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Information on EC 2.2.1.6 - acetolactate synthase and Organism(s) Haemophilus influenzae and UniProt Accession P45261

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IUBMB Comments
This enzyme requires thiamine diphosphate. The reaction shown is in the pathway of biosynthesis of valine; the enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine.
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This record set is specific for:
Haemophilus influenzae
UNIPROT: P45261
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The taxonomic range for the selected organisms is: Haemophilus influenzae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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2
pyruvate
=
2-acetolactate
+
CO2
2
=
+
Synonyms
acetolactate synthase, acetohydroxy acid synthase, alpha-acetolactate synthase, ahas1, ahass, ahas2, ahas ii, acetohydroxy acid synthetase, acetohydroxy acid synthase i, ahas3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetohydroxyacid synthase
-
acetohydroxy acid synthase
-
-
-
-
acetohydroxy acid synthetase
-
-
-
-
acetohydroxyacid synthase
-
-
-
-
acetolactate pyruvate-lyase (carboxylating)
-
-
-
-
acetolactate synthetase
-
-
-
-
acetolactic synthetase
-
-
-
-
AHAS
-
-
-
-
alpha-acetohydroxy acid synthetase
-
-
-
-
alpha-acetohydroxyacid synthase
-
-
-
-
alpha-acetolactate synthase
-
-
-
-
alpha-acetolactate synthetase
-
-
-
-
alpha-ALS
-
-
-
-
GST-mALS
-
-
-
-
GST-wALS
-
-
-
-
synthase, acetolactate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
C-C bond formation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
pyruvate:pyruvate acetaldehydetransferase (decarboxylating)
This enzyme requires thiamine diphosphate. The reaction shown is in the pathway of biosynthesis of valine; the enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-45-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
AHAS catalyzes the first common step in the biosynthetic pathway of the branched-amino acids leucine, isoleucine, and valine
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sulfometuron methyl
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.2
pyruvate
pH 7.5, 37°C, recombinant enzyme
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00053
AVS-2087
Haemophilus influenzae
pH 7.5, 37°C, recombinant enzyme
0.00491
KHG20612
Haemophilus influenzae
pH 7.5, 37°C, recombinant enzyme
0.00142
KSW30191
Haemophilus influenzae
pH 7.5, 37°C, recombinant enzyme
0.2763
sulfometuron methyl
Haemophilus influenzae
pH 7.5, 37°C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.5
purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
large subunit
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
63700
x * 63700, recombinant His-tagged catalytic subunit, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 63700, recombinant His-tagged catalytic subunit, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged AHAS catalytic subunit from Escherichia coli strain BL21(DE3) to homogeneity by nickel affinity and anion exchange chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged AHAS catalytic subunit , overexpression in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Choi, K.J.; Noh, K.M.; Kim, D.E.; Ha, B.H.; Kim, E.E.; Yoon, M.Y.
Identification of the catalytic subunit of acetohydroxyacid synthase in Haemophilus influenzae and its potent inhibitors
Arch. Biochem. Biophys.
466
24-30
2007
Haemophilus influenzae (P45261), Haemophilus influenzae
Manually annotated by BRENDA team