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
-
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
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Cysteine and methionine metabolism
-
-
ectoine biosynthesis
-
-
Glycine, serine and threonine metabolism
-
-
grixazone biosynthesis
-
-
L-homoserine biosynthesis
-
-
L-lysine biosynthesis I
-
-
L-lysine biosynthesis II
-
-
L-lysine biosynthesis III
-
-
L-lysine biosynthesis VI
-
-
Lysine biosynthesis
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Monobactam biosynthesis
-
-
norspermidine biosynthesis
-
-
spermidine biosynthesis II
-
-
threonine metabolism
-
-
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
LC411
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Azotobacter sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
VB217, ATCC6051
-
-
Manually annotated by BRENDA team
strain HD100
-
-
Manually annotated by BRENDA team
strain HD100
-
-
Manually annotated by BRENDA team
strain I110proC
-
-
Manually annotated by BRENDA team
strain I110proC
-
-
Manually annotated by BRENDA team
ATCC 10068
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
N13
-
-
Manually annotated by BRENDA team
carrot
-
-
Manually annotated by BRENDA team
Escherichia coli ATCC 9723
9723 (ATCC)
-
-
Manually annotated by BRENDA team
K12
-
-
Manually annotated by BRENDA team
strain NCIMB 8826
-
-
Manually annotated by BRENDA team
strain NCIMB 8826
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain MCS10
-
-
Manually annotated by BRENDA team
strain MCS10
-
-
Manually annotated by BRENDA team
strain AV19
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
homozygous tobacco plants expressing bacterialAK are crossed with homozygous transgenic tobacco lines expressing F-AtCGS, T-AtCGS (lacking its N-terminus region) or D-AtCGS (lacking 90-nt of the N-terminus region)
-
-
Manually annotated by BRENDA team
no activity in Edwardsiella sp.
-
-
-
Manually annotated by BRENDA team
no activity in Providencia sp.
-
-
-
Manually annotated by BRENDA team
no activity in Streptomyces akiyoshiensis
producer strain of 5-hydroxy-4-oxonorvaline
-
-
Manually annotated by BRENDA team
rice, IAC-165 upland variety
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-
Manually annotated by BRENDA team
strain 63 (ATCC 25901)
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-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae HT1(pIVUts31d)
strain HT1(pIVUts31d), has a feedback-resistent aspartate kinase
-
-
Manually annotated by BRENDA team
strain SG211, contains HOM3-R7 allel, insensitive to threonine
-
-
Manually annotated by BRENDA team
Massa 03
-
-
Manually annotated by BRENDA team
strain BHT
-
-
Manually annotated by BRENDA team
strain BHT
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
AT-62
-
-
Manually annotated by BRENDA team
wheat
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-
Manually annotated by BRENDA team
transgenic narbon bean
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
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
-
aspartokinase III
-
-
?
ATP + L-asparagine
?
show the reaction diagram
-
aspartokinase III
-
-
?
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
-
aspartokinase III
-
-
?
ATP + L-aspartate beta-methyl ester
?
show the reaction diagram
-
aspartokinase III
-
-
?
ATP + L-aspartic acid 1-benzyl ester
?
show the reaction diagram
-
aspartokinase III
-
-
?
ATP + L-aspartic acid 4-benzyl ester
?
show the reaction diagram
-
aspartokinase III
-
-
?
ATP + L-aspartic acid amide
ADP + 4-phospho-L-aspartic acid amide
show the reaction diagram
-
aspartokinase III
-
-
?
ATP + N-acetyl-L-aspartate
ADP + N-acetyl-4-phospho-L-aspartate
show the reaction diagram
-
aspartokinase III
-
-
?
ATP + N-chloroacetyl-L-aspartate
ADP + N-chloroacetyl-4-phospho-L-aspartate
show the reaction diagram
-
aspartokinase III
-
-
?
ATP + N-formyl-L-aspartate
ADP + N-formyl-4-phospho-L-aspartate
show the reaction diagram
-
aspartokinase III
-
-
?
GTP + L-aspartate
GDP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
additional information
?
-
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
-
competitive inhibition
aspartate-beta-semialdehyde
D-aspartate beta-hydroxamate
-
-
D-aspartic acid 1-benzyl ester
-
-
Diethyl aminomalonate
-
-
diethyldicarbonate
-
-
DL-2,6-Diaminoheptanoate
-
-
DL-3-amino-4-hydroxybutyrate methyl ester
-
-
DL-3-aminobutyrate
-
-
DL-3-hydroxy-L-norvaline
L-lysine-analog
DL-meso-diaminopimelic acid
HgSO4
-
15% inhibition
iodosalicylate
-
20% inhibition
L-2-aminobutyrate
-
competitive inhibitor
L-alanine
-
no significant effect on AK activity at 5 and 20 mM
L-glutamate
-
-
L-glutamate gamma-methyl ester
-
-
L-homoserine
-
-
L-isoleucine
L-leucine
-
allosteric effector
L-lysine
L-Lysine ethyl ester
-
-
L-Malate
-
-
L-methionine
L-norvaline
-
-
L-threonine
L-Threonine methyl ester
-
in combination with either L-lysine or L-methionine
malonate
-
-
methionine
-
concerted feedback inhibition with L-threonine
N-Acetylimidazole
-
-
N-epsilon-formyl-L-lysine
-
-
N-ethylmaleimide
p-chloromercuribenzoate
-
-
Rose bengal
-
-
S-(2-aminoethyl)-L-cysteine
L-threonine-analog; works as L-lysine analog
S-2-aminoethyl-L-cysteine
-
less effective on the first isoenzyme than L-lysine alone
S-adenosyl-L-methionine
succinate
-
-
Tetranitromethane
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-Alanine
-
10% activation at 0.33 M
Calmodulin
L-alanine
-
13fold activation at 2.5 mM; 3fold activation at 2.5 mM
L-cysteine
-
13fold activation at 2.5 mM; 3fold activation at 2.5 mM
L-isoleucine
-
13fold activation at 2.5 mM; 3fold activation at 2.5 mM
L-leucine
-
4fold activation at 2.5 mM
L-lysine
L-methionine
L-serine
-
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
-
pH 8.0, 25C, aspartokinase III
16
L-asparagine
-
pH 8.0, 25C, aspartokinase III
0.19 - 50.1
L-aspartate
2.5
L-aspartate beta-benzyl ester
-
pH 8.0, 25C, aspartokinase III
13
L-aspartate beta-hydroxamate
-
pH 8.0, 25C, aspartokinase III
4.9
L-aspartate beta-methyl ester
-
pH 8.0, 25C, aspartokinase III
1.8 - 50.1
L-aspartic acid
5.3
L-aspartic acid 1-benzyl ester
-
pH 8.0, 25C, aspartokinase III
184
L-aspartic acid amide
-
pH 8.0, 25C, aspartokinase III
48
N-acetyl-L-aspartate
-
pH 8.0, 25C, aspartokinase III
68
N-Chloroacetyl-L-aspartate
-
pH 8.0, 25C, aspartokinase III
41
N-formyl-L-aspartate
-
pH 8.0, 25C, aspartokinase III
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.333
aspartate
Bacillus subtilis
-
pH 7.0, 30C
0.31 - 56.9
ATP
0.16 - 245
L-aspartate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
110 - 370
ATP
44 - 290
L-aspartate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
87
D-aspartate beta-hydroxamate
-
pH 8.0, 25C, aspartokinase III
14
D-aspartic acid 1-benzyl ester
-
pH 8.0, 25C, aspartokinase III
63
Diethyl aminomalonate
-
pH 8.0, 25C, aspartokinase III
14
DL-3-amino-4-hydroxybutyrate methyl ester
-
pH 8.0, 25C, aspartokinase III
245
DL-3-aminobutyrate
-
pH 8.0, 25C, aspartokinase III
28
L-2-aminobutyrate
-
pH 8.0, 25C, aspartokinase III
128
L-glutamate
-
pH 8.0, 25C, aspartokinase III
82
L-glutamate gamma-methyl ester
-
pH 8.0, 25C, aspartokinase III
7.7
L-homoserine
-
pH 8.0, 25C, aspartokinase III
1.1
L-leucine
-
-
0.1 - 10
L-lysine
53
L-Malate
-
pH 8.0, 25C, aspartokinase III
32
L-norvaline
-
pH 8.0, 25C, aspartokinase III
0.049 - 28
L-threonine
108
malonate
-
pH 8.0, 25C, aspartokinase III
159
succinate
-
pH 8.0, 25C, aspartokinase III
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 157.2
L-lysine
0.3 - 18.7
L-threonine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00096
-
thrA2, in the presence of L-lysine
0.0013
-
mutant S2207A
0.0064
-
wild-type
0.0068
-
mutant RL4
0.0107
-
complemented mutant A2207A/pM1-1
0.0268
-
wild type X-2180-1A
0.08
at 37C culture temperature and 22C assay temperature
0.09
at 22C culture temperature and 22C assay temperature
0.11
in the presence of 20 mM threonine
0.16
at 37C culture temperature and 22C assay temperature
0.196
-
thrA2, in the presence of L-threonine
0.2
at 22C culture temperature and 22C assay temperature
0.21
at 37C culture temperature and 37C assay temperature
0.26
at 22C culture temperature and 22C assay temperature
0.27
at 22C culture temperature and 37C assay temperature
0.289
-
thrA2, in the presence of L-isoleucine
0.29
-
thrA2, in the presence of L-methionine
0.36
at 37C culture temperature and 37C assay temperature
0.38
-
truncated protein, which contains only the N-terminal region
0.39
at 22C culture temperature and 37C assay temperature
0.4
at 22C culture temperature and 37C assay temperature
0.488
in the presence of 20 mM threonine
0.51
at 37C culture temperature and 22C assay temperature
1.12
at 37C culture temperature and 37C assay temperature
5.6
glutathione-S-transferase fusion protein, 22C assay temperature
5.9
-
wild type
10.6
glutathione-S-transferase fusion protein, 37C assay temperature
18.87
reverse reaction
39.05
-
activity after the final purification step
45.6
GST-fusion protein, 37C assay temperature
52.2
GST-fusion protein, 22C assay temperature
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
no optimum point of activity in this range
6.2 - 7.1
-
meso-diaminopimelate sensitive isoenzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.5
-
aspartokinase I, pH range for 50% activity
6.5 - 8.2
-
aspartokinase II, pH range for 50% activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.43
-
in presence of 0.1 mM L-lysine, determined by chromatofocusing
5.16
-
in absence of L-lysine, determined by chromatofocusing
6.13
theoretical pI
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Neisseria meningitidis serogroup B (strain MC58)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Synechocystis sp. (strain PCC 6803 / Kazusa)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17700
aspartate kinase beta, calculated from amino acid sequence
17720
beta subunit (Met1-Ala161), calculated from nucleotide sequence; full-length beta subunit (Met1Ala161) with a His6-tag extension at the C-terminal end, calculated
18500
-
beta subunit, calculated from nucleotide sequence
20200
AKbeta analytical ultracentrifugation, absence of threonine
21700
aspartate kinase beta, gel filtration
23000
AKbeta, gel filtration; AKbeta gel-filtration chromatography, absence of additives, somewhat larger than the mass of a monomer, addition of lysine causes no change
33300
AKbeta gel-filtration chromatography, addition of threonine induces dimerization
33800
AKbeta in presence with 5 mM L-threonine, gel filtration
36000
AKbeta analytical ultracentrifugation, presence of threonine
42000
-
SDS-PAGE, recombinant protein
43200
-
alpha subunit, calculated from nucleotide sequence
43700
-
alpha subunit, calculated from nucleotide sequence
44000
-
SDS-PAGE, recombinant protein
44300
-
calculated from cDNA
52400
-
calculated from cDNA
53200
gel filtration; monofunctional AK2, proteins are separated on a 10% polyacrylamide (w/v) slab gel under denaturing conditions and stained with Coomassie brilliant blue R-250
55100
gel filtration; monofunctional AK3, proteins are separated on a 10% polyacrylamide (w/v) slab gel under denaturing conditions and stained with Coomassie brilliant blue R-250
55900
gel filtration; monofunctional AK1, proteins are separated on a 10% polyacrylamide (w/v) slab gel under denaturing conditions and stained with Coomassie brilliant blue R-250