Information on EC 2.7.2.4 - aspartate kinase

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

EC NUMBER
COMMENTARY hide
2.7.2.4
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RECOMMENDED NAME
GeneOntology No.
aspartate kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-aspartate = ADP + 4-phospho-L-aspartate
show the reaction diagram
; The enzyme from E. coli is a multifunctional protein, which also catalyses the reaction of EC 1.1.1.3 homoserine dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ectoine biosynthesis
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grixazone biosynthesis
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L-homoserine biosynthesis
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L-lysine biosynthesis I
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L-lysine biosynthesis II
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L-lysine biosynthesis III
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L-lysine biosynthesis VI
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norspermidine biosynthesis
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spermidine biosynthesis II
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threonine metabolism
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Glycine, serine and threonine metabolism
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Monobactam biosynthesis
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Cysteine and methionine metabolism
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Lysine biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
ATP:L-aspartate 4-phosphotransferase
The enzyme from Escherichia coli is a multifunctional protein, which also catalyses the reaction of EC 1.1.1.3 homoserine dehydrogenase. This is also the case for two of the four isoenzymes in Arabidopsis thaliana. The equilibrium constant strongly favours the reaction from right to left, i.e. the non-physiological direction of reaction.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-50-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
acetic acid bacteria
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
LC411
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
VB217, ATCC6051
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
strain HD100
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Manually annotated by BRENDA team
strain HD100
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
strain I110proC
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Escherichia coli ATCC 9723
9723 (ATCC)
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Manually annotated by BRENDA team
K12
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain NCIMB 8826
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain MCS10
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Manually annotated by BRENDA team
strain MCS10
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
strain AV19
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Manually annotated by BRENDA team
methylotrophic bacterium
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
no activity in Edwardsiella sp.
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Manually annotated by BRENDA team
no activity in Providencia sp.
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Manually annotated by BRENDA team
no activity in Streptomyces akiyoshiensis
producer strain of 5-hydroxy-4-oxonorvaline
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
strain 63 (ATCC 25901)
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Saccharomyces cerevisiae HT1(pIVUts31d)
strain HT1(pIVUts31d), has a feedback-resistent aspartate kinase
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Manually annotated by BRENDA team
strain SG211, contains HOM3-R7 allel, insensitive to threonine
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
Massa 03
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Manually annotated by BRENDA team
strain BHT
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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UniProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
AT-62
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
transgenic narbon bean
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Manually annotated by BRENDA team
yeasts
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Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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A 2fold increase in lysine production is observed by cloning of the ASK gene in Corynebacterium glutamicum rather than in Escherichia coli, due to the presence of lysine exporter channel which facilitates lysine extraction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + DL-threo-3-methyl aspartate
ADP + 3-methyl-4-phosphoaspartate
show the reaction diagram
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aspartokinase III
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?
ATP + L-asparagine
?
show the reaction diagram
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aspartokinase III
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?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
ATP + L-aspartate beta-hydroxamate
?
show the reaction diagram
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aspartokinase III
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?
ATP + L-aspartate beta-methyl ester
?
show the reaction diagram
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aspartokinase III
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?
ATP + L-aspartic acid 1-benzyl ester
?
show the reaction diagram
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aspartokinase III
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?
ATP + L-aspartic acid 4-benzyl ester
?
show the reaction diagram
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aspartokinase III
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?
ATP + L-aspartic acid amide
ADP + 4-phospho-L-aspartic acid amide
show the reaction diagram
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aspartokinase III
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?
ATP + N-acetyl-L-aspartate
ADP + N-acetyl-4-phospho-L-aspartate
show the reaction diagram
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aspartokinase III
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?
ATP + N-chloroacetyl-L-aspartate
ADP + N-chloroacetyl-4-phospho-L-aspartate
show the reaction diagram
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aspartokinase III
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?
ATP + N-formyl-L-aspartate
ADP + N-formyl-4-phospho-L-aspartate
show the reaction diagram
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aspartokinase III
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?
GTP + L-aspartate
GDP + 4-phospho-L-aspartate
show the reaction diagram
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r
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-hydroxy-L-norvaline
works as L-threonine analog
ADP
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competitive inhibition
aspartate-beta-semialdehyde
D-aspartate beta-hydroxamate
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D-aspartic acid 1-benzyl ester
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Diethyl aminomalonate
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diethyldicarbonate
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DL-2,6-Diaminoheptanoate
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DL-3-amino-4-hydroxybutyrate methyl ester
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DL-3-aminobutyrate
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DL-3-hydroxy-L-norvaline
L-lysine-analog
DL-meso-diaminopimelic acid
HgSO4
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15% inhibition
iodosalicylate
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20% inhibition
L-2-aminobutyrate
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competitive inhibitor
L-alanine
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no significant effect on AK activity at 5 and 20 mM
L-glutamate
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L-glutamate gamma-methyl ester
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L-homoserine
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L-isoleucine
L-leucine
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allosteric effector
L-lysine
L-Lysine ethyl ester
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L-methionine
L-norvaline
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L-threonine
L-Threonine methyl ester
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in combination with either L-lysine or L-methionine
methionine
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concerted feedback inhibition with L-threonine
N-Acetylimidazole
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N-epsilon-formyl-L-lysine
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N-ethylmaleimide
p-chloromercuribenzoate
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Rose bengal
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S-(2-aminoethyl)-L-cysteine
L-threonine-analog; works as L-lysine analog
S-2-aminoethyl-L-cysteine
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less effective on the first isoenzyme than L-lysine alone
S-adenosyl-L-methionine
succinate
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Tetranitromethane
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additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-Alanine
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10% activation at 0.33 M
Calmodulin
L-alanine
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13fold activation at 2.5 mM; 3fold activation at 2.5 mM
L-cysteine
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13fold activation at 2.5 mM; 3fold activation at 2.5 mM
L-isoleucine
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13fold activation at 2.5 mM; 3fold activation at 2.5 mM
L-leucine
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4fold activation at 2.5 mM
L-lysine
L-methionine
L-serine
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13fold activation at 2.5 mM; 3fold activation at 2.5 mM
L-threonine
L-valine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.095 - 2.037
aspartate
0.18 - 23.5
ATP
147
DL-threo-3-methyl aspartate
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pH 8.0, 25C, aspartokinase III
16
L-asparagine
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pH 8.0, 25C, aspartokinase III
0.19 - 50.1
L-aspartate
2.5
L-aspartate beta-benzyl ester
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pH 8.0, 25C, aspartokinase III
13
L-aspartate beta-hydroxamate
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pH 8.0, 25C, aspartokinase III
4.9
L-aspartate beta-methyl ester
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pH 8.0, 25C, aspartokinase III
1.8 - 50.1
L-aspartic acid
5.3
L-aspartic acid 1-benzyl ester
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pH 8.0, 25C, aspartokinase III
184
L-aspartic acid amide
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pH 8.0, 25C, aspartokinase III
48
N-acetyl-L-aspartate
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pH 8.0, 25C, aspartokinase III
68
N-Chloroacetyl-L-aspartate
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pH 8.0, 25C, aspartokinase III
41
N-formyl-L-aspartate
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pH 8.0, 25C, aspartokinase III
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.333
aspartate
Bacillus subtilis
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pH 7.0, 30C
0.31 - 56.9
ATP
0.16 - 245
L-aspartate