuron methyl
-
the enzyme inhibitor shows activity against Mycobacterium tuberculosis both in vitro and in vivo
sulfometuron methyl
-
active against Mycobacterium tuberculosis both in vitro and in vivo
sulfometuron methyl
-
-
sulfometuron methyl
Q42768
-
sulfometuron methyl
-
-
sulfometuron methyl
-
-
sulfometuron methyl
-
-
sulfometuron-methyl
-
enzyme form AHS I and AHS II
sulfometuron-methyl
-
-
sulfometuron-methyl
-
2.5 mM, 50% inhibition
sulfometuronmethyl
-
-
sulfonylurea
-
potently inhibiting herbicide
sulfonylurea
-
the inhibition by sulfonylurea is non-competitive or nearly competitive with respect to pyruvate
thiamine thiazolone diphosphate
-
-
thifensulfuron-methyl
-
-
thifensulfuronmethyl
-
-
triasulfuron
-
21 out of 27 isolated bacteria in pure culture are inhibited by triasulfuron, the addition of isoleucine and/or valine reverses the effect in 19 cases
tribenuron methyl
Q42768
-
trisulfuron
-
1 mM, 50% inhibition
-
Val
-
enzyme form AHS I is inhibited. Enzyme form AHS II is not inhibited
Val
-
cooperative effective with Leu
Val
-
5 mM, 89% inhibition; feed-back inhibition; noncompetitive
Val
-
isoenzymes I and II are inhibited, isoenzyme II is not inhibited
Val
-
isoenzyme I and III inhibited
Val
-
competitive
Val
-
isoenzyme I is more resistant to inhibition than isoenzyme III
Val
-
competitive; feed-back inhibition
Val
-
feed-back inhibition; noncompetitive
Val
-
feed-back inhibition; noncompetitive
Val
-
noncompetitive; pH-dependent inhibition
Val
-
two enzyme forms: one is very sensitive to inhibition by Val, the second is not subject to feedback inhibition
Val
-
isoenzyme AHS I is sensitive to feed-back inhibition, isoenzyme AHS II is insensitive
Val
-
no inhibition
Val
-
inhibition of the enzyme from Arabidopsis thaliana, no inhibition of the enzyme expressed in E. coli
Val
-
no inhibition
Val
-
0.1 mM, 50% inhibition
valine
-
1 mM, about 70%% residual activity in sulfonylurea-susceptible and 80% in sulfonylurea-resistant biotype
valine
-
feedback inhibition of wild-type enzyme about 50% at 10 mM, M8 and M13 mutants are resistant
valine
-
isozyme AHAS I, feedback inhibition
valine
-
feedback inhibition, reversible by MgATP2-
valine
-
isozyme AHAS I, cooperative feedback inhibition
valine
-
binding site structure, inhibition mechanism
valine
Q42768
feedback inhibition
valine
P07342
feedback inhibition, the inhibition by valine is uniquely in fungi reversed by MgATP
[1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
a triazolopyrimidine derivative herbicide, no inhibition of mutant R372S/F373P/D374V/D375E/R376Y
[1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
a triazolopyrimidine derivative herbicide, wild-type enzyme IC50: 0.0293 mM
[5-bromo-2-[([[2-(1-methoxyethenyl)phenyl]sulfonyl]carbamoyl)amino]pyrimidin-4-yl]methyl prop-2-enoate
-
-
Mn2+
-
activates, high concentrations inhibit
additional information
-
no effect: Mg2+
-
additional information
-
no effect: Mn2+, Mg2+, Ca2+
-
additional information
-
inhibition kinetics or recombinant wild.type and reconstituted isozymes AHAS I
-
additional information
-
computational database screening for non-sulfonylurea inhibitors of AHAS, overview
-
additional information
-
mechanism and potency of enzyme inhibition by sulfonylurea herbicides, overview
-
additional information
-
isozyme AHAS II is not feedback inhibited
-
additional information
-
screening of chemical libraries for effective inhibitors of the enzyme, overview
-
additional information
-
IC50 values of herbicides with mutant enzymes, overview
-
additional information
-
the majority of soil bacteria contain only one functional acetohydroxyacid synthase enzyme sensitive to sulfonylurea herbicides
-
additional information
P45261
inhibitor library screening
-
additional information
-
AHAS from Bacillus anthracis shows strong resistance to three classes of herbicides, the sulfonylurea Londax, the imidazolinone Cadre, and the triazolopyrimidine TP
-
additional information
-
inhibitor synthesis, overview. Determination of ligand-receptor interaction and resistance mechanism in AHAS-sulfonylurea herbicide system, molecular modeling, overview
-
additional information
-
screening of 100 sulfonylurea analogues for antimycobacterial activity, minimal inhibitory concentrations, overview
-
additional information
-
molecular docking of inhibitor molecules to the enzyme crystal structure, 3D-QSAR modeling, overview
-
additional information
-
bulky substitutions in ortho-position of the sulfamoyl group in N-[(4-chloropyrimidin-2-yl)carbamoyl]benzenesulfonamide may enhance inhibitory activity. Negative charge distributed over a large surface area may enhance this activity. For better activity, the number of electronegative atoms present in the molecule should be high
-
additional information
-
ligand binding structures, and inhibition mechanism, overview
-
additional information
Q42768
ligand binding structures, and inhibition mechanism, overview
-
additional information
-
ligand binding structures, and inhibition mechanism, overview
-
additional information
-
leucine had negligible effect on the activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
stimulates
acetate
-
stimulates
acetate
-
increases activity
dithiothreitol
-
stimulates
ethanol
-
increases activity
NH4+
-
200 mM, 1.6fold stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
2-oxobutanoate
-
at 1.5 mM pyruvate
1.37
2-oxobutanoate
-
pH 7.5, 37C
5
2-oxobutanoate
-
at 2 mM pyruvate
5.6
2-oxobutanoate
-
wild-type, pH 7.3, 37C
6.9
2-oxobutanoate
-
mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37C
9.1
2-oxobutanoate
-
mutant V375A, pH 7.6, 37C
300
2-oxobutanoate
-
wild-type, pH 7.6, 37C
0.0117
pyruvate
-
wild-type enzyme
0.0289
pyruvate
-
mutant R372S/F373P/D374V/D375E
0.0757
pyruvate
-
mutant R372S/F373P/D374V/D375E/R376Y
0.33
pyruvate
-
mutant C83T, pH 7.6, 37C
0.5
pyruvate
-
-
1
pyruvate
-
pH 7.6, isoenzyme AHAS I
1.08
pyruvate
P9WG41
mutant F147R, pH 7.5, 37C
1.1
pyruvate
-
mutant Q487S, pH 7.0, 37C
1.18
pyruvate
P9WG41
wild-type, pH 7.5, 37C
1.2
pyruvate
-
mutant C83S, pH 7.6, 37C
1.3
pyruvate
-
isoenzyme I
1.38
pyruvate
-
mutant S539R, pH not specified in the publication, temperature not specified in the publication
1.5
pyruvate
-
mutant C83A, pH 7.6, 37C
1.56
pyruvate
-
pH 7.0, 37C, holoenzyme
1.6
pyruvate
-
mutant Q487G, pH 7.0, 37C
1.89
pyruvate
P9WG41
mutant L141A, pH 7.5, 37C
2.1
pyruvate
-
-
2.2
pyruvate
-
pH 7.0, 30C, sulfonylurea-resistant biotype
2.3
pyruvate
-
-
2.49
pyruvate
P9WG41
wild-type, pH 7.5, 37C
2.6
pyruvate
-
native protein
2.76
pyruvate
-
catalytic subunit
2.76
pyruvate
-
pH 7.0, 37C, catalytic subunit
2.9
pyruvate
-
fusion protein containing an N-terminal oligohistidine sequence on the large subunit
3
pyruvate
-
-
3.2
pyruvate
-
-
3.33
pyruvate
-
mutant S539A, pH not specified in the publication, temperature not specified in the publication
3.35
pyruvate
P9WG41
mutant L89A, pH 7.5, 37C
3.36
pyruvate
-
mutant S167A, pH not specified in the publication, temperature not specified in the publication
3.6
pyruvate
-
mutant D375E, pH 7.5, 37C
3.6
pyruvate
-
mutant L476M/Q480W, pH 7.6, 37C
3.66
pyruvate
-
pH 7.5, 37C
3.7
pyruvate
-
pH 7.0, 30C, sulfonylurea-susceptible biotype
3.89
pyruvate
P9WG41
mutant F147A, pH 7.5, 37C
3.93
pyruvate
-
-
4
pyruvate
-
37C, reconstituted, recombinant holoenzyme
4.15
pyruvate
-
pH 7.6, 37C
4.5
pyruvate
-
-
4.58
pyruvate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
4.7
pyruvate
-
mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37C
4.7
pyruvate
-
mutant Q480W, pH 7.6, 37C
4.8
pyruvate
-
37C, recombinant holoenzyme
4.8
pyruvate
-
pH 7.4, 37C, recombinant enzyme
4.8
pyruvate
-
wild-type, pH 7.6, 37C
4.94
pyruvate
P9WG41
mutant W516R, pH 7.5, 37C
5
pyruvate
-
AHAS I
5
pyruvate
-
-
5
pyruvate
-
wild-type, 37C, pH 7.6
5.2
pyruvate
-
wild-type, pH 7.6, 37C
5.5
pyruvate
-
-
5.7
pyruvate
-
mutant D374A, pH 7.5, 37C
5.8
pyruvate
P9WG41
mutant R101A, pH 7.5, 37C
6
pyruvate
-
wild-type with His-tag, pH 7.6, 37C
6.53
pyruvate
-
pH 7.5, 37C, recombinant wild-type enzyme
6.6
pyruvate
-
wild-type, pH 7.6, 37C
6.8
pyruvate
-
-
7
pyruvate
-
pH 7.6, isoenzyme AHAS III
7
pyruvate
-
enzyme form II
7
pyruvate
-
mutant D428N, 37C, pH 7.6
7.1
pyruvate
-
mutant E47A, pH 7.6, 37C
7.3
pyruvate
-
mutant E47Q, 37C, pH 7.6
7.3
pyruvate
-
mutant V375I, pH 7.6, 37C
7.6
pyruvate
-
isoenzyme III
7.7
pyruvate
-
mutant E47A, 37C, pH 7.6
7.7
pyruvate
-
mutant E47Q, pH 7.6, 37C
7.8
pyruvate
-
wild-type, pH 7.3, 37C
7.82
pyruvate
-
mutant S539F, pH not specified in the publication, temperature not specified in the publication
8
pyruvate
-
AHAS II
8
pyruvate
-
enzyme form I
8
pyruvate
-
30C, 120 ng protein in assay
8
pyruvate
-
mutant V477I, pH 7.6, 37C
8.01
pyruvate
-
Km-value of the first active site
8.36
pyruvate
-
mutant S506R, pH not specified in the publication, temperature not specified in the publication
8.7
pyruvate
-
mutant Q487A, pH 7.0, 37C
8.9
pyruvate
P9WG41
mutant S27A, pH 7.5, 37C
9.2
pyruvate
P45261
pH 7.5, 37C, recombinant enzyme
10
pyruvate
-
30C, 60 ng protein in assay
10
pyruvate
-
pH 7.0, 37C, isoform ALS I
10.54
pyruvate
-
mutant S506A, pH not specified in the publication, temperature not specified in the publication
10.6
pyruvate
-
pH 7.6, isoenzyme AHAS II
11
pyruvate
-
pH 7.0, 37C, isoform ALS II
11.2
pyruvate
-
mutant W464L with His-tag, pH 7.6, 37C
11.48
pyruvate
-
mutant S167R, pH not specified in the publication, temperature not specified in the publication
11.7
pyruvate
-
wild-type, pH 7.5, 37C
11.7
pyruvate
-
pH 7.5, wild-type enzyme
11.9
pyruvate
O06335, O53554, P9WG39, P9WG41
pH 7.5, 37C; pH 7.5, 37C
12.1
pyruvate
-
wild-type recombinant enzyme
13
pyruvate
-
-
13
pyruvate
-
mutant L476M, pH 7.6, 37C
13.6
pyruvate
-
wild-type, pH 7.0, 37C
13.68
pyruvate
-
mutant C607S, pH 7.5, 37C
13.71
pyruvate
-
mutant H392M, 37C, pH 7.5
13.8
pyruvate
-
mutant V375A, pH 7.6, 37C
15.05
pyruvate
-
wild-type, pH 7.5, 37C
16.09
pyruvate
-
wild-type, 37C, pH 7.5
17
pyruvate
-
-
17
pyruvate
-
-
17.06
pyruvate
-
wild-type, pH 7.5, 37C
17.3
pyruvate
-
mutant F109M, pH 7.6, 37C
17.5
pyruvate
G0ZSE6
pH 7.5, 37C
17.9
pyruvate
-
mutant V391A, pH 7.6, 37C
20
pyruvate
-
37C
21
pyruvate
-
mutant E60Q, pH 7.6, 37C
21.55
pyruvate
-
mutant C411S, pH 7.5, 37C
22.6
pyruvate
-
-
25.5
pyruvate
-
pH 7.5, 37C, in the presence of 3.5 M KCl
26
pyruvate
-
mutant M263A, pH 7.6, 37C
26.23
pyruvate
-
mutant K299Q pH 7.5, 37C
28
pyruvate
-
mutant E60A, pH 7.6, 37C
29.5
pyruvate
-
mutant Q110N, pH 7.6, 37C
30.2
pyruvate
-
mutant Q110A, pH 7.6, 37C
36
pyruvate
-
mutant D428E, 37C, pH 7.6
36
pyruvate
-
mutant M250A with His-tag, pH 7.6, 37C
38
pyruvate
-
mutant R276K with His-tag, pH 7.6, 37C
40.4
pyruvate
-
mutant Q110H pH 7.6, 37C
50
pyruvate
-
-
50
pyruvate
-
wild-type, pH 7.3, 37C, presence of 10 mM L-valine
50
pyruvate
-
mutant R289K, pH 7.6, 37C
54
pyruvate
-
wild-type, pH 7.3, 37C, presence of 10 mM L-isoleucine
55.8
pyruvate
-
mutant D374A/D375A, pH 7.5, 37C
65
pyruvate
-
wild-type, pH 7.3, 37C, presence of 10 mM L-leucine
70
pyruvate
-
pH 6.5, 37C
76.63
pyruvate
-
mutantH351F, 37C, pH 7.5
100
pyruvate
-
Km-value of the second active site
104
pyruvate
-
mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37C, presence of 10 mM L-isoleucine; mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37C, presence of 10 mM L-leucine; mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37C, presence of 10 mM L-valine
109.3
pyruvate
-
mutant D375A, pH 7.5, 37C
109.4
pyruvate
-
mutant K255F, pH 7.5, 37C
110.6
pyruvate
-
mutant Q110E, pH 7.6, 37C
113.9
pyruvate
-
pH 7.5, mutant R141K
115.5
pyruvate
-
mutant K255Q, pH 7.5, 37C
116.8
pyruvate
-
pH 7.5, mutant R141F
124
pyruvate
-
mutant R289Q, pH 7.6, 37C
148
pyruvate
-
pH 7.5, 37C, recombinant mutant W573F
167.4
pyruvate
-
pH 7.5, mutant R372F
266.7
pyruvate
-
mutant D374E/D375E, pH 7.5, 37C
287.8
pyruvate
-
mutant H351M, 37C, pH 7.5
337.3
pyruvate
-
pH 7.5, mutant R376K
475.9
pyruvate
-
pH 7.5, mutant R372K
557.6
pyruvate
-
mutant D374E, pH 7.5, 37C
959.5
pyruvate
-
mutant H351Q, 37C, pH 7.5
0.28
thiamine diphosphate
-
-
8.31
Hydroxypyruvate
-
-
additional information
additional information
-
non-hyperbolic substrate-saturation curve, involving interaction between the active sites of the dimer
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics or recombinant wild-type and reconstituted isozymes AHAS I, exclusive binding model
-
additional information
additional information
-
steady-state kinetics at different reaction conditions
-
additional information
additional information
-
cofactor affinities of wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetics of recombinant wild-type and mutant enzymes, cofactor binding parameters, overview
-
additional information
additional information
-
kinetics of isozymes
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.3
2-oxobutanoate
-
wild-type, pH 7.6, 37C
11.9
2-oxobutanoate
-
mutant V375A, pH 7.6, 37C
5.47
Hydroxypyruvate
-
-
0.028
pyruvate
-
mutant DELTA598, 37C, pH 7.4
0.097
pyruvate
-
mutant DELTA567-582, 37C, pH 7.4
0.104
pyruvate
-
mutant DELTA630, 37C, pH 7.4
0.4
pyruvate
-
mutant Q110E, pH 7.6, 37C
1.6
pyruvate
-
mutant E47Q, pH 7.6, 37C; mutant Q110H pH 7.6, 37C
2
pyruvate
-
mutant C83T, pH 7.6, 37C; mutant E60A, pH 7.6, 37C; mutant E60Q, pH 7.6, 37C
2.32
pyruvate
-
wild-type, 37C, pH 7.4
2.7
pyruvate
-
mutant E47A, pH 7.6, 37C; mutant Q110A, pH 7.6, 37C
3.03
pyruvate
-
mutant M250A with His-tag, pH 7.6, 37C
3.19
pyruvate
-
catalytic subunit
3.27
pyruvate
-
mutant R276K with His-tag, pH 7.6, 37C
3.9
pyruvate
-
mutant F109M, pH 7.6, 37C
5.4
pyruvate
-
pH 7.5, 37C, recombinant mutant W573F
5.8
pyruvate
-
mutant Q110N, pH 7.6, 37C
6
pyruvate
-
mutant R289Q, pH 7.6, 37C
8
pyruvate
-
mutant V391A, pH 7.6, 37C
9
pyruvate
-
mutant V477I, pH 7.6, 37C
9.6
pyruvate
-
mutant V375A, pH 7.6, 37C
11
pyruvate
-
mutant Q487G, pH 7.0, 37C; mutant Q487S, pH 7.0, 37C
13.9
pyruvate
-
mutant W464L with His-tag, pH 7.6, 37C
15
pyruvate
-
mutant Q480W, pH 7.6, 37C
16.1
pyruvate
-
pH 7.5, 37C, recombinant wild-type enzyme
19.8
pyruvate
-
wild-type with His-tag, pH 7.6, 37C
20
pyruvate
-
mutant C83A, pH 7.6, 37C
23
pyruvate
-
mutant C83S, pH 7.6, 37C
23.3
pyruvate
-
wild-type, pH 7.6, 37C
25
pyruvate
-
mutant L476M/Q480W, pH 7.6, 37C
26.6
pyruvate
-
mutant V375I, pH 7.6, 37C
40.3
pyruvate
-
wild-type, pH 7.6, 37C
47.4
pyruvate
-
fusion protein containing an N-terminal oligohistidine sequence on the large subunit
58
pyruvate
-
mutant Q487A, pH 7.0, 37C
62
pyruvate
-
mutant M263A, pH 7.6, 37C
65
pyruvate
-
mutant L476M, pH 7.6, 37C
66.7
pyruvate
-
native enzyme
71
pyruvate
-
wild-type, pH 7.6, 37C
86
pyruvate
-
mutant R289K, pH 7.6, 37C
121
pyruvate
-
wild-type, pH 7.0, 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
2-oxobutanoate
-
wild-type, pH 7.6, 37C
390
1.3
2-oxobutanoate
-
mutant V375A, pH 7.6, 37C
390
0.004
pyruvate
-
mutant Q110E, pH 7.6, 37C
31
0.04
pyruvate
-
mutant Q110H pH 7.6, 37C
31
0.05
pyruvate
-
mutant R289Q, pH 7.6, 37C
31
0.07
pyruvate
-
mutant E60A, pH 7.6, 37C
31
0.09
pyruvate
-
mutant Q110A, pH 7.6, 37C
31
0.1
pyruvate
-
mutant E60Q, pH 7.6, 37C
31
0.2
pyruvate
-
mutant Q110N, pH 7.6, 37C
31
0.208
pyruvate
-
mutant E47Q, pH 7.6, 37C
31
0.23
pyruvate
-
mutant F109M, pH 7.6, 37C
31
0.375
pyruvate
-
mutant E47A, pH 7.6, 37C
31
0.46
pyruvate
-
mutant V391A, pH 7.6, 37C
31
0.7
pyruvate
-
mutant V375A, pH 7.6, 37C
31
1.2
pyruvate
-
mutant V477I, pH 7.6, 37C
31
1.7
pyruvate
-
mutant R289K, pH 7.6, 37C
31
2.4
pyruvate
-
mutant M263A, pH 7.6, 37C
31
3.3
pyruvate
-
mutant Q480W, pH 7.6, 37C
31
3.6
pyruvate
-
mutant V375I, pH 7.6, 37C
31
5
pyruvate
-
mutant L476M, pH 7.6, 37C
31
6.1
pyruvate
-
wild-type, pH 7.6, 37C
31
6.1
pyruvate
-
mutant C83T, pH 7.6, 37C
31
6.9
pyruvate
-
mutant L476M/Q480W, pH 7.6, 37C
31
13.5
pyruvate
-
mutant C83A, pH 7.6, 37C
31
14.9
pyruvate
-
wild-type, pH 7.6, 37C
31
18.8
pyruvate
-
mutant C83S, pH 7.6, 37C
31
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0421
(2E)-3,3'-dioxo-1,1',3,3'-tetrahydro-2,2'-biindole-5,5'-disulfonate
-
pH 7.0, 37C
3.62
2-(2-bromobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
-
2.1
2-(2-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
-
2.16
2-(3-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
-
2.03
2-(4-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
-
0.00000939
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
wild-type, pH 7.5, 37C
0.0000168
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant C411S, pH 7.5, 37C
0.0000202
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant C607S, pH 7.5, 37C
0.0008
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant D375A, pH 7.5, 37C
0.00109
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant K299Q pH 7.5, 37C
0.00122
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
wild-type, pH 7.5, 37C
0.00135
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
wild-type, 37C, pH 7.5
0.00205
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant H392M, 37C, pH 7.5
0.0041
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
wild-type, pH 7.5, 37C
0.0133
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant D374A/D375A, pH 7.5, 37C
0.0155
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant D374E, pH 7.5, 37C
0.01735
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutantH351F, 37C, pH 7.5
0.0296
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant D374E/D375E, pH 7.5, 37C
0.0389
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant D375E, pH 7.5, 37C
0.181
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant D374A, pH 7.5, 37C
6.47
2-bromopyruvate
-
pH 7.5, 37C
4.41
2-butyl-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
-
0.0907
3-(7H-cyclopenta[b]pyridin-5-yl)-N-[(2-nitrophenyl)sulfanyl]alanine
-
pH 7.0, 37C
0.0152
6,6'-disulfanediyldipyridine-3-carboxylic acid
-
pH 7.0, 37C
0.789
8-(4,6-dimethoxypyrimidin-2-yloxy)-4-methylphthalazin-1(2H)-one
-
-
7.89
8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
-
1.4
benzaldehyde
-
isozyme AHAS II
0.000011
chlorimuron ethyl
-
about
0.036
flumetsulam
G0ZSE6
pH 7.5, 37C
-
0.003
imazaquin
-
about
1
imazaquin
-
-
0.121
imazethapyr
G0ZSE6
pH 7.5, 37C
0.105
L-valine
G0ZSE6
pH 7.5, 37C
0.16
L-valine
-
catalytic subunit plus small subunit, pH 7.0, 30C
0.00000045
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
-
mutantH351F, 37C, pH 7.5
0.00000311
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
-
wild-type, 37C, pH 7.5
0.00000365
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
-
mutant H392M, 37C, pH 7.5
0.00000368
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
-
mutant H351M, 37C, pH 7.5
0.00000939
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
-
wild-type, pH 7.5, 37C
0.0000168
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
-
mutant C411S, pH 7.5, 37C
0.0000202
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
-
mutant C607S, pH 7.5, 37C
0.00004857
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
-
mutant H351Q, 37C, pH 7.5
0.00301
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
-
mutant K299Q pH 7.5, 37C
0.00527
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
-
wild-type, pH 7.5, 37C
0.0293
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
-
wild-type, pH 7.5, 37C
0.036
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
-
mutant D374E, pH 7.5, 37C
0.0741
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
-
mutant D374A, pH 7.5, 37C
0.198
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
-
mutant D375A, pH 7.5, 37C
0.309
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
-
mutant D374A/D375A, pH 7.5, 37C
0.79
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
-
mutant D374E/D375E, pH 7.5, 37C
0.00000823
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
wild-type, pH 7.5, 37C
0.00000902
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
mutant K299Q pH 7.5, 37C
0.0000093
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
mutant H392M, 37C, pH 7.5
0.0000109
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
wild-type, 37C, pH 7.5
0.000013
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
wild-type, pH 7.5, 37C
0.00002304
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
mutantH351F, 37C, pH 7.5
0.000108
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
mutant D374E, pH 7.5, 37C
0.00086
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
mutant D374A, pH 7.5, 37C
0.00000939
NC-311
-
wild-type, pH 7.5, 37C
0.0000168
NC-311
-
mutant C411S, pH 7.5, 37C
0.0000202
NC-311
-
mutant C607S, pH 7.5, 37C
1
primisulfuron-methyl
-
-
0.065
pyriminobac-methyl
G0ZSE6
pH 7.5, 37C
-
0.0003
sulfometuron methyl
-
mutant E47Q, 37C, pH 7.6
0.0006
sulfometuron methyl
-
mutant E47A, 37C, pH 7.6
0.0008
sulfometuron methyl
-
wild-type, 37C, pH 7.6
0.0032
sulfometuron methyl
-
mutant D428N, 37C, pH 7.6
0.0044
sulfometuron methyl
-
mutant Q480W, pH 7.6, 37C
0.005
sulfometuron methyl
-
pH 7.5, 37C, in the presence of 3.5 M KCl
0.006
sulfometuron methyl
-
mutant D428E, 37C, pH 7.6
0.041
sulfometuron methyl
-
mutant L476M/Q480W, pH 7.6, 37C
2.5
sulfometuron-methyl
-
-
1
trisulfuron
-
-
-
0.003
valine
-
pH 7.0, 30C, mutant L222A
0.006
valine
-
pH 7.0, 30C, mutant K218A
0.0156
valine
-
pH 7.0, 30C, mutant S212A
0.0162
valine
-
pH 7.0, 30C, mutant L177A
0.02
valine
-
pH 7.0, 30C, mutant H205A
0.0245
valine
-
pH 7.0, 30C, mutant R216A
0.026
valine
-
pH 7.0, 30C, mutant F204A
0.039
valine
-
pH 7.0, 30C, mutant P206A
0.058
valine
-
pH 7.0, 30C, mutant H181A
0.177
valine
-
pH 7.0, 30C, wild-type enzyme
0.231
valine
-
-
16.3
valine
-
pH 7.0, 37C, holoenzyme
0.336
leucine
-
-
additional information
leucine/valine
-
an equimolar mixture of leucine and valine
0.201
metsulfuron-methyl
G0ZSE6
pH 7.5, 37C
additional information
additional information
-
inhibition kinetics of sulfonylurea herbicides
-
additional information
additional information
-
-
-
additional information
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
(5-bromo-2-[[([2-[(2-chloroethoxy)methyl]phenyl]sulfonyl)carbamoyl]amino]pyrimidin-4-yl)methyl benzoate
-
pH 7.5, 22C
0.00484
(5-bromo-2-[[([2-[(2-chloroethoxy)methyl]phenyl]sulfonyl)carbamoyl]amino]pyrimidin-4-yl)methyl phenylacetate
-
pH 7.5, 22C
0.00584
(5-bromo-2-[[([2-[(2-chloroethoxy)methyl]phenyl]sulfonyl)carbamoyl]amino]pyrimidin-4-yl)methyl prop-2-enoate
-
pH 7.5, 22C
0.021
1-(4,6-dimethoxypyrimidin-2-yl)-5-methoxymethyl-N-(2-isopropyl-6-nitrophenyl)-1H-1,2,4-triazole-3-sulfonamide
-
pH 7.6, 37C
0.022
1-(4,6-dimethoxypyrimidin-2-yl)-5-methyl-N-(2-isopropyl-6-nitrophenyl)-1H-1,2,4-triazole-3-sulfonamide
-
pH 7.6, 37C
0.032
1-(4,6-dimethoxypyrimidin-2-yl)-5-methylthio-N-(2-chloro-6-fluorophenyl)-1H-1,2,4-triazole-3-sulfonamide
-
pH 7.6, 37C
0.03
1-(4-chloro-6-methoxypyrimidin-2-yl)-5-methoxy-N-(2-methyl-6-nitrophenyl)-1H-1,2,4-triazole-3-sulfonamide
-
pH 7.6, 37C
0.00603
2,3-dichloro-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.00568
2-(1,1-dihydroxyethyl)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.00746
2-(2-chloroethoxy)-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00452
2-(2-chloroethoxy)-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00719
2-(difluoromethoxy)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.00684
2-acetyl-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.00714
2-acetyl-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
-
0.007
2-amino-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.00782
2-bromo-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.0074
2-bromo-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
-
0.00621
2-butoxy-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.00762
2-chloro-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.00749
2-chloro-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
-
0.00529
2-chloro-N-([4-(methylamino)-6-[(1-methylethyl)sulfanyl]-1,3,5-triazin-2-yl]carbamoyl)benzenesulfonamide
-
pH 7.5, 22C
0.00693
2-chloro-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00471
2-chloro-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00649
2-chloro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00541
2-chloro-N-[[4-(ethylsulfanyl)-6-(methylamino)-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00369
2-chloro-N-[[4-(ethylsulfanyl)-6-methoxy-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00442
2-chloro-N-[[4-(ethylsulfanyl)-6-methylpyrimidin-2-yl]carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00525
2-chloro-N-[[4-(methylamino)-6-(methylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00556
2-chloro-N-[[4-methoxy-6-(methylsulfanyl)pyrimidin-2-yl]carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00355
2-chloro-N-[[4-methoxy-6-(propylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00352
2-chloro-N-[[4-methyl-6-(propylsulfanyl)pyrimidin-2-yl]carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00531
2-[(2-chloroethoxy)methyl]-N-[(4-chloropyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00533
2-[(2-chloroethoxy)methyl]-N-[(4-methylpyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
pH 7.5, 22C
0.00633
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3-fluorobenzoic acid
-
-
0.00539
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3-methylbenzoic acid
-
-
0.00432
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-(methylsulfanyl)benzoic acid
-
-
0.00459
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-ethylbenzoic acid
-
-
0.0047
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-ethynylbenzoic acid
-
-
0.00627
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-fluorobenzoic acid
-
-
0.0072
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-hydroxybenzoic acid
-
-
0.00505
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-iodobenzoic acid
-
-
0.0046
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methoxybenzoic acid
-
-
0.00503
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbenzoic acid
-
-
0.0039
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-nitrobenzoic acid
-
-
0.00573
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(1-methylethoxy)benzoic acid
-
-
0.00828
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(1H-pyrrol-1-yl)benzoic acid
-
-
0.00711
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(ethylsulfanyl)benzoic acid
-
-
0.00757
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(methylsulfanyl)benzoic acid
-
-
0.00587
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(methylsulfonyl)benzoic acid
-
-
0.00567
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(phenylcarbonyl)benzoic acid
-
-
0.00629
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(propylsulfanyl)benzoic acid
-
-
0.00696
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(trifluoromethoxy)benzoic acid
-
-
0.00705
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-ethoxybenzoic acid
-
-
0.00657
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-ethylbenzoic acid
-
-
0.0073
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-fluorobenzoic acid
-
-
0.00766
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-iodobenzoic acid
-
-
0.00736
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-methoxybenzoic acid
-
-
0.00689
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-methylbenzoic acid
-
-
0.00664
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-nitrobenzoic acid
-
-
0.0077
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-phenoxybenzoic acid
-
-
0.00624
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-propoxybenzoic acid
-
-
0.00589
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-propylbenzoic acid
-
-
0.00664
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.00488
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(1-methylethoxy)benzoic acid
-
-
0.00667
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(ethylsulfanyl)benzoic acid
-
-
0.00768
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(methylsulfanyl)benzoic acid
-
-
0.00519
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(phenylcarbonyl)benzoic acid
-
-
0.00572
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(propylsulfanyl)benzoic acid
-
-
0.00602
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(trifluoromethyl)benzoic acid
-
-
0.0067
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-ethoxybenzoic acid
-
-
0.00767
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-fluorobenzoic acid
-
-
0.00699
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-iodobenzoic acid
-
-
0.00705
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-methoxybenzoic acid
-
-
0.00753
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-methylbenzoic acid
-
-
0.00669
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-nitrobenzoic acid
-
-
0.0056
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-phenoxybenzoic acid
-
-
0.00614
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-propoxybenzoic acid
-
-
0.0068
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
-
0.00712
2-[[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]-N,N-dimethylbenzamide
-
pH 7.5, 22C
0.0078
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]biphenyl-2-carboxylic acid
-
-
0.00609
5-amino-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.00358
5-benzyl-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.00571
5-bromo-2-([[(2-chlorophenyl)sulfonyl]carbamoyl]amino)pyrimidin-4-yl benzoate
-
pH 7.5, 22C
0.0045
5-bromo-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.00535
5-chloro-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.00371
5-cyano-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
-
0.00053
AVS-2087
P45261
pH 7.5, 37C, recombinant enzyme
0.000007
bensulfuron-methyl
Q6K2E8
wild-type, pH 7.5, 30C
0.0000056
bispyribac-sodium
Q6K2E8
wild-type, pH 7.5, 30C
0.00000563
bispyribac-sodium
Q6K2E8
pH 7.5, 30C, wild-type enzyme, callus
0.000421
bispyribac-sodium
Q6K2E8
mutant W548L/S627I, pH 7.5, 30C; pH 7.5, 30C, mutant enzyme, callus
0.00024
Cadre
-
mutant S167R, pH not specified in the publication, temperature not specified in the publication
0.00089
Cadre
-
mutant S506A, pH not specified in the publication, temperature not specified in the publication
0.0026
Cadre
-
mutant S167A, pH not specified in the publication, temperature not specified in the publication
0.0035
Cadre
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0041
Cadre
-
an imidazole herbicide, wild-type enzyme IC50: 0.0041 mM
0.009
chlorimuron ethyl
-
IC50: 0.009 mM, over 80% inhibition at 0.04 mM
0.007
chlorimuronethyl
-
37C
0.000017
chlorsulfuron
Q6K2E8
wild-type, pH 7.5, 30C
0.0000173
chlorsulfuron
Q6K2E8
pH 7.5, 30C, wild-type enzyme, callus
0.0000928
chlorsulfuron
Q6K2E8
pH 7.5, 30C, mutant enzyme, callus
0.000093
chlorsulfuron
Q6K2E8
mutant W548L/S627I, pH 7.5, 30C
0.0078
ethyl 2-([[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.00651
ethyl 2-([[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.0067
ethyl 2-([[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.0055
ethyl 2-[(pyrimidin-2-ylcarbamoyl)sulfamoyl]benzoate
-
pH 7.5, 22C
0.00711
ethyl 2-[([4-[(acryloyloxy)methyl]-5-bromopyrimidin-2-yl]carbamoyl)sulfamoyl]benzoate
-
pH 7.5, 22C
0.0092
ethyl 2-[[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
pH 7.5, 22C
0.0061
ethyl 2-[[(4,6-dimethylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
pH 7.5, 22C
0.00834
ethyl 2-[[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
pH 7.5, 22C
0.00709
ethyl 2-[[(4-chloro-6-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
pH 7.5, 22C
0.00669
ethyl 2-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
pH 7.5, 22C
0.00703
ethyl 2-[[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
pH 7.5, 22C
0.00678
ethyl 2-[[(5-bromo-4,6-dimethylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
pH 7.5, 22C
0.0068
ethyl 2-[[(5-bromo-4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
pH 7.5, 22C
0.00002
ethyl 5-[(4,6-dimethoxy-2-pyrimidinyl)aminocarbonylaminosulfonyl]-1-methyl-1H-pyrazole-4-carboxylate
Q6K2E8
wild-type, pH 7.5, 30C
0.0096
imazapyr
Q6K2E8
wild-type, pH 7.5, 30C
0.00148
imazaquin
Q6K2E8
pH 7.5, 30C, wild-type enzyme, callus; wild-type, pH 7.5, 30C
0.00697
imazaquin
-
37C
0.0167
imazaquin
Q6K2E8
mutant W548L/S627I, pH 7.5, 30C; pH 7.5, 30C, mutant enzyme, callus
0.000025
imazosulfuron
Q6K2E8
wild-type, pH 7.5, 30C
0.065
imazosulfuron
Q6K2E8
mutant W548L/S627I, pH 7.5, 30C
0.00491
KHG20612
P45261
pH 7.5, 37C, recombinant enzyme
0.00142
KSW30191
P45261
pH 7.5, 37C, recombinant enzyme
0.012
L-isoleucine
P9WG41
wild-type, pH 7.5, 37C
0.04
L-isoleucine
P9WG41
R101A, pH 7.5, 37C
0.062
L-isoleucine
P9WG41
mutant S27A, pH 7.5, 37C
0.32
L-isoleucine
P9WG41
L89A, pH 7.5, 37C
0.0014
L-leucine
P9WG41
R101A, pH 7.5, 37C
0.0016
L-leucine
P9WG41
wild-type, pH 7.5, 37C
0.004
L-valine
P9WG41
R101A, pH 7.5, 37C
0.005
L-valine
P9WG41
wild-type, pH 7.5, 37C
0.0075
L-valine
P9WG41
mutant S27A, pH 7.5, 37C
0.012
L-valine
P9WG41
L89A, pH 7.5, 37C
0.00064
Londax
P9WG41
wild-type, pH 7.5, 37C
0.013
Londax
-
a sulfonylurea herbicide, wild-type enzyme IC50: 0.013 mM
0.021
Londax
P9WG41
mutant L141A, pH 7.5, 37C
0.00458
methyl 2-([[4-(ethylsulfanyl)-6-methoxypyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.00733
methyl 2-([[4-(methylamino)-6-(propylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.00686
methyl 2-([[4-chloro-6-(methylamino)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.00631
methyl 2-([[4-chloro-6-(methylsulfanyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.00786
methyl 2-([[4-ethoxy-6-(methylamino)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.00646
methyl 2-([[4-methoxy-6-(methylsulfanyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.00474
methyl 2-([[4-methoxy-6-(propylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.00415
methyl 2-([[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.00482
methyl 2-([[5-bromo-4-(dibromomethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.00461
methyl 2-([[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.00605
methyl 2-([[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
pH 7.5, 22C
0.0071
methyl 2-[[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]sulfamoyl]benzoate
-
pH 7.5, 22C
0.00571
methyl 2-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
pH 7.5, 22C
0.00453
methyl 2-[[(5-bromo-4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
pH 7.5, 22C
0.0046
N-([4-[(benzyloxy)methyl]-5-bromopyrimidin-2-yl]carbamoyl)-2-chlorobenzenesulfonamide
-
pH 7.5, 22C
0.00531
N-([5-bromo-4-[(prop-2-en-1-yloxy)methyl]pyrimidin-2-yl]carbamoyl)-2-(2-chloroethoxy)benzenesulfonamide
-
pH 7.5, 22C
0.008
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
pH 7.5, 22C
0.00769
N-[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
pH 7.5, 22C
0.00523
N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
pH 7.5, 22C
0.00552
N-[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-chlorobenzenesulfonamide
-
pH 7.5, 22C
0.0053
N-[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
pH 7.5, 22C
0.00545
N-[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
pH 7.5, 22C
0.0048
N-[(5-bromo-4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
pH 7.5, 22C
0.00488
N-[(5-bromo-4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
pH 7.5, 22C
0.00478
N-[(5-bromo-4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-2-chlorobenzenesulfonamide
-
pH 7.5, 22C
0.00477
N-[(5-bromo-4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
pH 7.5, 22C
0.00508
N-[(5-bromo-4-methoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
pH 7.5, 22C
0.00553
N-[(5-bromo-4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
pH 7.5, 22C
0.00388
N-[(5-bromopyrimidin-2-yl)carbamoyl]-2-chlorobenzenesulfonamide
-
pH 7.5, 22C
0.0044
N-[[5-bromo-4-(1-methylethoxy)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
pH 7.5, 22C
0.00516
N-[[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
pH 7.5, 22C
0.00669
N-[[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
pH 7.5, 22C
0.00503
N-[[5-bromo-4-(dibromomethyl)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
pH 7.5, 22C
0.00697
N-[[5-bromo-4-(dibromomethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
pH 7.5, 22C
0.0036
N-[[5-bromo-4-(ethenyloxy)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
pH 7.5, 22C
0.00427
N-[[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]-2-chlorobenzenesulfonamide
-
pH 7.5, 22C
0.00514
N-[[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
pH 7.5, 22C
0.00566
N-[[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]-2-chlorobenzenesulfonamide
-
pH 7.5, 22C
0.00617
N-[[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
pH 7.5, 22C
0.0058
N-[[5-bromo-4-(tribromomethyl)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
pH 7.5, 22C
0.008
NC-311
-
mutant S506A, pH not specified in the publication, temperature not specified in the publication
0.011
NC-311
P9WG41
mutant L141A, pH 7.5, 37C
0.032
NC-311
-
mutant S167A, pH not specified in the publication, temperature not specified in the publication
0.048
NC-311
P9WG41
wild-type, pH 7.5, 37C
0.054
NC-311
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0042
primisulfuron methyl
-
IC50: 0.0042 mM, over 80% inhibition at 0.04 mM
0.000087
pyrazosulfuron ethyl
-
IC50: 87 nM, over 80% inhibition at 0.04 mM
0.00087
pyrazosulfuron ethyl
-
IC50: 870 nM
0.05
pyrazosulfuron-ethyl
Q6K2E8
mutant W548L/S627I, pH 7.5, 30C
0.000008
pyriminobac
Q6K2E8
wild-type, pH 7.5, 30C
0.000011
pyrithiobac-sodium
Q6K2E8
wild-type, pH 7.5, 30C
0.0048
sulfometuron methyl
-
IC50: 0.0048 mM, over 80% inhibition at 0.04 mM
0.2763
sulfometuron methyl
P45261
pH 7.5, 37C, recombinant enzyme
0.01
sulfometuronmethyl
-
37C
0.0293
[1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
a triazolopyrimidine derivative herbicide, wild-type enzyme IC50: 0.0293 mM
0.00503
[5-bromo-2-[([[2-(1-methoxyethenyl)phenyl]sulfonyl]carbamoyl)amino]pyrimidin-4-yl]methyl prop-2-enoate
-
pH 7.5, 22C
0.006
metsulfuron methyl
-
IC50: 0.006 mM, over 80% inhibition at 0.04 mM
additional information
additional information
-
sensitivity of different varieties of Schoenoplectus juncoides against herbicides, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0043
-
substrate: pyruvate, pH 7.5, 37C, in the presence of 3.5 M KCl
0.03
-
mutant H351Q, 37C, pH 7.5
0.04
-
mutant H351M, 37C, pH 7.5
0.06
-
catalytic subunit ilvI, regulatory subunit ilvN, 37C, pH 7.6
0.063
-
mutant DELTA567-582, 37C, pH 7.4
0.068
-
mutant DELTA630, 37C, pH 7.4
0.09
-
mutant D374A/D375A, pH 7.5, 37C
0.17
P9WG41
isolated catalytic subunit, pH 7.5, 37C
0.64
-
mutant D374E/D375E, pH 7.5, 37C
0.65
-
mutant D375A, pH 7.5, 37C
0.66
-
-
0.77
-
mutant D374E, pH 7.5, 37C
0.91
-
mutant D374A, pH 7.5, 37C
1.02
-
mutant K255F, pH 7.5, 37C
1.13
P9WG41
holoenzyme, pH 7.5, 37C; pH 7.5, 37C
1.3
-
catalytic subunit ilvB, regulatory subunit ilvB, 37C, pH 7.6
1.5
P45261
purified recombinant enzyme
1.5
-
calculated per subunit, purified recombinant His-tagged enzyme
1.5
-
pH 7.6, 37C
1.53
-
mutant D375E, pH 7.5, 37C
1.55
-
wild-type, pH 7.5, 37C
1.58
-
mutantH351F, 37C, pH 7.5
1.6
-
mutant E47A, 37C, pH 7.6
1.73
-
wild-type, 37C, pH 7.4
1.87
-
wild-type, pH 7.5, 37C
2
-
mutant E47Q, 37C, pH 7.6
2.17
-
mutant K255Q, pH 7.5, 37C
2.6
-
mutant M250A with His-tag, pH 7.6, 37C
2.8
-
mutant R276K with His-tag, pH 7.6, 37C
2.8
-
purified catalytic subunit
3.23
-
mutant H392M, 37C, pH 7.5
3.4
-
mutant F109M, pH 7.6, 37C
4.15
-
mutant K299Q pH 7.5, 37C
4.4
-
mutant enzyme W574L
4.6
-
purified holoenzyme
5.78
-
wild-type, 37C, pH 7.5
6.8
-
catalytic subunit, pH 7.0, 30C
8
O06335, O53554, P9WG39, P9WG41
pH 7.5, 37C; pH 7.5, 37C
8.2
-
mutant V375A, pH 7.6, 37C
8.51
-
mutant S653N
9.3
-
catalytic subunit ilvI, regulatory subunit ilvM, 37C, pH 7.6
9.4
-
wild-type AHAS III, pH 7.6, 37C
11
-
mutant W574
11
O06335, O53554, P9WG39, P9WG41
presence of 20 mM acetate, pH 7.5, 37C; presence of 20 mM acetate, pH 7.5, 37C
11.9
-
mutant W464L with His-tag, pH 7.6, 37C
12
-
mutant enzyme A122V
13.5
G0ZSE6
pH 7.5, 37C
17
-
wild-type with His-tag, pH 7.6, 37C
20
-
wild-type, 37C, pH 7.6
20
-
wild-type, pH 7.6, 37C
20.9
-
wild-type AHAS III, truncated regulatory subunit ilvH-DELTA 86, pH 7.6, 37C
22.7
-
mutant V375I, pH 7.6, 37C
32
-
catalytic subunit ilvB, truncated regulatory subunit ilvB-DELTA86, 37C, pH 7.6
34.3
-
wild-type, pH 7.6, 37C
36
O06335, O53554, P9WG39, P9WG41
presence of 20 mM acetate, pH 7.5, 37C
42
O06335, O53554, P9WG39, P9WG41
pH 7.5, 37C
49
-
catalytic subunit plus small subunit, pH 7.0, 30C
49.8
-
catalytic subunit ilvB, regulatory subunit ilvM, 37C, pH 7.6
50.8
-
wild-type AHAS I, 37C, pH 7.6
53
-
fusion protein with N-terminal oligohistidine at the large subunit
60.4
-
wild-type AHAS II, 37C, pH 7.6
60.5
-
reconstituted, recombinant holoenzyme
63.6
-
recombinant holoenzyme
150
-
30C, 60 ng protein per assay
267
-
30C, 90 ng protein per assay
2883
-
pH 7.0, 30C, sulfonylurea-susceptible biotype
2950
-
pH 7.0, 30C, sulfonylurea-resistant biotype
additional information
-
spectrophotometric assay involving an indirect detection of the product acetolactate
additional information
-
-
additional information
-
assay methods
additional information
-
-
additional information
-
-
additional information
-
time lag during the production of acetolactate from pyruvate and cofactors. Time lag is temperature depended being lowest at 37C with 250 seconds
additional information
-
specific activity also depends on protein concentration, with lower concentration giving lower activity, activity may be generally increased by pre-incubation at 30C prior to assay
additional information
-
isozyme substrate specificities
additional information
-
-
additional information
-
-
additional information
-
effects of pyruvate and sucrose on relative ALS activity in light and dark conditions, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
-
acetate buffer
5.8
-
acetate buffer
6 - 7
-
AHAS I
6 - 7
-
-
6 - 8
-
catalytic subunit
6 - 8.5
-
enzyme from green barley extract
6.5
-
enzyme from etiolated preparations
7 - 7.4
-
enzyme form I
7
-
AHAS II
7
-
phosphate buffer
7
-
isoform ALS I
7
P37251
assay at
7.2 - 7.6
-
enzyme form II
7.5
-
isoenzyme I
7.5
-
enzyme from mutant A122V, W574S, W574L and S653N
7.5
-
isoform ALS I
7.5
-
standard assay at
7.5
P45261
assay at
7.5
-
assay at
7.5
Q6K2E8
assay at
7.5
-
assay at
7.6
-
assay at
8.5
-
isoenzyme III
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
pH 6.5: about 40% of maximal activity, pH 10.0: about 65% of maximal activity, pH profile
5.5 - 8
-
pH 5.5: about 80% of maximal activity, pH 8.0: about 55% of maximal activity, AHAS I
5.5 - 8
-
-
6 - 6.9
-
pH 6.0: about 50% of maximal activity, pH 6.9: about 30% of maximal activity
6 - 7.5
-
pH 6.0: about 25% of maximal activity, pH 7.5: about 65% of maximal activity
6 - 8
-
pH 6.0: about 55% of maximal activity, pH 8.0: about 50% of maximal activity
6.5 - 7
-
phosphate buffer
6.5 - 7.5
-
about 60% of maximal activity at pH 6.5 and pH 7.5, AHAS II
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
assay at room temperature
25
-
assay at
30
Q6K2E8
assay at
37
-
assay at
37
-
standard assay at
37
-
assay at
37
P45261
assay at
37
P37251
assay at
37
-
assay at
46 - 50
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 50
-
30C: about 50% of maximal activity, 50C: about 65% of maximal activity, temperature profile
25 - 45
-
activity can be detected between 25 and 45C, with the 3540C range being optimal. A rapid loss in catalytic activity is observed above 45C
38 - 40
-
pH 6.5
additional information
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6
-
isoelectric focusing, isoform ALS I
5.3
-
isoelectric focusing, isoform ALS I
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
an N-terminal peptide, which is subsequently removed, is required to direct the protein to chloroplasts in plants
Manually annotated by BRENDA team
Q42768
an N-terminal peptide, which is subsequently removed, is required to direct the protein to chloroplasts in plants
Manually annotated by BRENDA team
P07342
an N-terminal peptide, which is subsequently removed, is required to direct the protein to mitochondria in fungi
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
-
PAGE
658566
55000
-
AHAS II, gel filtration
395871
109000
-
gel filtration in absence of FAD
395902
113000
-
gel filtration in presence of FAD
395902
119000
-
gel filtration
395904
120000
-
PAGE
658566
124000
-
gel filtration
395907
128000
-
gel filtration
395908
130000
-
sucrose density gradient sedimentation, glycerol density gradient sedimentation
395885
132000
-
glycerol density gradient sedimentation
395907
150000
-
-
395912
150000
-
-
395915
150000
-
-
395918
150000
-
gel filtration
657572
172000
-
gel filtration
395922
178000
-
non-denaturing PAGE
395923
182000
-
PAGE
658566
190000 - 210000
-
another enzyme species with MW of 430000-460000 Da is detected, gel filtration
395910
193000
-
AHAS I, gel filtration
395871
200000
-
calculation from sedimentation and diffusion data
395898
200000
-
gel filtration
660559
204000
-
gel filtration
395923
220000
-
equilibrium sedimentation
395897
225000 - 250000
-
nondenaturing PAGE
395916
238000
-
PAGE, isoform ALS II
659100
248000
-
PAGE, isoform ALS I
659100
250000
-
gel filtration
395889
277000
-
gel filtration
395919
300000
-
above, recombinant holoenzyme, gel filtration
673626
430000 - 460000
-
another enzyme species with MW of 190000-210000 Da is detected, gel filtration
395910
440000
-
gel filtration
395877
456000
-
predominant form, an enzyme form of 110000 Da also detected, gel filtration
395896
600000
-
equilibrium sedimentation
395892
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 62000, SDS-PAGE
?
-
x * 65000, SDS-PAGE
?
P9WG41
x * 20000, SDS-PAGE
?
P9WG41
x * 68000, SDS-PAGE
?
-
x * 9500 + x * 60000, isoenzyme I, SDS-PAGE
?
-
x * 17500 + x * 61800, calculation from nucleotide sequence
?
-
x * 11000 + x * 60000
?
-
3 major bands detected by SDS-PAGE: 26000 Da, 35000 Da and 46000 Da
?
-
x * 15000 + x * 57000 + x * 58000, SDS-PAGE
?
-
x * 16200 + x * 67200, SDS-PAGE
?
-
x * 58000, SDS-PAGE with urea
?
-
x * 48000, deduced from gene sequence
?
-
x * 65000, recombinant enzyme, SDS-PAGE
?
-
x * 65000, about, SDS-PAGE and MALDI-TOF spectrometry
?
P45261
x * 63700, recombinant His-tagged catalytic subunit, SDS-PAGE
?
G0ZSE6
x * 62000, SDS-PAGE, catalytic subunit
?
Synechocystis sp. PCC6803
-
x * 65000, about, SDS-PAGE and MALDI-TOF spectrometry
-
?
-
x * 68000, SDS-PAGE
-
?
-
x * 62000, SDS-PAGE, catalytic subunit
-
?
Leuconostoc lactis NCW1
-
3 major bands detected by SDS-PAGE: 26000 Da, 35000 Da and 46000 Da
-
dimer
-
2 * 75000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE
dimer
-
2 * 64000, SDS-PAGE
dimer
-
2 * 64000, SDS-PAGE
dimer
-
2 * 61000, SDS-PAGE, 2 * 63864, ion spray MS analysis
dimer
-
2 * 65000 and/or 66000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
dimer
-
the mobile loop comprising residues 567-582 on the C-terminus is involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
dimer
-
1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit
dimer
P07342
1 * 59000-66000, catalytic subunit + 1 * 34000, regulatory subunit
dimer
-
1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit
dimer
Q42768
1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit
dimer
Leuconostoc lactis NCW1
-
2 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
-
monomer
-
1 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
oligomer
-
8 * 15000 + 8 * 60000, SDS-PAGE
oligomer
-
x * 68300, recombinant His-tagged catalytic subunit, + x * 20400, recombinant His-tagged regulatory subunit, SDS-PAGE
oligomer
-
x * 68300, recombinant His-tagged catalytic subunit, + x * 20400, recombinant His-tagged regulatory subunit, SDS-PAGE
-
tetramer
-
4 * 58000, SDS-PAGE
tetramer
-
2 * 9800 + 2 * 59000, SDS-PAGE
tetramer
-
4 * 65000, SDS-PAGE, both isoforms
trimer
-
3 * 60000, SDS-PAGE
trimer
-
3 * 55000, SDS-PAGE
trimer
-
3 * 55000, SDS-PAGE
trimer
-
3 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
trimer
Leuconostoc lactis NCW1
-
3 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
-
monomer
Leuconostoc lactis NCW1
-
1 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
-
additional information
-
N-terminal sequence analysis
additional information
-
enzymes in the AHAS family generally consist of regulatory and catalytic subunits, subunit composition, dimeric structure analysis of the regulatory subunit of isozyme AHAS III, overview
additional information
-
heterotetrameric enzyme composed of a small, regulatory and a large, catalytic subunit
additional information
-
pairs of catalytic subunits form an intimate dimer containing two active sites, each of which lies across a dimer interface and involves both monomers, the catalytic subunit of AHAS II is not active alone
additional information
-
the enzyme consists of two diffrent types of subunits, a catalytic one and a regulatory one
additional information
-
by mapping the 3D contour maps of CoMFA and CoMSIA models into the possible inhibitory active site in the crystal structure of catalytic subunit of yeast AHAS, a plausible binding model for AHAS, with best fit QSAR in the literature so far, is proposed
additional information
-
isozyme AHAS I, catalytic subunit ilvB, regulatory subunit ilvN. AHAS II, catalytic subunit ilvG, regulatory subunit ilvM. Isozyme AHAS III, catalytic subunit ilvI, regulatory subunit ilvH. AHAS II regulatory subunit ilvM is able to activate the catalytic subunits of all three of the isozymes, and the truncated AHAS III regulatory subunits ilvH-DELTA80, ilvH-DELTA86 and ilvH-DELTA89 are able to activate the catalytic subunits of both AHAS I and AHAS III. Contrary to wild-type, none of the heterologously activated enzymes have any feedback sensitivity
additional information
-
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
Q42768
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
P07342
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
-
the enzyme consists of two diffrent types of subunits, a catalytic one and a regulatory one
-
additional information
Leuconostoc lactis NCW1
-
N-terminal sequence analysis
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the N-terminal peptide of the precursor protein is removed
side-chain modification
-
6 atoms of phosphorus tightly bound to one molecule of enzyme, 3 molecules of cocarboxylase tightly bound per molecule of enzyme
proteolytic modification
Q42768
the N-terminal peptide of the precursor protein is removed
proteolytic modification
-
the N-terminal peptide of the precursor protein is removed
side-chain modification
-
disulfide bond between C163 and C309
proteolytic modification
P07342
the N-terminal peptide of the precursor protein is removed
proteolytic modification
-
enzyme contains a N-terminal mitochondrial targeting sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitors N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide and methyl 2-([(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl)benzoate, to 3.0 A and 2.8 A resolution, respectively. In both complexes, the inhibitors are bound in the tunnel leading to the active site, such that the sole substituent of the heterocyclic ring is buried deepest and oriented towards the thiamine diphosphate. The cofactor is intact and present most likely as the hydroxylethyl intermediate
P17597
resolution of the diffraction data for herbicide-AHAS complexes varies between 2.2 A for the chlorsulfuron-bound structure to 2.8 A for the chlorimuron ethyl-bound structure, between 2.5 and 2.9 A for other catalytic subunit-herbicide complexes, overview
-
purified recombinant wild-type and selenomethionine-labeled isozyme AHAS III in complex with valine, hanging drop vapour diffusion method, room temperature, 0.0036 ml of protein solution containing 10-25 mg/ml protein and 0.5 M MgCl2, is mixed with reservoir solution containing 30-40% PEG 400, 0.4-0.6 M MgCl2, 100 mM Tris-HCl, pH 8.5, tetragonal or orthorhombic crystals, X-ray diffraction structure determination and analysis at 1.75-2.5 A resolution
-
solution NMR studies. The secondary structure of the FAD binding domain of large subunit ilvB is similar to the structure of this domain in the catalytic subunit of yeast AHAS. The regulatory subunit ilvN interacts with ilvBalpha and ilvBbeta domains of the catalytic subunit and not with the ilvBgamma domain. ilvN binds close to the FAD binding site in ilvBbeta and proximal to the intrasubunit ilvBalpha/ilvBbeta domain interface
-
homology modeling of enzyme based on the structure of the yeast enzyme.In the model, the S167 and S506 residues lie near the FAD binding site, while the S539 residue is found near the thiamine diphosphate binding site
-
crystal structure analysis
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
-
80% residual activity
660559
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0
-
freezing and subfreezing temperatures are severely damaging
395896
30
-
1 hour, no loss of activity
658566
37
-
half-life: 7.5 min, without substrate and cofactors
395890
45
-
15 min, 69% loss of activity, isoenzyme I, slight stimulation of activity of isoenzyme III
395887
50
-
30 min, stable
395923
60
-
30 min, stable
395912
65
-
half-life: 88 seconds
395914
70
-
half-life: 65 seconds
395914
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
FAD protects the enzyme during dialysis
-
glycerol, bovine serum albumin and pyruvate-thiamine diphosphate stabilize
-
dialysis causes 38% loss of activity of isoenzyme I, stimulates activity of isoenzyme III
-
stabilized by pyruvate, 2-mercaptoethanol or dithiothreitol
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
10% O2, 37C, 30 min, 90% loss of activity
-
395875
5% O2, half-life: 35 min
-
395921
10% O2, 37C, 30 min, 90% loss of activity
-
395875
oxygen-dependent inactivation of the enzyme complexed with thiamine diphosphate, FAD and magnesium acetolactate, no inactivation of the enzyme-FAD complex
-
395879
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, 21 days, 15% loss of activity of mutant enzyme A122V, less than 1% loss of activity of mutant enzymes W574S and S653N, 3% loss of activity of mutant enzyme W574L
-
-70C, 4% loss of activity after 3 weeks with three freeze-thaw cycles, 8% loss of activity after 5 weeks with five freeze-thaw cycles, 9-10% loss of activity after 6 months with no intervening freeze-thaw cycle
-
4C, 10% loss of activity after 3 weeks, 23% loss of activity after 5 weeks
-
4C, 21 days, 30% loss of activity of mutant enzyme A122V, 6% loss of activity of mutant enzyme W574S, 20% loss of activity of mutant enzyme W574L, 18% loss of activity of mutant enzyme S653N
-
-25C, no significant loss of activity after 6 months
-
4C, stable for several days
-
4C, 24 h, 36% loss of activity
-
-20C, 20% glycerol, stable for 2 months
-
-20C, stable for over 1 month
-
0-4C, 50 mM potassium phosphate, pH 7.0, 10 mM mercaptoethanol, 1 mM MgCl2, 0.01 mM thiamine diphosphate, 1 month, 20% loss of activity
-
-70C, 3 weeks, loss of 5% of activity
G0ZSE6
4C, 3 weeks, loss of 10% of activity
G0ZSE6
-80C, concentrated enzyme solution is indefinitely stable
-
-20C, 50 mM phosphate, pH 8, 50% v/v glycerol, 3 weeks, less than 25% loss of activity
-
-20C or -80C, not stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant enzymes A122V, W574S, W574L and S653N expressed in Escherichia coli
-
His-tagged recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to 96% purity
-
isoenzyme II
-
recombinant His-tagged isozyme I holoenzyme or individual subunits from strain BL21 by affinity chromatography
-
recombinant His-tagged AHAS catalytic subunit from Escherichia coli strain BL21(DE3) to homogeneity by nickel affinity and anion exchange chromatography, and gel filtration
P45261
recombinant His-tagged catalytic subunit to homogeneity
-
recombinant His-tagged enzyme subunits from Escherichia coli to homogeneity by nickel affinity chromatography and dialysis
-
recombinant wild-type and mutant enzymes from Escherichia coli strain DH5alpha
-
recombinant wild-type and mutant GST-tagged enzymes from Escherichia coli strain BL21(DE3) by two steps of glutathione affinity chromatography to homogeneity
-
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain JM105 by glutathione affinity chromatography
Q6K2E8
wild-type and natural mutant enzymes from rice leaves
Q6K2E8
isoenzyme II, recombinantly produced
-
native enzyme to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into the bacterial expression plasmid pKK233-2, expression in AHAS-deficient Escherichia coli strain MF2000
-
cloned into the bacterial expression vector pT7-7 and expressed in Escherichia coli BL21(DE3)
-
gene AHAS, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3), the enzyme contains additional 34 residues, MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGS, at the N-terminus
-
co-expression of acetolactate synthase and omega-transaminase in Escherichia coli
-
gene alsS, inducible overexpression in a constructed pta mutant strains RH35 and RH36 of Bacillus subtilis, the recombinant overexpression of the enzyme leads to increased acetolactate synthase activity and alteration of carbon flux into the acetoin biosynthesis pathway, alterations of involved enzyme activities, overview
-
gene ilvB, DNA and amino acid sequence determination and analysis
P37251
expression of wild-type and mutant enzymes via shuttle vector pECKA in Escherichia coli and in Corynebacterium glutamicum
-
expression in Escherichia coli BL21
-
expression is considerably higher from a vector that introduces a 50 residue N-terminal fusion containing an oligohistidine sequence on the large subunit
-
gene ilvH, encoding the regulatory subunit SSU, expression of wild-type and mutants, and of the selenomethionine variant
-
isozyme I subunit-encoding genes ilvB and ilvN, DNA and amino acid sequence determination and analysis, expression of His-tagged holoenzyme or individual subunits in strain BL21
-
His-tagged AHAS catalytic subunit , overexpression in Escherichia coli strain BL21(DE3)
P45261
DNA and amino acid sequence determination and analysis, genotyping
-
overexpression in Escherichia coli
-
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
O06335, O53554, P9WG39, P9WG41
expression of the His-tagged catalytic subunit
-
inducible overexpression of the His-tagged enzyme subunits in Escherichia coli strain BL21(DE3)
-
cloned into the bacterial expression vector pGEX-2T and used to transform Escherichia coli strain pGEX-2T; GST-wALS, and sulfonylurea-resistant enzyme fused with glutathione S-transferase, GST-mALS; wild-type recombinant enzyme fused with glutathione S-transferase
-
cloned into the bacterial expression vector pGEX-2T and used to transform Escherichia coli strain pGEX-2T; wild-type recombinant enzyme fused with glutathione S-transferase
-
expression in Escherichia coli strain DH5alpha
-
expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha
-
expression of wild-type and mutant GST-tagged enzymes in Escherichia coli strain BL21(DE3)
-
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; expression in Escherichia coli
Q6K2E8
expression in Glycine max
-
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
Q6K2E8
expression in Escherichia coli
-
gene ALS1, DNA and amino acid sequence determination and analysis; gene ALS2, DNA and amino acid sequence determination and analysis
Q14TG2, Q14TG4
isozyme ALS1, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetics, genotyping
-
sll1981, DNA and amino acid sequence determination and analysis, phylogenetic analysis, subcloning and expression in Escherichia coli and in Schizosaccharomyces pombe strain PR 109, functional complementation of a Schizosaccharomyces pombe mutant strain
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression level is 0.16 relative to sigA mRNA. Genome sequence of Mycobacterium tuberculosis reveals four genes encoding catalytic subunits, and one regulatory subunit, ilvN. All these genes are expressed in Mycobacterium tuberculosis growing in vitro
O06335, O53554, P9WG39, P9WG41
expression level is 0.53 relative to sigA mRNA. Genome sequence of Mycobacterium tuberculosis reveals four genes encoding catalytic subunits, and one regulatory subunit, ilvN. All these genes are expressed in Mycobacterium tuberculosis growing in culture
O06335, O53554, P9WG39, P9WG41
expression level is 0.6 relative to sigA mRNA. Genome sequence of Mycobacterium tuberculosis reveals four genes encoding catalytic subunits, and one regulatory subunit, ilvN. All these genes are expressed in Mycobacterium tuberculosis growing in vitro
O06335, O53554, P9WG39, P9WG41
expression level is 0.63 relative to sigA mRNA. Genome sequence of Mycobacterium tuberculosis reveals four genes encoding catalytic subunits, and one regulatory subunit, ilvN. All these genes are expressed in Mycobacterium tuberculosis growing in vitro
O06335, O53554, P9WG39, P9WG41
expression is upregulated in extended stationary phase, ex vivo, and in acid stress and hypoxic environments
O06335, O53554, P9WG39, P9WG41
expression level is 0.63 relative to sigA mRNA. Genome sequence of Mycobacterium tuberculosis reveals four genes encoding catalytic subunits, and one regulatory subunit, ilvN. All these genes are expressed in Mycobacterium tuberculosis growing in vitro
-
-
expression level is 0.16 relative to sigA mRNA. Genome sequence of Mycobacterium tuberculosis reveals four genes encoding catalytic subunits, and one regulatory subunit, ilvN. All these genes are expressed in Mycobacterium tuberculosis growing in vitro
-
-
expression is upregulated in extended stationary phase, ex vivo, and in acid stress and hypoxic environments
-
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A122V
-
reduced affinity for all Mg2+, thiamine diphosphate and FAD
A122V
-
naturally occuring mutation
A122V
P17597
Nicotiana tabacum plants with transplastomic expression of mutant are specifically tolerant to pyrimidinylcarboxylate, imidazolinon, and sulfonylurea/pyrimidinylcarboxylate herbicides, respectively
G121A
P17597
Nicotiana tabacum plants with transplastomic expression of mutant are specifically tolerant to pyrimidinylcarboxylate, imidazolinon, and sulfonylurea/pyrimidinylcarboxylate herbicides, respectively
P197S
-
naturally occuring mutation
P197S
P17597
Nicotiana tabacum plants with transplastomic expression of mutant are specifically tolerant to pyrimidinylcarboxylate, imidazolinon, and sulfonylurea/pyrimidinylcarboxylate herbicides, respectively
R199E
-
naturally occuring mutation
S653F
-
naturally occuring mutation
S653N
-
binds FAD more strongly than the wild-type enzyme
S653N
-
naturally occuring mutation
S653T
-
naturally occuring mutation
W574L
-
insensitive to sulfonurea herbicides
W574L
-
naturally occuring mutation
W574S
-
reduction in sensitivity to sulfonurea herbicides compared to the wild-type enzyme
W574S
-
naturally occuring mutation
K176G
P37251
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
Q487A
-
mutation diminishes decarboxylase activity but maintains the synthase activity
Q487G
-
mutation diminishes decarboxylase activity but maintains the synthase activity
Q487I
-
complete loss of synthase activity
Q487L
-
complete loss of synthase activity
A108V
-
naturally occuring mutation
A36V
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
C83A
-
about 91% of wild-type activity
C83S
-
about 126% of wild-type activity
C83T
-
about 41% of wild-type activity
D428E
-
8% activity compared to wild-type
D428N
-
8% activity compared to wild-type
E47A
-
8% activity compared to wild-type
E47A
-
about 5% of wild-type activity
E47Q
-
10% activity compared to wild-type
E47Q
-
about 5% of wild-type activity
E60A
-
about 48% of wild-type activity
E60Q
-
about 1% of wild-type activity
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
L476M
-
about 34% of wild-type activity
L476M/Q480W
-
about 47% of wild-type activity
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
M250A
-
large decrease in activity, increase in Km-value
M263A
-
about 16% of wild-type activity
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
Q110A
-
about 3% of wild-type activity
Q110E
-
about 1.5% of wild-type activity
Q110H
-
about 15% of wild-type activity
Q110N
-
about 8% of wild-type activity
Q480W
-
about 22% of wild-type activity
R269Q
-
about 0.5% of wild-type activity
R276K
-
large decrease in activity, increase in Km-value
R289K
-
about 11% of wild-type activity
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
-
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
-
slightly reduced kcat value with a moderate increase of the apparent KM of pyruvate. The specificity for 2-ketobutyrate as acceptor is not altered
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
V391A
-
about 3% of wild-type activity
V477I
-
about 8% of wild-type activity
W464A
-
naturally occuring mutation
W464L
-
decrease in activity, increase in Km-value
W464L
-
the mutant of isozyme AHAS II has lost the preference for 2-ketobutyrate as second substrate
W464L
-
naturally occuring mutation
W464Q
-
naturally occuring mutation
W464Y
-
naturally occuring mutation
W563C
Q42768
naturally occuring mutation
W563S
Q42768
naturally occuring mutation
F147A
-
4fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
F147R
-
2.5fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
L141A
-
5fold decrease in vmax value
W561R
-
30fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
F147A
-
4fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
-
F147R
-
2.5fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
-
L141A
-
5fold decrease in vmax value
-
W561R
-
30fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
-
A121T
-
naturally occuring mutation
C163S
-
labile, readlily degraded
C309S
-
labile, readlily degraded
C411A
-
no enzymic activity, no binding of FAD
C607S
-
no significant effects
D374A
-
substrate inhibition at high concentrations, strong resistance to Londax and Cadre, 10fold increase in activation efficiency for thiamine diphosphate
D374A
-
naturally occuring mutation
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
D374E/D375E
-
strong resistance to Londax and to C
D375A
-
about 10fold increase in Km-value, strong resistance to Londax
D375A
-
naturally occuring mutation
D375E
-
about 3fold reduction in Km-value, strong resistance to Londax, about 3fold increase in activation efficiency of FAD
D375E
-
naturally occuring mutation
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
F577D
-
naturally occuring mutation
F577E
-
naturally occuring mutation
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
-
60fold increase in Km-value, strong resistance to Londax and Cadre, difference in secondary structure compared to wild-type
H351Q
-
naturally occuring mutation
H392M
-
no significant effects
H487F
-
no enzymic activity, no affinity for FAD
H487L
-
no enzymic activity, no affinity for FAD
K219Q
-
no residual activity, no binding of FAD
K255F
-
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
K255F
-
naturally occuring mutation
K255Q
-
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
-
naturally occuring mutation
K299Q
-
no significant effects
M350C
-
naturally occuring mutation
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
S167A
-
73% of wild-type activity
S167F
-
inactive, mutation abolishes the binding affinity for cofactor FAD. The far-UV spectrum is similar to wild-type
S167R
-
250% of wild-type activity
S506A
-
230% of wild-type activity
S506F
-
inactive, mutation abolishes the binding affinity for cofactor FAD. The far-UV spectrum is similar to wild-type
S506R
-
183% of wild-type activity
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
S539R
-
30% of wild-type activity
S652T
-
naturally occuring mutation
V570Q
-
naturally occuring mutation
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
Q6K2E8
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
A96V
Q6K2E8
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
F180R
Q6K2E8
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
G95A
Q6K2E8
the naturally occuring mutation leads to resistance against pyrimidinyl carboxy herbicides, e.g. bispyribac-sodium
M98E
Q6K2E8
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
M98H
Q6K2E8
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides