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
2.7.2.4
-
RECOMMENDED NAME
GeneOntology No.
aspartate kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
phospho group transfer
P61489
-
phospho group transfer
Q0KJ33, -
-
phospho group transfer
-, Q9RUL9
-
phospho group transfer
O23653, Q9LYU8, Q9S702
-
phospho group transfer
B0L9J2, -
-
phospho group transfer
P26512
-
phospho group transfer
-
-
phospho group transfer
-, Q57991
-
phospho group transfer
Deinococcus radiodurans R1, Streptomyces albulus CR1
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Cysteine and methionine metabolism
-
ectoine biosynthesis
-
Glycine, serine and threonine metabolism
-
grixazone biosynthesis
-
homoserine biosynthesis
-
Lysine biosynthesis
-
lysine biosynthesis I
-
lysine biosynthesis II
-
lysine biosynthesis III
-
lysine biosynthesis VI
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
norspermidine biosynthesis
-
spermidine biosynthesis II
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AK
-
-
-
-
AK-R7
Saccharomyces cerevisiae HT1(pIVUts31d), Saccharomyces cerevisiae SG211
-
-
-
AK-ts31d
Saccharomyces cerevisiae HT1(pIVUts31d), Saccharomyces cerevisiae SG211
-
-
-
AK2
-, O23653
-
AKbeta
P74569
-
AKbeta
Synechocystis sp. PCC6803
P74569
-
-
AKbeta
P61489
-
AKsyn
P74569
-
AKsyn
Synechocystis sp. PCC6803
P74569
-
-
Ask
-, Q0KJ33
-
Ask
Streptomyces albulus CR1
-, Q0KJ33
-
-
ASK1
-, B0L9J2
-
ASK2
-, B0L9J2
-
aspartate kinase
-
-
aspartate kinase
Q9LYU8, Q9S702
-
aspartate kinase
-
-
aspartate kinase
P26512
-
aspartate kinase
Q9RUL9
-
aspartate kinase
Q9RUL9
-
-
aspartate kinase
P0A4Z8
-
aspartate kinase
-
-
aspartate kinase
P10869
-
aspartate kinase
Saccharomyces cerevisiae HT1(pIVUts31d), Saccharomyces cerevisiae SG211
-
-
-
aspartate kinase
-
-
aspartate kinase
P61489
-
aspartate kinase
-
-
aspartate kinase
-
-
aspartate kinase
B0L9J2
-
aspartate kinase (phosphorylating)
-
-
-
-
aspartate kinase 1
Q9LYU8
-
aspartate kinase 2
-
-
aspartate kinase 3
Q9S702
-
aspartate kinase beta
P74569
-
aspartate kinase beta
Synechocystis sp. PCC6803
P74569
-
-
aspartate kinase I
-
also acts as homoserine dehydrogenase (EC 1.1.1.3)
aspartate kinase II
-
also acts as homoserine dehydrogenase (EC 1.1.1.3)
aspartate kinase III
-
-
aspartic kinase
-
-
-
-
aspartokinase
-
-
-
-
aspartokinase
-
-
-
aspartokinase
-
-
aspartokinase
-
-
aspartokinase
-
-
-
aspartokinase
Q57991
-
aspartokinase
-
-
aspartokinase
-
-
aspartokinase
-
-
aspartokinase
-, Q0KJ33
-
aspartokinase
Streptomyces albulus CR1
-, Q0KJ33
-
-
aspartokinase 1-homoserine dehydrogenase 1
-
-
aspartokinase 1-homoserine dehydrogenase 1
Escherichia coli ATCC 9723
-
-
-
aspartokinase I
-
-
aspartokinase II
-
-
aspartokinase II
Bacillus subtilis VB217
-
-
-
aspartokinase III
-
-
aspartokinase-homoserine dehydrogenase
-
-
aspartokinase-homoserine dehydrogenase
-
-
beta-aspartokinase
-
-
-
-
dap-aspartokinase
-
mesodiaminopimelate-sensitive isoenzyme
HOM3 product
P10869
-
HOM3-R7 product
-
-
HOM3-R7 product
Saccharomyces cerevisiae HT1(pIVUts31d), Saccharomyces cerevisiae SG211
-
-
-
HOM3-ts31d product
-
-
HOM3-ts31d product
Saccharomyces cerevisiae HT1(pIVUts31d), Saccharomyces cerevisiae SG211
-
-
-
LT-aspartokinase
-
lysine-threonine-sensitive isoenzyme
lysC
-
gene name
MtbAKbeta
P0A4Z8
-
Thr-sensitive aspartate kinase
P61489
-
thrA
-
gene name
CAS REGISTRY NUMBER
COMMENTARY
9012-50-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Amycolatopsis lactamdurans LC411
LC411
-
-
Manually annotated by BRENDA team
; ligated into pET 23d(+) vector and Escherichia coli strain DH10B for cloning, expression in Escherichia coli BL21 (DE3) pLysS codon+
SwissProt
Manually annotated by BRENDA team
; Saccharomyces cerevisiae M20-20D cells are transformed with A. thaliana cDNA, protein expressed and purified from Saccharomyces cerevisiae, all data refer to the recombinant yeast protein
-
-
Manually annotated by BRENDA team
ligated into pET 23d(+) vector and Escherichia coli strain DH10B for cloning, expression in Escherichia coli BL21 (DE3) pLysS codon+
UniProt
Manually annotated by BRENDA team
var. Bensheim, mutant RL4
-
-
Manually annotated by BRENDA team
Azotobacter sp.
-
-
-
Manually annotated by BRENDA team
; chimera composed of the chimeric alpha subunit that comprises the N-terminal catalytic region from Bacillus subtilis AK II and the C-terminal region from Thermus flavus; chimera composed of the chimeric alpha subunit that comprises the N-terminal catalytic region from Bacillus subtilis AK II and the C-terminal region from Thermus flavus, and the beta subunit from Thermus flavus
-
-
Manually annotated by BRENDA team
VB217, ATCC6051
-
-
Manually annotated by BRENDA team
Bacillus subtilis VB217
VB217, ATCC6051
-
-
Manually annotated by BRENDA team
strain I110proC
-
-
Manually annotated by BRENDA team
Bradyrhizobium japonicum I110proC
strain I110proC
-
-
Manually annotated by BRENDA team
ATCC 10068
-
-
Manually annotated by BRENDA team
Corynebacterium flavescens N13
N13
-
-
Manually annotated by BRENDA team
ATCC 21799, nucleotide sequence encoding the beta-subunit
SwissProt
Manually annotated by BRENDA team
expression in Escherichia coli BL21-CodonPlus(DE3)-RIL cells with pET-26b(+) vector
SwissProt
Manually annotated by BRENDA team
carrot
-
-
Manually annotated by BRENDA team
strain R1, Deinococcus radiodurans AK has a different protein structure and a different evolutionary history from Thermus thermophilus AK, the disruption mutant exhibits a similar phenotype and the functions are not different
UniProt
Manually annotated by BRENDA team
strain R1, Deinococcus radiodurans AK has a different protein structure and a different evolutionary history from Thermus thermophilus AK, the disruption mutant exhibits a similar phenotype and the functions are not different
UniProt
Manually annotated by BRENDA team
9723 (ATCC)
-
-
Manually annotated by BRENDA team
strain B
-
-
Manually annotated by BRENDA team
strain K-12
-
-
Manually annotated by BRENDA team
Tir 8, derepressed strain of K 12 and mutant Gif 108
-
-
Manually annotated by BRENDA team
Escherichia coli ATCC 9723
9723 (ATCC)
-
-
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
Manually annotated by BRENDA team
strain U112
-
-
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
barley; L. cv. Jagriti
-
-
Manually annotated by BRENDA team
strain NCIMB 8826
-
-
Manually annotated by BRENDA team
Lactobacillus plantarum NCIMB 8826
strain NCIMB 8826
-
-
Manually annotated by BRENDA team
strain MCS10
-
-
Manually annotated by BRENDA team
strain MCS10
-
-
Manually annotated by BRENDA team
Methanococcus jannaschii has only a single, monofunctional form of AK; pET-41a vector and Rosetta (DE3) Escherichia coli cells for protein expression
UniProt
Manually annotated by BRENDA team
strain AV19
-
-
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
-
-
Manually annotated by BRENDA team
strain 63 (ATCC 25901)
-
-
Manually annotated by BRENDA team
Paenibacillus polymyxa 63
strain 63 (ATCC 25901)
-
-
Manually annotated by BRENDA team
wild-type strain P-14
-
-
Manually annotated by BRENDA team
strain HT1(pIVUts31d), has a feedback-resistent aspartate kinase; strain SG211, contains HOM3-R7 allel, insensitive to threonine
-
-
Manually annotated by BRENDA team
wildtype strain 8723c, parental strain of SG211
SwissProt
Manually annotated by BRENDA team
Saccharomyces cerevisiae HT1(pIVUts31d)
strain HT1(pIVUts31d), has a feedback-resistent aspartate kinase
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae SG211
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
Streptococcus mutans BHT
strain BHT
-
-
Manually annotated by BRENDA team
strain CR1
-
-
Manually annotated by BRENDA team
strain CR1, homologous expression in Streptomyces albulus CR1, expression with pQE30 plasmid in Escherichia coli M15 (pREP4)
TrEMBL
Manually annotated by BRENDA team
Streptomyces albulus CR1
strain CR1
-
-
Manually annotated by BRENDA team
Streptomyces albulus CR1
strain CR1, homologous expression in Streptomyces albulus CR1, expression with pQE30 plasmid in Escherichia coli M15 (pREP4)
TrEMBL
Manually annotated by BRENDA team
Synechocystis sp. PCC6803
-
UniProt
Manually annotated by BRENDA team
; chimera composed of the chimeric alpha subunit that comprises the N-terminal catalytic region from Bacillus subtilis AK II and the C-terminal region from Thermus flavus; chimera composed of the chimeric alpha subunit that comprises the N-terminal catalytic region from Bacillus subtilis AK II and the C-terminal region from Thermus flavus, and the beta subunit from Thermus flavus
-
-
Manually annotated by BRENDA team
; expression in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
SwissProt
Manually annotated by BRENDA team
Thermus thermophilus AT-62
AT-62
-
-
Manually annotated by BRENDA team
transgenic narbon bean
-
-
Manually annotated by BRENDA team
Black Mexican Sweet; maize
-
-
Manually annotated by BRENDA team
Cat100-1 inbred line
-
-
Manually annotated by BRENDA team
expression in Saccharomyces cerevisiae sigma a3hu
TrEMBL
Manually annotated by BRENDA team
maize
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
aspartate + ATP
aspartyl-phosphate + ADP
show the reaction diagram
-
part of the aspartate pathway of amino acid biosynthesis, aspartate kinase activity
-
-
?
ATP + aspartate
ADP + aspartyl-phosphate
show the reaction diagram
-
-
-
-
?
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
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
B0L9J2, -
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
O23653, Q9LYU8, Q9S702
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-, O81852
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
P26512
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-, Q57991
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Q46133
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Q0KJ33, -
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
P61489
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
P74569
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
maximum velocity of the reverse reaction is only one-twelfth that of the forward reaction, but has the advantage of using commercial substrates
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first enzyme of aspartic acid metabolic pathway, leads to synthesis of lysine, threonine, methionine and isoleucine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
branched pathway for biosynthesis of isoleucine, threonine, homoserine, methionine and lysine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step of a branched biosynthetic pathway for L-lysine, L-threonine, L-isoleucine and L-methionine, regulated by the end products through feedback inhibition, the 3 aspartate kinases I, II and II are regulated by different end products
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
physiological role of aspartokinase II is to supply precursors for the amino acid pool
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step of the branched biosynthetic pathway for lysine, threonine, isoleucine and methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step in the branched biosynthetic pathway for the synthesis of L-lysine, L-methionine, L-threonine, L-isoleucine and diaminopimelic acid
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step common to the biosynthesis of L-lysine, L-threonine, isoleucine and methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step common to the biosynthesis of L-lysine, L-threonine, isoleucine and methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step common to the biosynthesis of L-lysine, L-threonine, isoleucine and methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step in the branched pathway leading to synthesis of threonine and methionine from aspartate
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first and key enzyme of the aspartate pathway leading to the biosynthesis of essential amino acids L-lysine and L-threonine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-, O81852
first and third step of the synthesis of methionine, catalyzed by a bifunctional enzyme
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first specific step in the biosynthesis of L-lysine, L-threonine and L-methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-, Q9RUL9
disruption analyes of Deinococcus radiodurans AK indicates that the AK is not used for lysine biosynthesis, but for threonine and methionine biosyntheses
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-, Q57991
L-aspartate binds to this recombinant enzyme in two different orientations
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Synechocystis sp. PCC6803
P74569
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Bacillus subtilis VB217
-
-, first specific step in the biosynthesis of L-lysine, L-threonine and L-methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Lactobacillus plantarum NCIMB 8826
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-, Q9RUL9
disruption analyes of Deinococcus radiodurans AK indicates that the AK is not used for lysine biosynthesis, but for threonine and methionine biosyntheses
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Thermus thermophilus AT-62
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Bradyrhizobium japonicum I110proC
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Escherichia coli ATCC 9723
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Streptomyces albulus CR1
Q0KJ33, -
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Escherichia coli K12
-
-, maximum velocity of the reverse reaction is only one-twelfth that of the forward reaction, but has the advantage of using commercial substrates
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Paenibacillus polymyxa 63
-
-
-
r
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
ADP + phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
P10869, -
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
-
maximum activity is achieved with 12.5 mM MgSO4 and 20 mM ATP
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
Saccharomyces cerevisiae HT1(pIVUts31d), Saccharomyces cerevisiae SG211
-
-
-
-
?
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
?
-
-
-
-
-
-
additional information
?
-
-
activity is regulated by light
-
-
-
additional information
?
-
-
D-aspartate, L-glutamate and beta-alanine are inactive as substitutes for L-aspartate in the forward reaction, in the reverse reaction ADP cannot be replaced by AMP, UDP, GDP or IDP
-
-
-
additional information
?
-
-
aspartokinase III, D-isomers of the derivatives of aspartic acid, including D-aspartate alpha-benzyl ester and D-aspartate beta-hydroxamate are not substrates regardless of whether the alpha- or the beta-carboxyl group is derivatized, L-cysteine sulfinate and 2-methyl-DL-aspartate are no substrates
-
-
-
additional information
?
-
-
no reaction observed with ITP, CTP or UTP
-
-
-
additional information
?
-
-
absolute requirement for ATP, no other nucleoside phosphates serve as phosphate donor, analogs of aspartate such as L-glutamate, DL-alpha-methyl aspartate, N-acetyl aspartate and D-aspartate are inactive as acceptors
-
-
-
additional information
?
-
-
no other natural aminoacids or D-aspartate are substrates of this reaction
-
-
-
additional information
?
-
-
aspartate analogues succinate, maleate, L-glutamate and DL-2-amino-3-phosphonopropionate have no influence on the reaction
-
-
-
additional information
?
-
-
strict requirement for ATP as a phosporylating agent, CTP and GTP are not active
-
-
-
additional information
?
-
Q46133
no isoenzymes
-
-
-
additional information
?
-
Escherichia coli K12
-
-
-
-
-
additional information
?
-
Streptococcus mutans BHT
-
strict requirement for ATP as a phosporylating agent, CTP and GTP are not active
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
aspartate + ATP
aspartyl-phosphate + ADP
show the reaction diagram
-
part of the aspartate pathway of amino acid biosynthesis
-
-
?
ATP + aspartate
ADP + aspartyl-phosphate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
P26512
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Q46133
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
O23653, Q9LYU8, Q9S702
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
P61489
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Q0KJ33, -
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
B0L9J2, -
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
P26512
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first enzyme of aspartic acid metabolic pathway, leads to synthesis of lysine, threonine, methionine and isoleucine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
branched pathway for biosynthesis of isoleucine, threonine, homoserine, methionine and lysine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step of a branched biosynthetic pathway for L-lysine, L-threonine, L-isoleucine and L-methionine, regulated by the end products through feedback inhibition, the 3 aspartate kinases I, II and II are regulated by different end products
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
physiological role of aspartokinase II is to supply precursors for the amino acid pool
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step of the branched biosynthetic pathway for lysine, threonine, isoleucine and methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step in the branched biosynthetic pathway for the synthesis of L-lysine, L-methionine, L-threonine, L-isoleucine and diaminopimelic acid
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step common to the biosynthesis of L-lysine, L-threonine, isoleucine and methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step common to the biosynthesis of L-lysine, L-threonine, isoleucine and methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step common to the biosynthesis of L-lysine, L-threonine, isoleucine and methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first step in the branched pathway leading to synthesis of threonine and methionine from aspartate
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first and key enzyme of the aspartate pathway leading to the biosynthesis of essential amino acids L-lysine and L-threonine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-, O81852
first and third step of the synthesis of methionine, catalyzed by a bifunctional enzyme
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
first specific step in the biosynthesis of L-lysine, L-threonine and L-methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-, Q9RUL9
disruption analyes of Deinococcus radiodurans AK indicates that the AK is not used for lysine biosynthesis, but for threonine and methionine biosyntheses
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-, Q57991
L-aspartate binds to this recombinant enzyme in two different orientations
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
P10869, -
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Bacillus subtilis VB217
-
first specific step in the biosynthesis of L-lysine, L-threonine and L-methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-, Q9RUL9
disruption analyes of Deinococcus radiodurans AK indicates that the AK is not used for lysine biosynthesis, but for threonine and methionine biosyntheses
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Thermus thermophilus AT-62
-
-
-
r
ATP + L-aspartate
ADP + phospho-L-aspartate
show the reaction diagram
Saccharomyces cerevisiae HT1(pIVUts31d), Saccharomyces cerevisiae SG211
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Bradyrhizobium japonicum I110proC
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Escherichia coli ATCC 9723
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Streptomyces albulus CR1
Q0KJ33, -
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Escherichia coli K12
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
Paenibacillus polymyxa 63
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
isoenzyme I is insensitive to Ca2+ and calmodulin, isoenzyme II is activated by calmodulin, the effect is further increased by Ca2+
Ca2+
-
activated by
Ca2+
-
takes part in the signal transduction pathway for the light response
Ca2+
-
activity slightly increased
Fe2+
-
can partially replace Mg2+, but to a smaller extent than Mn2+
K+
-
significantly stimulates dap-aspartokinase
K+
-
addition of 200 mM increases the reaction rate by about 40%
K+
-
activity enhanced
Mg2+
-
essential for enzyme activity, can be partially replaced by Mn2+ and to a smaller extent by Fe2+
Mg2+
-
-
Mg2+
-
required for activity
Mg2+
-, Q57991
stabilizes the negative charge density on the terminal phosphoryl group and lowers the barrier towards transfer to the beta-carboxyl group of L-aspartate
Mn2+
-
can partially replace Mg2+
additional information
-
Li+ and Na+ ions have no effect, Zn2+, Ca2+ and Co2+ cannot replace Mg2+ or Mn2+
additional information
-
Ca2+ shows a trace of activity, Zn2+ is inactive
additional information
-
does not require monovalent cations for optimum activity
additional information
-
KCl up to 500 mM does not cause any change in activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-hydroxy-L-norvaline
Q0KJ33, -
works as L-threonine analog
ADP
-
competitive inhibition
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
Q0KJ33, -
L-lysine-analog
DL-meso-diaminopimelic acid
-
aspartokinase I, noncompetitive inhibition
DL-meso-diaminopimelic acid
-
-
DL-meso-diaminopimelic acid
-
-
DL-meso-diaminopimelic acid
-
ATCC6051, aspartokinase I
EGTA
-
isoenzyme II
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
-
repression of aspartokinase gene transcription
L-isoleucine
-
no significant effect on AK activity at 5 and 20 mM
L-leucine
-
allosteric effector
L-lysine
-
repression of aspartokinase gene transcription
L-lysine
-
-
L-lysine
-
concerted feedback inhibition with L-threonine
L-lysine
-
concerted feedback inhibition with L-threonine
L-lysine
-
-
L-lysine
-
concerted feedback inhibition with L-threonine
L-lysine
-
inhibited 50% by 0.7 mM, almost completely by 5.0 mM
L-lysine
-
concerted feedback inhibition with L-threonine; L-threonine methyl ester and L-threonine amide are able to substitute for L-threonine in feedback inhibition, but the requirement for L-lysine is strict
L-lysine
-
isoenzyme I
L-lysine
-
wild-type
L-lysine
-
no significant effect on AK activity at 5 and 20 mM
L-lysine
-
no inhibition is observed; the truncated protein is no longer inhibited by lysine, even at 10 mM, wild type protein is inhibited by lysine
L-lysine
-
no inhibition is observed
L-lysine
-
2 mM, significant inhibition
L-lysine
-
inhibits the activity of ThrA2 by 87% at 1 mM and by 96% at 10 mM, no concerted inhibition by L-lysine plus L-threonine
L-lysine
-
partially inhibits the first isoenzyme
L-lysine
Q0KJ33, -
feedback resistance of Ask, more than 20% relative activity of Ask in the assay mixture even with extremely high concentrations of 100 mM L-lysine and L-threonine each, L-Lysine alone has no effect on activity; more than 20% relative activity of rAsk is detected in the assay mixture even with extremely high concentrations of L-lysine and L-threonine (100 mM each), L-lysine alone has no effect on activity
L-lysine
O23653, Q9LYU8, Q9S702
AK1 is inhibited in a synergistic manner by lysine and S-adenosyl-L-methionine, in the absence of S-adenosyl-L-methionine AK1 displays low apparent affinity for lysine compared to AK2 and AK3; AK1 is inhibited in a synergistic manner by lysine and SAM; AK2 is inhibited by lysine, SAM by itself has no effect on the enzyme activity; AK3 is inhibited only by lysine, SAM by itself has no effect on the enzyme activity
L-lysine
-
binding of L-lysine to the regulatory ACT1 domain in R-state AKIII instigates a series of changes that release a 'latch', the beta15-alphaK loop, from the catalytic domain, which in turn undergoes large rotational rearrangements, promoting tetramer formation and completion of the transition to the T-state. L-lysine-induced allosteric transition in AKIII involves both destabilizing the R-state and stabilizing the T-state tetramer. Rearrangement of the catalytic domain blocks the ATP-binding site, which is therefore the structural basis for allosteric inhibition of AKIII by L-lysine
L-lysine
B0L9J2, -
Ask2-Oh545o2 and Ask2-Oh51Ao2 have similar lysine-sensitivity properties but differ in basal activity; Ask2-Oh545o2 and Ask2-Oh51Ao2 have similar lysine-sensitivity properties but differ in basal activity, to measure inhibition of AK activity by lysine, reaction rates using 50 mM Asp substrate are measured in the presence of 5 microM to 10 mM L-lysine
L-lysine
P26512
AK is inhibited moderately by Lys, the enzyme is inhibited dramatically by simultaneous addition of Lys and Thr, dimerization of the regulatory subunit induced by Thr binding is a key step in the inhibitory mechanism of AK; feedback inhibition, inhibits moderately, simultaneous addition of lysine and threonine inhibits dramatically
L-lysine
-
L-lysine inhibits Ask_LysC only in a mixture with L-threonine
L-lysine
-
enzyme is inhibited by lysine and threonine in a concerted manner: comparison of the crystal structures between inhibitory and active forms reveal that binding inhibitors causes a conformational change to a closed inhibitory form, and the interaction between the catalytic domain in the alpha subunit and beta subunit
L-lysine
P74569
enzyme is inhibited synergistically by L-threonine and L-lysine with the binding of threonine first. In the absence of L-lysine, the enzyme displays partial inhibition by L-threonine (50% residual activity at saturation with L-threonine) with a K0.5 value of 0.7 mM
L-Lysine ethyl ester
-
-
L-methionine
-
inhibits the first isoenzyme at 5 mM
L-norvaline
-
-
L-threonine
-
repression of aspartokinase gene transcription
L-threonine
-
above 10 mM
L-threonine
-
aspartokinase II, competitive inhibition
L-threonine
-
concerted inhibition together with L-lysine
L-threonine
-
-
L-threonine
-
isoenzyme II
L-threonine
-
-
L-threonine
-
feedback inhibition
L-threonine
-
inhibition at 0.5-1.0 mM in complemented S2207A cells is variable, it does not exceed 67%
L-threonine
-
; almost insensitive to threonine
L-threonine
-
allosteric inhibition, causes a decrease in the apparent molecular mass of the enzyme, no inhibition is detected in the threonine insensitive mutant up to 50 mM threonine
L-threonine
-
in the presence of 1 mM aspartate and 2 mM ATP
L-threonine
-
no inhibitory effect at 2 mM
L-threonine
P10869, -
75% inhibition at 10 mM, 22C culture temperature, 22C assay temperature, 71% inhibition at 10 mM, 37C culture temperature, 22C assay temperature, 87% inhibition at 10 mM, 22C culture temperature, 37C assay temperature, 86% inhibition at 10 mM, 37C culture temperature, 37C assay temperature, 93% inhibition of glutathione-S-transferase fusion protein at 10 mM, 22C assay temperature, 73% inhibition of glutathione-S-transferase fusion protein at 10 mM, 37C assay temperature; reduced sensitivity to threonine inhibition, 0% inhibition at 10 mM, 22C culture temperature, 22C assay temperature, 15% inhibition at 10 mM, 37C culture temperature, 22C assay temperature, 4% inhibition at 10 mM, 22C culture temperature, 37C assay temperature, 14% inhibition at 10 mM, 37C culture temperature, 37C assay temperature; resistance to feedback inhibition, 16% inhibition at 10 mM, 22C culture temperature, 22C assay temperature, 15% inhibition at 10 mM, 37C culture temperature, 22C assay temperature, 9% inhibition at 10 mM, 22C culture temperature, 37C assay temperature, 6% inhibition at 10 mM, 37C culture temperature, 37C assay temperature, 31% inhibition of GST-fusion protein at 10 mM, 22C assay temperature, 16% inhibition of glutathione-S-transferase fusion protein at 10 mM, 37C assay temperature
L-threonine
-
represses, reduces growth rate, no concerted inhibition by L-lysine plus L-threonine
L-threonine
P61489
; feedback inhibition by the end product
L-threonine
-
some inhibition of the first isoenzyme, together with L-lysine total inhibition
L-threonine
Q0KJ33, -
feedback resistance of Ask, more than 20% relative activity of Ask in the assay mixture even with extremely high concentrations of 100 mM L-lysine and L-threonine each, L-threonine alone has no effect on activity; more than 20% activity in the rAsk is detected even with extremely high concentrations of L-lysine and L-threonine (100 mM each), L-threonine alone has no effect on activity
L-threonine
P26512
Thr alone has no effect on the inhibitory profile, the enzyme is inhibited dramatically by simultaneous addition of Lys and Thr; threonine alone has no effect, simultaneous addition of lysine and threonine inhibits dramatically
L-threonine
-, Q57991
mechanism for allosteric regulation in which the domain movements induced by L-threonine binding causes displacement of the substrates from the enzyme, resulting in a relaxed, inactive conformation
L-threonine
-
enzyme is inhibited by lysine and threonine in a concerted manner: comparison of the crystal structures between inhibitory and active forms reveal that binding inhibitors causes a conformational change to a closed inhibitory form, and the interaction between the catalytic domain in the alpha subunit and beta subunit
L-threonine
P74569
enzyme is inhibited synergistically by L-threonine and L-lysine with the binding of threonine first. In the absence of L-threonine, the enzyme is inhibited by Lys in a cooperative manner, but the inhibition requires very high concentrations of L-lysine
L-Threonine methyl ester
-
in combination with either L-lysine or L-methionine
N-Acetylimidazole
-
-
N-epsilon-formyl-L-lysine
-
-
N-ethylmaleimide
-
17% inhibition
N-ethylmaleimide
-
-
p-chloromercuribenzoate
-
-
Rose bengal
-
-
S-(2-aminoethyl)-L-cysteine
Q0KJ33, -
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
-
potentiates inhibition by lysine
S-adenosyl-L-methionine
-
inhibits the reaction by 12%
S-adenosyl-L-methionine
-
only able to inhibit AK activity of the the first isoenzyme synergistically, when present with either L-lysine or L-threonine
S-adenosyl-L-methionine
O23653, Q9LYU8, Q9S702
AK1 is inhibited in a synergistic manner by lysine and S-adenosyl-L-methionine, in the presence of S-adenosyl-L-methionine, the apparent affinity of AK1 for lysine increases considerably for lysine inhibition similar to those of AK2 and AK3
Tetranitromethane
-
-
methionine
-
concerted feedback inhibition with L-threonine
additional information
-
no inhibition with L-homoserine, L-methionine and L-isoleucine
-
additional information
-
threonine has no effect
-
additional information
-
L-methionine does not affect the enzyme by itself but at low concentrations increases the inhibition by L-lysine
-
additional information
Q46133
completely resistant to inhibition by mixtures of L-lysine and threonine
-
additional information
-
mutant RL4 is lysine-resistant
-
additional information
-
addition of lysine and threonine together at 2 mM each results in a stronger inhibition than lysine alone
-
additional information
-, Q57991
L-lysine has no effect on activity at concentrations up to 10 mM, not inhibited by L-isoleucine and L-methionine
-
additional information
-
KCl, calcium, EGTA, calmodulin, compound 48/80 and L-valine have no effect on AK activity of the first isoenzyme
-
additional information
Q0KJ33, -
Ask of Streptomyces albulus CR1 is found to be the feedback resistant enzyme, but Ask of Streptomyces albulus CR1 is also subject to feedback inhibition by a mixture of L-lysine plus L-threonine of more than 1 mM each. L-lysine or L-threonine alone has no effect on activity.
-
additional information
O23653, Q9LYU8, Q9S702
no additional inhibition is observed upon addition of Thr or Leu in the presence of 100 microM Lys and 20 microM SAM; no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK2; no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK3; the other amino acids tested (Met, Gln, Asn, Glu, Arg) have no effect on the enzyme activities at 2.5 mM either in the presence or the absence of the inhibitor Lys or Lys plus SAM
-
additional information
P26512
dimerization of the regulatory subunit by Thr binding is the critical step of inhibition
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
beta-Alanine
-
10% activation at 0.33 M
Calmodulin
-
isoenzyme II
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
-
slightly stimulatory
L-methionine
-
slightly stimulatory
L-methionine
-
displays slight activation
L-methionine
-
simulates slight increases in activity
L-serine
-
13fold activation at 2.5 mM; 3fold activation at 2.5 mM
L-threonine
-
slight activation at low concentration
L-threonine
-
0.01 mM, mutant G135A, activity 110%, mutant R150A, activity 115%
L-threonine
-
enhances activity up to 140% at 0.2 mM
L-valine
-
simulates slight increases in activity
L-valine
-
13fold activation at 2.5 mM; 3fold activation at 2.5 mM
NH4+
-
significantly stimulates dap-aspartokinase
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.095
-
aspartate
O23653, Q9LYU8, Q9S702
AK3, 30C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana
1.94
-
aspartate
O23653, Q9LYU8, Q9S702
AK2, 30C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana
2.037
-
aspartate
O23653, Q9LYU8, Q9S702
30C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana
0.18
-
ATP
-
aspartokinase I
0.26
-
ATP
-
mutant K18R
0.27
-
ATP
-
pH 7.5, 60C, mutant G177A
0.29
-
ATP
-
pH 7.5, 60C, mutant G149A
0.35
-
ATP
-
pH 7.0, 25C
0.41
-
ATP
-
pH 7.5, 60C, mutant G149A
0.42
-
ATP
-
50 mM aspartate, presence of alanine
0.43
-
ATP
-
pH 8.0, 25C
0.43
-
ATP
-
pH 7.5, 60C, mutant D174A
0.44
-
ATP
-
pH 7.5, 60C, mutant S153A
0.45
-
ATP
-
pH 7.5, 60C, mutant A157L
0.46
-
ATP
-
pH 7.5, 60C, mutant G150A
0.48
-
ATP
-
50 mM aspartate, presence of alanine
0.5
-
ATP
-
pH 7.5, 60C, wild-type and mutant G152A
0.52
-
ATP
-
pH 7.5, 60C, mutant S12A, G135A
0.56
-
ATP
-
pH 7.5, 60C, mutant T238A
0.56
-
ATP
O23653, Q9LYU8, Q9S702
; AK3, 30C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana
0.57
-
ATP
-
pH 7.5, 60C, mutant F136A
0.6
-
ATP
-
pH 7.5, 30C
0.6
-
ATP
-
pH 7.5, 60C, mutant I171A
0.61
-
ATP
-
mutant K18Q
0.63
-
ATP
-
pH 7.5, 60C, mutant D154N
0.7
-
ATP
-
mutant E254A
0.72
-
ATP
-
pH 7.5, 60C, mutant A23L
0.74
-
ATP
-
wild type
0.8
-
ATP
-
wild type, in the presence of 10 mM aspartate
0.86
-
ATP
-
pH 7.5, 60C, mutant Y8A
0.89
-
ATP
-
pH 7.5, 60C, mutant V39A
0.89
-
ATP
-
mutant K18A
0.97
-
ATP
-
pH 7.5, 60C, mutant L148A
0.98
-
ATP
-
pH 7.5, 60C, mutant A189L
0.98
-
ATP
O23653, Q9LYU8, Q9S702
AK2, 30C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana
1
-
ATP
-
pH 8.0, 37C
1
-
ATP
-
pH 7.5, isoenzyme I
1.02
-
ATP
-
pH 7.5, 60C, mutant A42S
1.05
-
ATP
-
pH 7.5, 60C, mutant D154A
1.05
-
ATP
-
mutant S23A
1.15
-
ATP
-
mutant E279A
1.2
-
ATP
-
pH 7.8, 27C
1.2
-
ATP
-
glutathione-S-transferase fusion protein, in the presence of 10 mM aspartate; threonine insensitive mutant, in the presence of 10 mM aspartate
1.26
-
ATP
-
mutant H497A
1.28
-
ATP
-
pH 7.5, 60C, mutant G73A
1.3
-
ATP
-
pH 7.8, 27C
1.3
-
ATP
-
pH 8.0, 30C
1.39
-
ATP
-
pH 7.5, 60C, mutant S41A
1.45
-
ATP
-
mutant H292Q
1.62
-
ATP
-
pH 8.0, 30C, mutant E257K/T359I
1.67
-
ATP
-
pH 7.5, isoenzyme II
1.7
-
ATP
O23653, Q9LYU8, Q9S702
; 30C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana
1.82
-
ATP
-
pH 8.0, 30C, mutant T359I
1.89
-
ATP
-
pH 8.0, 30C, mutant E257K
1.9
-
ATP
-
aspartokinase II, 27C
1.9
-
ATP
-
pH 7.5, 60C, mutant P183A
2.1
-
ATP
-
pH 7.5, 60C, mutant T47A
2.2
-
ATP
-
pH 8.1, 29C
2.2
-
ATP
-
50 mM aspartate, absence of alanine
2.35
-
ATP
-
mutant T295V
2.4
-
ATP
-
mutant R419A
2.45
-
ATP
-
pH 7.5, 60C, mutant D182A
2.56
-
ATP
-
pH 8.0, 30C, wild-type
3
-
ATP
Q0KJ33, -
wild-type; wild-type, recombinant enzyme purified to homogeneity
3.1
-
ATP
-
mutant T22A
3.36
-
ATP
-
mutant H292A
3.57
-
ATP
-
pH 7.5, 60C, mutant G10A
3.7
-
ATP
Q0KJ33, -
mutant M68V; mutant M68V, recombinant enzyme purified to homogeneity
3.8
-
ATP
-
pH 8.0, 30C
4
-
ATP
-
aspartokinase I
4.8
-
ATP
-
aspartokinase III, 27C
5.4
-
ATP
-
mutant hom3-S45
5.5
-
ATP
O81852
pH 8.0, 30C
6.5
-
ATP
-
wild type
6.5
-
ATP
-
50 mM aspartate, absence of alanine
10.4
-
ATP
-
mutant hom3-S49
12.9
-
ATP
O81852
pH 8.0, 30C, 0.5 M effector threonine
23.5
-
ATP
-
pH 7.0, 30C
147
-
DL-threo-3-methyl aspartate
-
pH 8.0, 25C, aspartokinase III
16
-
L-asparagine
-
pH 8.0, 25C, aspartokinase III
0.19
-
L-aspartate
-
pH 7.5, 60C, mutant A157L
0.27
-
L-aspartate
-
pH 7.5, 60C, mutant E202A
0.32
-
L-aspartate
-
pH 7.5, 60C, mutant Y8A, S12A
0.33
-
L-aspartate
-
pH 7.5, 60C, mutant V39A
0.34
-
L-aspartate
-
pH 7.5, 60C, mutant G177A
0.36
-
L-aspartate
-
pH 7.5, 60C, mutant G149A, G177A
0.37
-
L-aspartate
-
pH 7.5, 60C, mutant I171A
0.39
-
L-aspartate
-
pH 7.5, 60C, mutant T238A
0.41
-
L-aspartate
-
pH 7.5, 60C, mutant S41A
0.42
-
L-aspartate
-
pH 7.5, 60C, mutant G152A, P183A
0.45
-
L-aspartate
-
pH 7.5, 60C, mutant A189L
0.47
-
L-aspartate
-
pH 7.5, 60C, mutant S153A
0.51
-
L-aspartate
-
recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, asparate kinase activity
0.53
-
L-aspartate
-
pH 7.5, 60C, mutant D174A
0.6
-
L-aspartate
-
pH 8.0, 25C, aspartokinase III
0.6
-
L-aspartate
-
pH 7.5, 60C, mutant A42S
0.61
-
L-aspartate
-
pH 7.5, 60C, mutant G73A
0.63
-
L-aspartate
-
recombinant wild-type bifunctional holoenzyme, asparate kinase activity
0.65
-
L-aspartate
-
pH 7.5, 60C, mutant A23L
0.9
-
L-aspartate
-
-
1
-
L-aspartate
-
pH 7.0, 25C
1.04
-
L-aspartate
-
pH 8.0, 25C
1.095
-
L-aspartate
O23653, Q9LYU8, Q9S702
-
1.1
-
L-aspartate
-
threonine insensitive mutant, in the presence of 10 mM ATP; wildtype, in the presence of 10 mM ATP
1.2
-
L-aspartate
-
pH 7.5, 60C, mutant P183A
1.2
-
L-aspartate
-
glutathione-S-transferase fusion protein, in the presence of 10 mM ATP
1.23
-
L-aspartate
-
pH 7.5, 60C, mutant R150A, D154A
1.31
-
L-aspartate
-
pH 7.5, 60C, D182A
1.34
-
L-aspartate
-
pH 7.5, 60C, mutant G10A, G135A
1.5
-
L-aspartate
-
pH 8.0, 25C
1.5
-
L-aspartate
-
aspartokinase I
1.5
-
L-aspartate
-
-
1.5
-
L-aspartate
-
20 mM ATP, presence of alanine
1.63
-
L-aspartate
-
mutant K18R
1.8
-
L-aspartate
Q0KJ33, -
mutant M68V
2
-
L-aspartate
-
pH 7.5, isoenzyme I and II
2.037
-
L-aspartate
O23653, Q9LYU8, Q9S702
-
2.1
-
L-aspartate
-
aspartokinase II, 27C
2.1
-
L-aspartate
-
pH 7.5, 60C, mutant L148A
2.3
-
L-aspartate
-
20 mM ATP, presence of alanine
2.31
-
L-aspartate
-
pH 8.0, 30C, mutant T359I
2.33
-
L-aspartate
-
mutant E279A
2.35
-
L-aspartate
-
pH 7.5, 30C
2.6
-
L-aspartate
-
pH 8.0, 55C, in presence of inhibitor
2.6
-
L-aspartate
-
20 mM ATP, absence of alanine
2.73
-
L-aspartate
-
pH 8.0, 30C, wild-type
3
-
L-aspartate
-
aspartokinase I
3.06
-
L-aspartate
-
pH 8.0, 30C, mutant E257K
3.1
-
L-aspartate
-
pH 8.0, 30C, mutant E257K/T359I
3.19
-
L-aspartate
-
mutant T295V
3.21
-
L-aspartate
-
mutant K18A
3.25
-
L-aspartate
-
mutant R419A
4.25
-
L-aspartate
-
mutant K18Q
4.59
-
L-aspartate
-
wild type
4.7
-
L-aspartate
-
aspartokinase III, 27C
4.8
-
L-aspartate
-
-
5
-
L-aspartate
-
pH 8.0, 55C
5.29
-
L-aspartate
-
pH 7.5, 60C, mutant F136A
5.5
-
L-aspartate
-
pH 8.1, 29C
6.15
-
L-aspartate
-
20 mM ATP, absence of alanine
6.81
-
L-aspartate
-
mutant H292A
6.99
-
L-aspartate
-
mutant S23A
7.08
-
L-aspartate
-
mutant T22A
8.66
-
L-aspartate
-
mutant H497A
9.77
-
L-aspartate
-
mutant E254A
10
-
L-aspartate
-
wild type
11.3
-
L-aspartate
-
mutant hom3-S45
11.6
-
L-aspartate
O81852
pH 8.0, 30C
11.6
-
L-aspartate
-
-
11.9
-
L-aspartate
-
mutant H292Q
12.4
-
L-aspartate
-
mutant hom3-S49
16.7
-
L-aspartate
-
pH 7.8, 27C
17
-
L-aspartate
-
aspartokinase II
19.5
-
L-aspartate
-
pH 7.5, 60C, mutant T47A
21
-
L-aspartate
-
pH 7.0, 30C
21.6
-
L-aspartate
-
pH 8.0, 30C
26.4
-
L-aspartate
O81852
pH 8.0, 30C, 0.5 M effector threonine
29.7
-
L-aspartate
-
pH 8.0, 30C
50.1
-
L-aspartate
Q0KJ33, -
wild-type
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
-
L-aspartic acid
Q0KJ33, -
mutant M68V, recombinant enzyme purified to homogeneity
50.1
-
L-aspartic acid
Q0KJ33, -
wild-type, recombinant enzyme purified to homogeneity
5.3
-
L-aspartic acid 1-benzyl ester
-
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
184
-
L-aspartic acid amide
-
pH 8.0, 25C, aspartokinase III
additional information
-
additional information
-
at 37C, but not at 25C, the apparent Km for L-aspartate is highly dependent on enzyme concentration, increasing from 0.4 mM to about 50 mM. As the enzyme concentration decreases from 13.4 to 0.17 units per ml, the presence of dioxane increases apparent Km for L-aspartate
-
additional information
-
additional information
-
Km for MgCl2 3.3 mM
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.333
-
aspartate
-
pH 7.0, 30C
0.31
-
ATP
-
mutant K18R
0.41
-
ATP
-
mutant H292A
0.53
-
ATP
-
mutant K18A
0.6
-
ATP
-
mutant K18Q
1.13
-
ATP
-
mutant E279A
4.43
-
ATP
-
mutant E254A
5.55
-
ATP
-
mutant R419A
7.33
-
ATP
-
mutant H497A
8.3
-
ATP
-
mutant H292Q
8.4
-
ATP
O23653, Q9LYU8, Q9S702
; monofunctional AK3
14.5
-
ATP
O23653, Q9LYU8, Q9S702
; monofunctional AK2
15.87
-
ATP
-
wild type
19.1
-
ATP
-
mutant S23A
23.3
-
ATP
-
mutant T295V
23.4
-
ATP
O23653, Q9LYU8, Q9S702
; monofunctional AK1
49.3
-
ATP
-
wild type
56.9
-
ATP
-
mutant T22A
0.16
-
L-aspartate
-
recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, asparate kinase activity
0.3
-
L-aspartate
-
mutant K18R
0.39
-
L-aspartate
-
recombinant wild-type bifunctional holoenzyme, asparate kinase activity
0.41
-
L-aspartate
-
mutant K18A
0.54
-
L-aspartate
-
mutant K18Q
0.8
-
L-aspartate
-
pH 7.5, 60C, mutant S41A
0.967
-
L-aspartate
-
pH 7.5, 60C, mutant G135A
0.98
-
L-aspartate
-
mutant E279A
1.83
-
L-aspartate
-
pH 7.5, 60C, mutant R150A, D154A
2.17
-
L-aspartate
-
pH 7.5, 60C, mutant D154N, D182A
2.49
-
L-aspartate
-
mutant H292A
2.83
-
L-aspartate
-
pH 7.5, 60C, mutant G10A
3
-
L-aspartate
-
pH 7.5, 60C, mutant D174A
4
-
L-aspartate
-
pH 7.5, 60C, mutant E202A
4.33
-
L-aspartate
-
pH 7.5, 60C, mutant G152A, P183A
4.65
-
L-aspartate
-
mutant R419A
4.67
-
L-aspartate
-
pH 7.5, 60C, mutant A157L
5.14
-
L-aspartate
-
mutant E254A
6
-
L-aspartate
-
pH 7.5, 60C, mutant A189L
6.67
-
L-aspartate
-
pH 7.5, 60C, mutant T47A
6.92
-
L-aspartate
-
mutant H497A
7.33
-
L-aspartate
-
pH 7.5, 60C, mutant T238A
10.3
-
L-aspartate
-
mutant H292Q
10.8
-
L-aspartate
-
pH 7.5, 60C, mutant I171A
12
-
L-aspartate
-, Q57991
at 37C
12.3
-
L-aspartate
-
pH 7.5, 60C, mutant S153A
13.3
-
L-aspartate
-
pH 7.5, 60C, mutant G149A, G177A
13.8
-
L-aspartate
-
pH 7.5, 60C, mutant Y8A
14.2
-
L-aspartate
-
aspartokinase II
16.7
-
L-aspartate
-
pH 7.5, 60C, mutant F136A
17.9
-
L-aspartate
-
mutant S23A
18
-
L-aspartate
-
mutant T295V
23.2
-
L-aspartate
-
pH 7.5, 60C, mutant A42S
23.3
-
L-aspartate
-
pH 7.5, 60C, mutant L148A
24.3
-
L-aspartate
-
pH 7.5, 60C, mutant A23L
24.7
-
L-aspartate
-
pH 7.5, 60C, mutant S12A
25
-
L-aspartate
-
pH 7.5, 60C, wild-type
31.7
-
L-aspartate
-
pH 7.5, 60C, mutant G73A
32
-
L-aspartate
-
pH 7.5, 60C, mutant V39A
39.2
-
L-aspartate
-
aspartokinase III
45
-
L-aspartate
-
mutant T22A
46.6
-
L-aspartate
-
wild type
56.7
-
L-aspartate
-
aspartokinase I
227
-
L-aspartate
-
-
245
-
L-aspartate
-, Q57991
at 70C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
110
-
ATP
-
pH 8.0, 30C, mutant E257K
22040
170
-
ATP
-
pH 8.0, 30C, mutant E257K/T359I
22040
310
-
ATP
-
pH 8.0, 30C, wild-type
22040
370
-
ATP
-
pH 8.0, 30C, mutant T359I
22040
44
-
L-aspartate
-
pH 8.0, 30C, mutant E257K
12113
120
-
L-aspartate
-
pH 8.0, 30C, mutant E257K/T359I
12113
270
-
L-aspartate
-
pH 8.0, 30C, wild-type
12113
290
-
L-aspartate
-
pH 8.0, 30C, mutant T359I
12113
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
L-lysine
-
pH 7.0, 25C
1.28
-
L-lysine
-
-
10
-
L-lysine
-
pH 8.1, 29C, noncompetitive inhibition with respect to aspartate, mixed with respect to ATP
53
-
L-Malate
-
pH 8.0, 25C, aspartokinase III
32
-
L-norvaline
-
pH 8.0, 25C, aspartokinase III
0.049
-
L-threonine
-
in the presence of 1 mM aspartate and 2 mM ATP
0.091
-
L-threonine
-
in the presence of 1 mM aspartate and 2 mM ATP
0.33
-
L-threonine
-
recombinant wild-type bifunctional holoenzyme, inhibition of asparate kinase activity
1.24
-
L-threonine
-
-
1.4
-
L-threonine
-
glutathione-S-transferase fusion protein, in the presence of 10 mM aspartate and 10 mM ATP; wildtype, in the presence of 10 mM aspartate and 10 mM ATP, binds threonine in a hyperbolic manner
1.9
-
L-threonine
-
wild type, with aspartate as substrate
3.4
-
L-threonine
-
wild type, with ATP as substrate
14
-
L-threonine
-
mutant E279A, with aspartate as substrate
28
-
L-threonine
-
mutant E279A, with ATP as substrate
108
-
malonate
-
pH 8.0, 25C, aspartokinase III
159
-
succinate
-
pH 8.0, 25C, aspartokinase III
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.08
-
L-lysine
B0L9J2, -
Ask2-Oh545o2 and Ask2-Oh51Ao2; extract of transformed yeast hom3 cells by Ask2-Oh545o2 and Ask2-Oh51Ao2
1.4
-
L-lysine
-
pH 8.0, 30C, wild-type
121.5
-
L-lysine
-
pH 8.0, 30C, mutant E257K
145.4
-
L-lysine
-
pH 8.0, 30C, mutant T359I
157.2
-
L-lysine
-
pH 8.0, 30C, mutant E257K/T359I
0.3
-
L-threonine
-, Q57991
-
0.4
-
L-threonine
-
pH 8.0, 30C, mixture with L-lysine
0.7
-
L-threonine
-
pH 8.0, 30C, + 650 mM NaCl
2.9
-
L-threonine
-
pH 8.0, 30C
3.6
-
L-threonine
-
pH 8.0, 30C
3.9
-
L-threonine
-
pH 8.0, 30C, + 650 mM KCl
13.5
-
L-threonine
-
pH 8.0, 30C, + 650 mM KCl
18.7
-
L-threonine
-
pH 8.0, 30C, + 650 mM NaCl
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00036
-
-
thrA1
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
-
P10869, -
at 37C culture temperature and 22C assay temperature
0.09
-
P10869, -
at 22C culture temperature and 22C assay temperature
0.11
-
P10869, -
in the presence of 20 mM threonine
0.13
-
Q0KJ33, -
wild-type
0.16
-
P10869, -
at 37C culture temperature and 22C assay temperature
0.196
-
-
thrA2, in the presence of L-threonine
0.2
-
P10869, -
at 22C culture temperature and 22C assay temperature
0.21
-
P10869, -
at 37C culture temperature and 37C assay temperature
0.26
-
P10869, -
at 22C culture temperature and 22C assay temperature
0.27
-
P10869, -
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
-
P10869, -
at 37C culture temperature and 37C assay temperature
0.38
-
-
truncated protein, which contains only the N-terminal region
0.39
-
P10869, -
at 22C culture temperature and 37C assay temperature
0.4
-
P10869, -
at 22C culture temperature and 37C assay temperature
0.488
-
P10869, -
in the presence of 20 mM threonine
0.51
-
P10869, -
at 37C culture temperature and 22C assay temperature
0.698
-
P10869, -
-
1.12
-
P10869, -
at 37C culture temperature and 37C assay temperature
1.373
-
P10869, -
-
5.4
-
O81852
forward reaction
5.4
-
Q0KJ33, -
in the absence of a mixture of L-lysine and L-threonine, mutant I19V/M68V/T309A; mutant I19V/M68V/T309A
5.6
-
P10869, -
glutathione-S-transferase fusion protein, 22C assay temperature
5.9
-
-
wild type
10.6
-
P10869, -
glutathione-S-transferase fusion protein, 37C assay temperature
18.87
-
O81852
reverse reaction
39.05
-
-
activity after the final purification step
45.6
-
P10869, -
GST-fusion protein, 37C assay temperature
52.2
-
P10869, -
GST-fusion protein, 22C assay temperature
additional information
-
-
0.483 units/mg
additional information
-
-
18.9 units/mg
additional information
-
-
1711.0 nmol per ml/min
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
9
-
no optimum point of activity in this range
6.2
7.1
-
meso-diaminopimelate sensitive isoenzyme
7.5
-
-
-
7.5
-
-
assay at
8
-
-
assay at
8
-
P74569
assay at
8
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9.5
-
aspartokinase I, pH range for 50% activity
6.5
8.2
-
aspartokinase II, pH range for 50% activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
30
-
-
assay at
30
-
P74569
assay at
30
-
-
assay at
35
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
O81852
theoretical pI
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
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)
Neisseria meningitidis serogroup B (strain MC58)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Synechocystis sp. (strain PCC 6803 / Kazusa)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
17700
-
P61489
aspartate kinase beta, calculated from amino acid sequence
17720
-
P61489
beta subunit (Met1-Ala161), calculated from nucleotide sequence; full-length beta subunit (Met1Ala161) with a His6-tag extension at the C-terminal end, calculated
18000
-
-
beta subunit, calculated from nucleotide sequence
18000
-
-
SDS-PAGE, recombinant protein, beta-subunit (amino acids 248-255)
18500
-
-
beta subunit, calculated from nucleotide sequence
20200
-
P26512
AKbeta analytical ultracentrifugation, absence of threonine
21700
-
P61489
aspartate kinase beta, gel filtration
23000
-
P26512
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
-
P26512
AKbeta gel-filtration chromatography, addition of threonine induces dimerization
33800
-
P26512
AKbeta in presence with 5 mM L-threonine, gel filtration
36000
-
P26512
AKbeta analytical ultracentrifugation, presence of threonine
42000
-
-
SDS-PAGE, recombinant protein
42700
-
-
alpha subunit, calculated from nucleotide sequence
43200
-
-
alpha subunit, calculated from nucleotide sequence
43700
-
-
alpha subunit, calculated from nucleotide sequence
43900
-
-
alpha subunit, calculated from nucleotide sequence
44000
-
-
SDS-PAGE, recombinant protein
44300
-
-
calculated from cDNA
50000
-
-
recombinant protein, expressed in E. coli, gel filtration
50000
-
-
SDS-PAGE, recombinant protein
52400
-
-
calculated from cDNA
53200
-
O23653, Q9LYU8, Q9S702
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
-
O23653, Q9LYU8, Q9S702
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
-
O23653, Q9LYU8, Q9S702
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
58000
-
-
wild type, gel filtration
58000
-
-, Q57991
dynamic light-scattering, addition up to 4000 mM guanidine-HCl leads to dissociation of the AK dimers into monomers
58100
-
-
wild type, calculated from protein sequence
58700
-
-
wild type, SDS-PAGE
60700
-
-
alphabeta, calculated from nucleotide sequence
61200
-
-
alphabeta, calculated from nucleotide sequence
62200
-
-
alphabeta, calculated from nucleotide sequence
64200
-
-
alpha2, gel filtration
70000
-
-
gel filtration
79000
-
-
second AK isoenzyme, gel filtration
83000
-
-, Q57991
dynamic light-scattering, addition of increasing levels of guanidine-HCl up to 2000 mM causes a decrease in the AK particle size, dissociation into dimers
87800
-
-
alpha2, calculated from nucleotide sequence
90300
-
-
alpha2, beta2, gel filtration
95000
-
-
aspartokinase II
100000
-
-
gel filtration
100000
-
-
sucrose density gradient centrifugation, peak 1
110000
-
-
gel filtration
110000
-
-
aspartokinase I
113000
-
-
gel filtration, native PAGE, isoenzyme AK Late
115000
-
-
aspartokinase II, equilibrium sedimentation
116000
-
-
equilibrium ultracentrifugation
121400
-
-
alpha2, beta2, calculated from nucleotide sequence
122400
-
-
alpha2, beta2, calculated from nucleotide sequence
124400
-
-
alpha2, beta2, calculated from nucleotide sequence
125000
-
-
aspartokinase II
126000
-
-
gel filtration
127000
-
-
aspartokinase III, sedimentation equilibrium
133000
-
-
sedimentation velocity centrifugation
137000
-
-
gel filtration
140000
-
P74569
gel filtration, homodimer
150000
-
-
sucrose density gradient centrifugation, peak 2
154000
-
-, Q57991
dynamic light-scattering, crystallization
166000
-
-
in presence of KCl and L-lysine at 11C, sedimentation equilibrium
167000
-
-
first AK isoenzyme, gel filtration
169000
-
-
aspartokinase II, equilibrium sedimentation
180000
200000
-
aspartokinase devoid of homoserine dehydrogenase activity in presence of threonine, gel filtration
181000
-
-
in presence of KCl and L-lysine at 25C, sedimentation equilibrium
200000
-
-
isoenzyme II, gel filtration
230000
-
-
sucrose density gradient centrifugation, peak 3
240000
-
-
calculated from Stokes' radius
242000
-
-
gel filtration
246000
-
-
gel filtration, Superose 6
250000
-
-
aspartokinase I
253000
-
-
gel filtration, non-denaturing electrophoresis, 4-20% polyacrylamide gradient gels
254000
-
-
gel filtration
255000
-
-
gel filtration
258000
-
-
gel filtration, Superose 12
280000
-
-
gel filtration
280000
-
-
glutathione-S-transferase fusion protein, in the presence of threonine, gel filtration
297000
-
-
glutathione-S-transferase fusion protein, in the presence of threonine, blue native gel electrophoresis
298000
-
-
wild type, in the presence of threonine, gel filtration
320000
-
O81852
gel filtration, in presence of 5.0 mM L-threonine
330000
-
-
isoenzyme I, gel filtration
334000
-
-
native complex, Svedberg equation
344000
-
-
glutathione-S-transferase fusion protein, gel filtration; threonine insensitive mutant, with and without threonine in the buffer, blue native gel electrophoresis
345000
-
-
threonine insensitive mutant, with and without threonine in the buffer, gel filtration; wild type, blue native gel electrophoresis, gel filtration
346000
-
-
aspartokinase-homoserine dehydrogenase complex, sedimentation equilibrium
346000
-
-
glutathione-S-transferase fusion protein, blue native gel electrophoresis; wild type, gel filtration
358000
-
-
light scattering studies
360000
-
-
equilibrium sedimentation
470000
-
O81852
gel filtration
470000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 122000, ultracentrifugation in TES or HEPES buffer
dimer
-
2 * 50000
dimer
-
alpha2, 2 * 43900, gel filtration, calculated from nucleotide sequence
dimer
-, Q57991
dynamic light-scattering, addition of increasing levels of guanidine-HCl up to 2000 mM
dimer
Escherichia coli K12
-
2 * 122000, ultracentrifugation in TES or HEPES buffer
-
heterodimer
-
-
heterodimer
-
1 * 17000 + 1 * 43000, alpha and beta subunits, SDS-PAGE
heterodimer
-
1 * 18000 + 1 * 45000, Western blot immunoanalysis
heterodimer
-
1 * 17000 + 1 * 53000, urea treatment, SDS-PAGE
heterodimer
-
1 * 17000 + 1 * 43000, SDS-PAGE
heterodimer
-
1 * 44108 + 1 * 18145, ask alpha and ask beta, SDS-PAGE
heterodimer
Amycolatopsis lactamdurans LC411
-
1 * 44108 + 1 * 18145, ask alpha and ask beta, SDS-PAGE
-
heterodimer
Bacillus subtilis VB217
-
1 * 17000 + 1 * 43000, alpha and beta subunits, SDS-PAGE
-
heterodimer
Corynebacterium flavescens N13
-
1 * 18000 + 1 * 45000, Western blot immunoanalysis
-
heterotetramer
-
crystal structure, heterotetramer composed of two alpha subunits and two beta subunits
hexamer
-
6 * 40000, SDS-PAGE
hexamer
-
6 * 58000, gel filtration, native gel electrophoresis
hexamer
Streptococcus mutans BHT
-
6 * 40000, SDS-PAGE
-
homodimer
P26512
AKbeta is the regulatory subunit of the alpha2beta2 heterotetramer and contains two ACT domain motifs per monomer; regulatory subunit of an alpha2beta2-type AK, crystallography
homodimer
P61489
aspartate kinase beta in complex with L-threonine, X-ray crystallography
homodimer
P74569
crystal structure, dimerization involves only the catalytic domain
homodimer
-, P0A4Z8
MtbAKbeta, crystal structure
homodimer
Synechocystis sp. PCC6803
-
crystal structure, dimerization involves only the catalytic domain
-
monomer
-
1 * 50000, SDS-PAGE
monomer
-, Q57991
dynamic light-scattering, addition up to 4000 mM guanidine-HCl
oligomer
-
? * 60000, high-speed sedimentation equilibrium in 6.0 mM guanidinium chloride
oligomer
O81852
? * 93000, SDS-PAGE
pentamer
-
glutathione-S-transferase fusion protein, in the presence of threonine, gel filtration
tetramer
-
4 * 80000, aspartokinase-homoserine dehydrogenase complex, sedimentation equlibrium performed on guanidinium chloride dissolved complex; 4 * 87500, SDS-PAGE
tetramer
-
4 * 48000, SDS-PAGE
tetramer
-
2 * 17000 +2 * 43000, catalytic centre as well as the 3 types of allosteric sites reside on the alpha subunit, beta subunit may function during the folding or maturation of the enzyme, SDS-PAGE
tetramer
-
4 * 43000, aspartokinase II, equilibrium sedimentation; 4 * 66000, ultracentrifugation; 4 * 80000-120000, sedimentation in sucrose gradient in absence of threonine; 4 * 80000, aspartokinase-homoserine dehydrogenase complex, sedimentation equlibrium performed on guanidinium chloride dissolved complex; 4 * 84000, SDS-PAGE; 4 * 88000, gel filtration in 6.0 mM guanidinium chloride
tetramer
-
2 * 17000 + 2 * 47000, SDS-PAGE
tetramer
-
4 * 46000-50000, SDS-PAGE
tetramer
-
2 * 49000 + 2 * 60000, SDS-PAGE; native AK Late isoform is a tetramer which dissociates into active dimers during native gradient PAGE
tetramer
-
2 * 49000 + 2 * 60000, SDS-PAGE
tetramer
O81852
-
tetramer
-
alpha2, beta2, 2 * 42700 + 2 * 18000, gel filtration, ultracentrifugation, calculated from nucleotide sequence; alpha2, beta2, 2 * 43700 + 2 * 18500, calculated from nucleotide sequence
tetramer
-
alpha2, beta2, 2 * 42700 + 2 * 18000, gel filtration, ultracentrifugation, calculated from nucleotide sequence; alpha2, beta2, 2 * 43200 + 2 * 18000, gel filtration, ultracentrifugation, calculated from nucleotide sequence
tetramer
-, Q57991
crystallography, dynamic light-scattering, organized into a dimer of dimers, dimer interface mediated through both ACT subdomains, formation of the tetramer stabilized by the interaction of complementary residues from alpha4 of the catalytic domain
tetramer
-
crystallography
tetramer
-, Q57991
dimer of dimers
tetramer
Escherichia coli ATCC 9723
-
4 * 80000, aspartokinase-homoserine dehydrogenase complex, sedimentation equlibrium performed on guanidinium chloride dissolved complex; 4 * 87500, SDS-PAGE
-
tetramer
Escherichia coli K12
-
4 * 43000, aspartokinase II, equilibrium sedimentation; 4 * 80000-120000, sedimentation in sucrose gradient in absence of threonine; 4 * 80000, aspartokinase-homoserine dehydrogenase complex, sedimentation equlibrium performed on guanidinium chloride dissolved complex; 4 * 84000, SDS-PAGE
-
tetramer
Paenibacillus polymyxa 63
-
2 * 17000 +2 * 43000, catalytic centre as well as the 3 types of allosteric sites reside on the alpha subunit, beta subunit may function during the folding or maturation of the enzyme, SDS-PAGE
-
trimer
-
3 * 43000, SDS-PAGE
monomer or dimer
P61489
aspartate kinase beta is present in equilibrium between a monomer and dimer, ultracentrifugation
additional information
-
at 37C, but not at 25C, the active form of aspartokinase dissociates into lower molecular weight units which have markedly lower affinity for L-aspartate than the native enzyme
additional information
P26512
The regulatory subunit of AK is a monomer in the absence of Thr but becomes a dimer by adding Thr
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by the hanging-drop vapor-diffusion method, crystal structure of the regulatory subunit of AK at 1.58 A resolution in the Thr-binding form, regulatory subunit contains two ACT domain motifs per monomer and is arranged as a dimer, regulatory subunit is a monomer in the absence of Thr but becomes a dimer by adding Thr; the structure of the regulatory subiunit AKbeta complexed with threonine is determined at 1.58 A resolution, 0.2 M ammonium sulfate, 0.1 M citrate, 36%(w/v) PEG 4000, 10 mM threonine, pH 5.0, vapor diffusion, hanging drop, temperature 293 K, space group C 2 (C 1 2 1)
P26512
by sitting drop vapor-diffusion method, AKIII in the inactive T-state with bound feedback allosteric inhibitor L-lysine, to 2.8 A resolution, and in the R-state with L-aspartate and ADP, to 2.5 A resolution, unusual configuration for the regulatory ACT domains, in which ACT2 is inserted into ACT1 rather than the expected tandem repeat
-
3C20, 14% PEG4000, 0.1 M Tris, 0.8 M ammonium formate, pH 8.0, vapor diffusion, hanging drop, temperature 293 K, space group C2221, 3C1N, 0.2 M ammonium iodide, 2.2 M ammonium sulfate, pH 5.0, vapor diffusion, hanging drop, temperature 293 K, space group P212121, 3C1M, 14% PEG4000, 100 mM Tris, 800 mM ammonium formate, pH 8.0, vapor diffusion, hanging drop, temperature 293 K, space group P212121, the structure is determined under three different transition states: ternary complex with MgAMP-PNP and L-aspartate, binary complex with L-aspartate, and binary complex in the presence of its allosteric inhibitor L-threonine
-, Q57991
by hanging-drop vapor-diffusion method, in the presence of L-aspartate and MgADP, to 2.822.69 A resolution, N-terminal catalytic domain (residues 2-300) and a C-terminal regulatory domain (residues 310-470) joined through a hinge region (residues 301-309)
-, Q57991
crystal structure of the regulatory subunit of aspartate kinase from Mtb alone and in complex with threonine are determined at resolutions of 2.6 A and 2.0 A, respectively. MtbAKbeta is composed of two perpendicular non-equivalent ACT domains (aspartate kinase, chorismate mutase, and TyrA (prephenate dehydrogenase)) per monomer. Each ACT domain contains two alpha helices and four antiparallel beta strands
-, P0A4Z8
regulatory domain (AK-beta) in the presence of the potential feedback inhibitor threonine is crystallized to 1.6 A resolution. Crystal form belongs to space group P2-1-2-12-1, with unit-cell parameters a = 53.70, b = 63.43, c = 108.85 A and two molecules per asymmetric unit
-
refined at 2.55 A resolution in complex with L-lysine and L-threonine
P74569
by hanging-drop vapour-diffusion method, regulatory subunit in the presence of the inhibitor threonine, to 2.15 A resolution, crystal belongs to the cubic space group P4332 or P4132, with unit-cell parameters a = b = c = 141.8 A; by the hanging-drop vapour-diffusion method using Crystal Screen kits, the regulatory subunit (the beta subunit of Thermus thermophilus AK) is crystallized in the presence of the inhibitor threonine. Diffraction data are collected to 2.15 A at a synchrotron source. The crystal belongs to the cubic space group P4332 or P4132, with unit-cell parameters a = b = c = 141.8 A.
P61489
enzyme free or in complex with L-threonine, hanging drop vapor diffusion method, using 0.1 M sodium acetate (pH 5.0) and 1.2-2.0 M NaCl
P61489
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
10
-
stable at slight alkali to acidic pH range, most stable at about pH 7.0, unstable at high alkali pH range, losing 90% of its original activity after 30 min at 70C at pH 10.0
6
9
-
in pH regions below 6.0 and above 9.0 the enzyme activity rapidly decreases
7.5
-
-
very unstable in 10 mM tris-HCl buffer, stabilized by addition of 500 mM ammoinium sulfate
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
35
-
stable in this range
20
-
O23653, Q9LYU8, Q9S702
AK3 is highly unstable when stored at room temperature, losing 95% of its activity in 24 h. During this period of time, AK1 and AK2 retained all their activity; in 24 h, AK1 retains all its activity
45
-
-
loses 70% of its original activity after heating for 15 min
50
-
-
very heat-labile, being largely destroyed when kept for 10 min
50
-
-
about 50% of the enzyme is inactivated after 20 min
60
-
-
very rapid loss of catalytic activity above
70
85
-
very heat stable, not inactivated after 30 min at 70C, 30% of the original activity is lost after 30 min at 80C, rapid inactivation above 85C
70
-
-
AK II loses activity very rapidly with a half-life of 31.5 s; loss of activity with a half-life of 45.7 s; no loss of activity even after 1 h of heat treatment
70
-
-
AK retains the full activity after 1 h of heat treatment; loss of activity with a half-life of 45.7 s; no loss of activity even after 1 h of heat treatment
91.7
-
P61489
the melting temperature in the absence of any additive is at 91.7C
additional information
-
O23653, Q9LYU8, Q9S702
AK1 retaines all activity when stored at room temperature; AK2 retaines all activity when stored at room temperature; AK3 is highly unstable when stored at room temperature, losing 95% of its activity in 24 h; AK3 proves to be highly unstable when stored at room temperature, losing 95% of its activity in 24 h
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
pure protein , quickly frozen in N2 can be stored at -80C for several months without any loss of activity
-
pure protein, quickly frozen in N2 can be stored at -80C for several months without any loss of activity
-
aspartokinase II unstable in absence of L-lysine, both isoenzymes stablized by sulfhydryl reducing agents
-
stable up to. In the DEAE-Sephacel stage of purification, L-lysine and L-proline protect from heat inactivation
-
feedback inhibitor can partially protect from heat inactivation up to 70C
-
nonpolar L-amino acids protect from inactivation by heat and detergent and reverse the inhibition caused by feedback inhibitors L-lysine and L-threonine
-
L-lysine, L-threonine or L-methionine protects the enzymic activity against heat inactivation
-
feedback inhibitor pair protects the enzyme against heat denaturation
-
L-lysine and L-threonine partially prevents from heat inactivation
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
urea
-
enzyme is completely inactivated by 4 M
urea
Paenibacillus polymyxa 63
-
enzyme is completely inactivated by 4 M
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, HEPES buffer, pH 7.5, 1 mM Lys, 10% (v/v) glycerol, several month, without any loss of activity
-
-80C, HEPES buffer, pH 7.5, 1 mm Lys, 10% (v/v) glycerol, several months
-
-80C, stored frozen without noticeable loss of enzyme activity
O81852
4C, all activity is lost in 1 day
-
4C, refolded enzyme, no loss of activity for 24 h
-
-20C, can be stored without any noticeable loss in activity
-
use of bicine buffer and addition of sorbitol, bovine serum albumin or poly(ethyleneglycol) 6000 allows storage of the partially purified enzyme as a freeze-dried powder with relatively small loss of activity upon rehydration
-
-15C, aspartokinase II, stable in buffer containing 20% glycerol, remaining 100% active and homogenous for several months
-
-80C, 150 mM KCl, 20 mM Tris HCl, pH 7.4
-
25C, aspartokinase I, stable at room temperature either in presence of 1.0 mM L-threonine or of 0.15 M KCl
-
-20C, storage of the enzyme in the frozen state followed by subsequent thawing leads to a rapid decline in activity
-
4C, enzyme activity can be maintained for several months
-
-10C, can be stored over a period of 6 months with a 40% loss of activity, longer storage does not lead to further inactivation
-
-15C, diluted with glycerol to a final concentration of 40%, no loss of enzyme activity observed over a period of more than 1 year
-
-20C, appears to be stable over a period of several months' storage
-
4C, during 24 h of storage the loss of enzyme activity is substantial
-
4C, purified enzyme stable for at least 2 weeks in gel filtration buffer
-
-15C, dissolved in 0.05 M TES buffer containing 30% glycerol, pH 8.0, activity remains unchanged after 2.5 months
-
4C, dissolved in 0.05 M TES buffer containing 30% glycerol, pH 8.0, activity remains unchanged after 6 days
-
-70C, stored in buffer containing 200 mM KCl and 2 mg/ml bovine serum albumin, stable for more than 1 year
-
23C, more than 90% stable for up to 1 week
-
4C, stable for more than 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme, expressed in E. coli
-
native and recombinant enzyme
O81852
on anion exchange column and by gel filtration; on anion exchange column and by gel filtration; on anion exchange column and by gel filtration; weak anion exchange chromatography, affinity chromatogrphy for AK1; weak anion exchange chromatography, gel filtration; weak anion exchange chromatography, gel filtration
O23653, Q9LYU8, Q9S702
recombinant protein, expressed in Escherichia coli Gif106M1
-
VB217, aspartokinase II
-
recombinant enzyme
-
partially, 2 isoenzymes
-
by Ni2+-affinity chromatography and gel filtration; Ni2+-affinity with Ni2+-NTA resin and gel-filtration chromatogrphy
P26512
using Ni-NTA chromatography
-
aspartokinase devoid of homoserine dehydrogenase activity extracted from mutant Gif 108
-
aspartokinase III
-
aspartokinase-homoserine dehydrogenase complex
-
His-tagged AKIII by nickel affinity chromatography followed by gel filtration, more than 99%, untagged AKIII by gel filtration, more than 98%
-
by anion-exchange chromatography and gel filtration, more than 99% pure
-, Q57991
two successive chromatography steps: first a high resolution anionic exchange resin, followed by gel filtration column, the resulting protein is shown by SDS-PAGE to be more than 99% pure, concentration to 30 mg/ml by using a 10000 molecular weight cut-off Amicon concentrator
-, Q57991
using Ni-NTA chromatography
-
2 isoenzymes partially purified
-
partial; partial
P10869, -
recombinant enzyme from E. coli
-
partially purified, 29.9fold, by gel filtration
-
nickel-nitriloacetic acid (Ni-NTA) affinity chromatography; to near homogeneity
Q0KJ33, -
by nickel-affinity chromatography and gel filtration, to more than 95% homogeneity; nickel-affinity chromatography, gel-filtration FPLC column, more than 95% homogeneity of the purified subunit is verified by SDS-PAGE
P61489
recombinant enzyme, expressed in E. coli
-
extraction from cotyledons
-
using Ni-NTA chromatography
-
threonine-sensitive aspartokinase, copurified with homoserine dehydrogenase, 3 isoenzymes, threonine, lysine and lysine plus S-adenosylmethionine-sensitive, purified
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ask gene conferred to Escherichia coli DH5alpha transformants
-
operon encoding aspartokinase cloned and sequenced, introduced into auxotrophic Escherichia coli CGSC5074 and Escherichia coli X6118 and functionally expressed
-
; cDNA located on chromosome 4, cloned in Escherichia coli DH5alpha, overproduced in Escherichia coli BL21pLysS
O81852
by functional complementation of a Saccharomyces cerevisiae strain mutated in its homoserine dehydrogenase gene (hom6), expression in Escherichia coli, two of the three isolated clones are also able to complement a mutant yeast aspartate kinase gene (hom3), expression of the AK-HSDH gene in Arabidopsis thaliana (meristematic cells, leaves and stamens)
-
expression in Escherichia coli
-
ligated into pET 23d(+) vector and Escherichia coli strain DH10B for cloning, expression in Escherichia coli BL21 (DE3) pLysS codon+; ligated into pET 23d(+) vector and Escherichia coli strain DH10B for cloning, expression in Escherichia coli BL21 (DE3) pLysS codon+; ligated into pET 23d(+) vector and Escherichia coli strain DH10B for cloning, expression in Escherichia coli BL21 (DE3) pLysS codon+; ligated into pET 23d(+) vector, expressed in Escherichia coli BL21 codon (+); ligated into pET 23d(+) vector, expressed in Escherichia coli BL21 codon (+); ligated into pET 23d(+) vector, expressed in Escherichia coli BL21 codon (+)
O23653, Q9LYU8, Q9S702
expression in Escherichia coli
-
gene yclM introduced into aspartate kinase deficient Escherichia coli cells
-
aspartokinase encoded by lysC, expressed in Escherichia coli HB101
-
ask-asd operon cloned
Q46133
aspartokinase gene (ask) by cloning into an Escherichia coli/Corynebacterium glutamicum shuttle expression vector. Recombinant vector is transformed into Escherichia coli DH5alpha and then into Corynebacterium glutamicum. The induction of recombinant vector by IPTG has an inhibitory effect on cell growth due to over-expression of the cloned gene. 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
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in Escherichia coli BL21-CodonPlus(DE3)-RIL cells with pET-26b(+) vector; into vector pET-26b(+), introduced into Escherichia coli BL21-CodonPlus(DE3)-RIL cells
P26512
DR1365 gene of Deinococcus radiodurans is isolated, after PCR amplification and several steps the amplified DNA fragment is introduced into Deinococcus radiodurans ATCC13939 to generate a DR1365 disruptant.
-, Q9RUL9
both catalytic domains of the enzyme, performing each one of the enzyme activities, are expressed separately with or without the interface region, resulting in increased activity of each domain compared to the wild-type bifunctional holoenzyme, the isolated catalytic domains are no longer allosterically regulated, expression of hybrid holoenzyme AKIII-HDHI+
-
into plasmid pET15b, N-terminal His-tagged AKIII transformed into the B834 (DE3) met- strain, untagged AKIII ligated into plasmid pET3d and transformed into Escherichia coli BL21(DE3) pLysS for protein expression
-
lysC geneencoding for AKIII cloned into vector pTZ19U and expressed in the protease-deficient Escherichia coli BL21DE3
-
into vector pCR2.1-TOPO, subcloned to pUC18 for heterologous expression of thrA1 or thrA2 in Escherichia coli Gif 102
-
into pET-41a expression vector and expression in Escherichia coli Rosetta (DE3) cells
-, Q57991
pET-41a vector and Rosetta (DE3) Escherichia coli cells for protein expression
-, Q57991
expressed in Escherichia coli as a His-tagged fusion protein
-
recombinantly expressed in Escherichia coli
-
expression in Escherichia coli and as fusion protein with GST (glutathione-S-transferase) in Saccharomyces cerevisiae
-
single aspartate kinase encoded by the HOM3 gene, Escherichia coli DH5alpha as host
-
the gene is cloned into the NheI and BamHI restriction enzyme sites of the expression vector pET28 to create pET28+AKSc, expression in Escherichia coli
-
expressed as N-terminal 6 His-tagged fusion proteins under control of the T5 promoter in Escherichia coli M15(pREP4), homologous expression of wild-type and mutant M68V in Streptomyces albulus CR1; The BamHI-PstI 6.5-kb fragment is cloned and sequenced. The ApaI 1.9-kb fragment carrying the Ask genes (wild type and M68V mutant) is cloned into the pLAE003 plasmid. The resulting plasmids are used for homologous expression in Streptomyces albulus CR1. The PCR amplified fragments carrying the Ask genes (wild type and M68V mutant) with their own ribosome binding site (RBS) are cloned into the pLAE006 plasmid. The resulting plasmids are used for the homologous expression in Streptomyces albulus CR1. The pQE30 plasmid and Escherichia coli M15 (pREP4) are used to overexpress the recombinant protein.
Q0KJ33, -
expressed in Escherichia coli
P74569
2 subunits, alpha and beta, encoded by an inframe overlapping gene, askAB genes cloned and expressed in Escherichia coli GT3
-
expression in Escherichia coli
-
into the NdeI/HindIII site of pET26b(+) and introduced into Escherichia coli BL21-CodonPlus(DE3)-RIL cells; into vector pET26b(+) and introduced into Escherichia coli BL21-CodonPlus(DE3)-RIL cells
P61489
expressed in Escherichia coli as a His-tagged fusion protein
-
the monofunctional AK, Ask1 and Ask2 coding sequences are cloned using RNA from the B73 inbred, the two maize genes share a high degree of identity with each other and similar genes of other species, Ask2-Oh545o2 and Ask2-Oh51Ao2 sequences are expressed in Saccharomyces cerevisiae hom3/ura3 mutant sigma a3hu, there is one amino acid difference between the Ask2 alleles, Ask2-Oh545o2 and Ask2-Oh51Ao2 have similar lysine-sensitivity properties but differ in basal activity, the Ask2 gene is tightly linked to the QTL on chromosome 2 that is associated with a high endosperm lysine content. There is one amino acid difference in the Ask2 enzymes of Oh545o2 and Oh51Ao2.; yeast hom3/ura3 mutant sigmaa3hu was transformed with plasmids expressing the maize Ask2-Oh545o2 and Ask2-Oh51Ao2 sequences
B0L9J2, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
transcription of aspartate kinase genes is down-regulated under energy-depleted conditions formed by darkness and low sugar levels.The sugar-sensitive enhancer sequence of the AK/HSD1 promoter interacts with DPBF4 (Atb-ZIP12/EEL1) and ABI5 (AtbZIP39/DPBF1) in yeast one-hybrid system and in planta
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
I441A
-
site-directed mutagenesis
I552A
-
site-directed mutagenesis
Q443A
-
site-directed mutagenesis
Q524A
-
site-directed mutagenesis
S2207A
-
phenotype Thr- Met- Ura-
S2207A/pM1-1
-
mutant S2207A complemented with plasmid pM1-1, phenotype Thr+ Met+ Ura+
G345D
-
mutation in the beta-subunit of the ask gene
G345D
Corynebacterium flavescens N13
-
mutation in the beta-subunit of the ask gene
-
D45A
-
the inhibition of CgAK by lysine is substantially reduced in D45A mutant
E114A
P26512
changes in the inhibitory profile upon addition of threonine, monomer even with the addition of Thr; changes in the inhibitory profile upon addition of Thr, monomer even with the addition of Thr
F115A
P26512
changes in the inhibitory profile upon addition of threonine, pentamer or hexamer in the presence and in the absence of Thr; changes in the inhibitory profile upon addition of Thr, pentamer or hexamer in the presence and in the absence of Thr
G110A
P26512
mutant enzyme shows normal and negligible response to Thr and Lys, dimerized by Thr
G28A
P26512
changes in the inhibitory profile upon addition of Thr; changes in the inhibitory profile upon addition of threonine
K106A
P26512
mutant showing change in Lys response
M105A
P26512
mutant showing change in Lys response
N50A
P26512
mutant showing change in Lys response
Q49A
P26512
changes in the inhibitory profile upon addition of threonine, monomer even with the addition of Thr; changes in the inhibitory profile upon addition of Thr, monomer even with the addition of Thr
S301F
-
the S301F mutant exhibits resistance to feedback inhibition by lysine and threonine, showing activity in the presence of both lysine and threonine
T112A
P26512
changes in the inhibitory profile upon addition of threonine, monomer even with the addition of Thr; changes in the inhibitory profile upon addition of Thr, monomer even with the addition of Thr
V111A
P26512
changes in the inhibitory profile upon addition of threonine, pentamer or hexamer in the presence and in the absence of Thr; changes in the inhibitory profile upon addition of Thr, pentamer or hexamer in the presence and in the absence of Thr
V51A
P26512
mutant showing change in Lys response
C428R
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
E346A
-
mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity
E346R
-
mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
F329R
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
G323D
-
mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
H320A
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
I337P
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
I344P
-
mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity
I427P
-
mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity
L325F
-
mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
M251P
-
mutation destroys van der Waals interaction significantly which releases L-lysine inhibition
M318I
-
mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
M417I
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
N424A
-
mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity
N426A
-
mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity
Q351A
-
mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity
R305A
-
mutation destroys van der Waals interaction significantly which releases L-lysine inhibition
R416A
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
S315A
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
S338L
-
mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
S345L
-
mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
T253R
-
mutation leads to repulse interaction with Arg305 which destroys the allosteric regulation by L-lysine
T344M
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
T352I
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
V339A
-
mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
V347M
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
V349M
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
A406T
-
site-directed mutagenesis, 30fold more strongly inhibited by threonine
D34E
P10869, -
wild type background
E254A
-
9.1fold decrease in kcat for aspartate and 11fold decrease in kcat for ATP
E279A
-
kcat is decreased 47 times for aspartate and 44 times for ATP
E282D
P10869, -
feedback-resistant
G25D
-
site-directed mutagenesis, reduced affinity for its substrates aspartate and ATP
H292A
-
4.5 times increase in Km for ATP and 120 times decrease in kcat for ATP
H292Q
-
no significant differences to wild type
H497A
-
kcat is decreased 6.7fold for both substrates
K18A
-
Km values for both substrates similar to wild type
K18Q
-
Km values for both substrates similar to wild type
K18R
-
Km values for aspartate similar to wildtype, Km value for ATP 2.9fold decreased
K26I
-
site-directed mutagenesis, reduced affinity for its substrates aspartate and ATP
R419A
-
10fold decrease in kcat for aspartate and 8.9fold decrease in kcat for ATP
S23A
-
differs significantly only in the kcat/Km ratio, which is decreased 4fold for aspartate and 3.7fold for ATP
S399F
P10869, -
feedback-resistant
T22A
-
Km for ATP increases 4.2fold
T295V
-
6.7 times decrease in the kcat/Km ratio for ATP
I119V/M68V/T309
Q0KJ33, -
random mutagenesis by error-prone PCR and subsequent site-directed mutagenesis, the mutations remove the regulation from the Ask wild type enzyme and conferre a feedback-inhibition resistance
I19V/M68V/T309A
Q0KJ33, -
removes regulation from the Ask wild type enzyme and conferrs a feedback-inhibition resistance, assay mixture with 100 mM L-lysine plus 100 mM L-threonine reveals more than 80% activity
M68V
Q0KJ33, -
is almost fully resistant to feedback inhibition, increase in the catalytic activity, homologous expression reveals increase in varepsilon-poly-lysine productivity; random mutagenesis by error-prone PCR and subsequent site-directed mutagenesis, fully resistant to feedback inhibition, increase in epsilon-poly-L-lysine productivity
I119V/M68V/T309
Streptomyces albulus CR1
-
random mutagenesis by error-prone PCR and subsequent site-directed mutagenesis, the mutations remove the regulation from the Ask wild type enzyme and conferre a feedback-inhibition resistance
-
I19V/M68V/T309A
Streptomyces albulus CR1
-
removes regulation from the Ask wild type enzyme and conferrs a feedback-inhibition resistance, assay mixture with 100 mM L-lysine plus 100 mM L-threonine reveals more than 80% activity
-
M68V
Streptomyces albulus CR1
-
is almost fully resistant to feedback inhibition, increase in the catalytic activity, homologous expression reveals increase in varepsilon-poly-lysine productivity; random mutagenesis by error-prone PCR and subsequent site-directed mutagenesis, fully resistant to feedback inhibition, increase in epsilon-poly-L-lysine productivity
-
A157L
-
site-directed mutagenesis
A189L
-
site-directed mutagenesis
A23L
-
site-directed mutagenesis
A42S
-
site-directed mutagenesis
D154A
-
site-directed mutagenesis
D154N
-
site-directed mutagenesis
D174A
-
site-directed mutagenesis
D182A
-
site-directed mutagenesis
E202A
-
site-directed mutagenesis
F136A
-
site-directed mutagenesis
G10A
-
site-directed mutagenesis
G135A
-
site-directed mutagenesis
G149A
-
site-directed mutagenesis
G152A
-
site-directed mutagenesis
G177A
-
site-directed mutagenesis
G73A
-
site-directed mutagenesis
I171A
-
site-directed mutagenesis
L148A
-
site-directed mutagenesis
P183A
-
site-directed mutagenesis
R150A
-
site-directed mutagenesis
S12A
-
site-directed mutagenesis
S153A
-
site-directed mutagenesis
S41A
-
site-directed mutagenesis
T238A
-
site-directed mutagenesis
T47A
-
site-directed mutagenesis
V39A
-
site-directed mutagenesis
Y8A
-
site-directed mutagenesis
E257K
-
mutation of the conserved Glu-257 to Lys or the double mutations T359I/E257K render the enzyme insensitive to L-lysine with 86- and 112fold increases in IC50 values, respectively, when compared to the wild-type enzyme. E257K and E257K/T359I alleles exhibit a 1.2- to 1.7fold decrease in Vmax value and 2- to 6fold decrease in kcat/Km value for either substrate compared to wild-type
T359I
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mutation increases the L-lysine IC50 value by 104fold, but no substantial differences are observed in kinetic parameters except lower Km ATP value compared to the wild-type enzyme. Seed-specific expression of the feedback-resistant mutant T359I or mutant E257K results in increases of free L-threonine levels of up to 100fold in R1 soybean seed when compared to wild-type
T359I/E257K
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mutation of the conserved Glu-257 to Lys or the double mutations T359I/E257K render the enzyme insensitive to L-lysine with 86- and 112fold increases in IC50 values, respectively, when compared to the wild-type enzyme. E257K and E257K/T359I alleles exhibit a 1.2- to 1.7fold decrease in Vmax value and 2- to 6fold decrease in kcat/Km value for either substrate compared to wild-type
DR1365
-, Q9RUL9
disruption mutant does not grow in the minimal medium, Deinococcus radiodurans uses DR1365 for biosyntheses of methionine and threonine, but does not use it for lysine biosynthesis, the growth rate is lower than that of the wild type
additional information
-, Q9RUL9
AK DR1365 disruption mutant, does not grow in minimal medium, growth rate in minimal medium supplemented with methionine and threonine is identical to that supplemented with methionine, threonine and lysine, this phenotype is similar to a Thermus thermophilus AK TTC0166 disprution mutant
DR1365
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disruption mutant does not grow in the minimal medium, Deinococcus radiodurans uses DR1365 for biosyntheses of methionine and threonine, but does not use it for lysine biosynthesis, the growth rate is lower than that of the wild type
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additional information
-
AK DR1365 disruption mutant, does not grow in minimal medium, growth rate in minimal medium supplemented with methionine and threonine is identical to that supplemented with methionine, threonine and lysine, this phenotype is similar to a Thermus thermophilus AK TTC0166 disprution mutant
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Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
when renatured after treatment with 6.0 M guanidine hydrochloride 80 to 90% of the original activity regained, renaturation of isolated alpha subunits leads to a lower recovery of activity, 65%, which is increased by about 30% in presence of an equivalent amount of beta subunit
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
O81852
enzyme does not exist in animals, good target for conception of new pesticides controlling weeds, fungi and bacteria
additional information
O23653, Q9LYU8, Q9S702
upon binding to the inactive AK1Lys complex, S-adenosyl-l-methionine promotes a slow conformational transition leading to formation of a stable aspartate kinase 1LysS-adenosyl-l-methionine complex. Increase in AK1 apparent affinity for lysine in the presence of S-adenosyl-l-methionine results from the displacement of the unfavorable equilibrium between AK1 and aspartate kinase 1Lys towards the inactive form, S-adenosyl-l-methionine and Lys binding to AK1 is sequential, with Lys binding preceding S-adenosyl-l-methionine binding; upon binding to the inactive AK1-Lys complex, S-adenosyl-L-methionine promotes a slow conformational transition leading to formation of a stable aspartate kinase 1-Lys-S-adenosyl-L-methionine complex. Increase in AK1 apparent affinity for lysine in the presence of S-adenosyl-L-methionine results from the displacement of the unfavorable equilibrium between AK1 and aspartate kinase 1-Lys towards the inactive form, S-adenosyl-L-methionine and Lys binding to AK1 is sequential, with Lys binding preceding S-adenosyl-L-methionine binding
additional information
P26512
AK has biological importance, as a target candidate for developing new antifungal and antibacterial compounds, because mammals cannot biosynthesize lysine.
additional information
-, Q9RUL9
AK DR1365 is not used for lysine biosynthesis but for threonine and methionine biosynteses, AK TTC0166 in Thermus thermophilus and AK DR1365 in Deinococcus radiodurans have different protein structure and evolutionary origins, but their functions are not different
additional information
-
AK DR1365 is not used for lysine biosynthesis but for threonine and methionine biosynteses, AK TTC0166 in Thermus thermophilus and AK DR1365 in Deinococcus radiodurans have different protein structure and evolutionary origins, but their functions are not different
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additional information
-, Q57991
The absence of the aspartate biosynthetic pathway in humans makes it a good target for new pesticides and antibiotics.
nutrition
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high methionine and methionine metabolite levels are found in tobacco plants expressing bAK/D-AtCGS and bAK/T-AtCGS, this is the result of the enhanced flux of the carbon/amino skeleton towards methionine synthesis, to improve the nutritional quality of crop plants, by increasing the levels of nutritionally important essential amino acids, methionine and threonine, by expressing bAK and F-AtCGS, a significantly higher methionine level could be achieved in plants expressing bAK together with D-AtCGS.
additional information
B0L9J2, -
ASK1 and ASK2 share a high degree of identity with each other, there is one amino acid difference in the Ask2 enzymes of Oh545o2 and Oh51Ao2