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Information on EC 2.7.2.4 - aspartate kinase and Organism(s) Bacillus subtilis and UniProt Accession P08495
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2.7.2.4 aspartate kinaseIUBMB Comments
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.
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Word Map
- 2.7.2.4
- corynebacterium
- glutamicum
-
threonine-sensitive
- l-lysine
- l-threonine
- dihydrodipicolinate
-
i-homoserine
- diaminopimelate
- semialdehyde
-
feedback-resistant
-
aspartate-derived
-
feedback-insensitive
- aec
- l-isoleucine
- s-2-aminoethyl-l-cysteine
-
lysine-producing
- flavum
- thialysine
- meso-diaminopimelate
- ectoine
- synthesis
- agriculture
- medicine
- nutrition
- food industry
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aspartokinase, aspartate kinase, thra1, aspartokinase ii, aspartokinase iii, aspartokinase i, akiii, thra2, ak iii, ak ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AK
-
-
-
-
aspartate kinase (phosphorylating)
-
-
-
-
aspartic kinase
-
-
-
-
aspartokinase
-
-
-
-
beta-aspartokinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:L-aspartate 4-phosphotransferase
The enzyme from Escherichia coli is a multifunctional protein, which also catalyses the reaction of EC 1.1.1.3 homoserine dehydrogenase. This is also the case for two of the four isoenzymes in Arabidopsis thaliana. The equilibrium constant strongly favours the reaction from right to left, i.e. the non-physiological direction of reaction.
CAS REGISTRY NUMBER
COMMENTARY
9012-50-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
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
-
physiological role of aspartokinase II is to supply precursors for the amino acid pool
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first specific step in the biosynthesis of L-lysine, L-threonine and L-methionine
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
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
-
physiological role of aspartokinase II is to supply precursors for the amino acid pool
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first specific step in the biosynthesis of L-lysine, L-threonine and L-methionine
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-lysine
-
the truncated protein is no longer inhibited by lysine, even at 10 mM, wild type protein is inhibited by lysine
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18000
-
alpha2, beta2, 2 * 42700 + 2 * 18000, gel filtration, ultracentrifugation, calculated from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
alpha2, 2 * 43900, gel filtration, calculated from nucleotide sequence
heterodimer
tetramer
tetramer
-
alpha2, beta2, 2 * 42700 + 2 * 18000, gel filtration, ultracentrifugation, calculated from nucleotide sequence
tetramer
-
alpha2, beta2, 2 * 43700 + 2 * 18500, calculated from nucleotide sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G10D/G324W
construction of an engineered chimeric mutant enzyme containing the N-terminal catalytic region from Bacillus subtilis AKII and the C-terminal region from Thermus thermophilus AKII, through random mutagenesis and then screened using a high throughput synthetic RNA device which comprises of an L-lysine-sensing riboswitch and a selection module. Of three evolved aspartate kinases, the best mutant BT3 shows 160% increased in vitro activity compared to the wild-type enzyme from Bacillus subtilis. The mutant enzymes is feedback-resistant to L-lysine
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
-
very unstable in 10 mM tris-HCl buffer, stabilized by addition of 500 mM ammoinium sulfate
642339
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
functional recombinant expression of His-tagged chimeric mutant BT3 in Escherichia coli strain BL21(DE3)
gene yclM introduced into aspartate kinase deficient Escherichia coli cells
-
RENATURED/Commentary
ORGANISM
UNIPROT
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Truffa-Bachi, P.
Microbial aspartokinases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
8
509-553
1973
Azotobacter sp., Bacillus cereus, Bacillus licheniformis, Bacillus subtilis, Cereibacter sphaeroides, Corynebacterium glutamicum, Escherichia coli, Geobacillus stearothermophilus, Neurospora crassa, no activity in Edwardsiella sp., no activity in Providencia sp., Paenibacillus polymyxa, Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas putida, Rhodobacter capsulatus, Rhodocyclus tenuis, Rhodospirillum rubrum, Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium, [Brevibacterium] flavum
-
Moir, D.; Paulus, H.
Properties and subunit structure of aspartokinase II from Bacillus subtilis VB217
J. Biol. Chem.
252
4648-4654
1977
Bacillus subtilis, Bacillus subtilis VB217
Kobashi, N.; Nishiyama, M.; Yamane, H.
Characterization of aspartate kinase III of Bacillus subtilis
Biosci. Biotechnol. Biochem.
65
1391-1394
2001
Bacillus subtilis
Kato, C.; Kurihara, T.; Kobashi, N.; Yamane, H.; Nishiyama, M.
Conversion of feedback regulation in aspartate kinase by domain exchange
Biochem. Biophys. Res. Commun.
316
802-808
2004
Bacillus subtilis, Thermus thermophilus
Wang, J.; Gao, D.; Yu, X.; Li, W.; Qi, Q.
Evolution of a chimeric aspartate kinase for L-lysine production using a synthetic RNA device
Appl. Microbiol. Biotechnol.
99
8527-8536
2015
Bacillus subtilis (P08495), Bacillus subtilis, Thermus thermophilus (P61489), Thermus thermophilus, Bacillus subtilis 168 (P08495)
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