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Information on EC 2.7.2.4 - aspartate kinase and Organism(s) Thermus thermophilus and UniProt Accession P61489
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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: Thermus thermophilus
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
-
-
-
-
AK
-
-
-
-
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 the branched biosynthetic pathway for lysine, threonine, isoleucine and 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 the branched biosynthetic pathway for lysine, threonine, isoleucine and methionine
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-threonine
-
0.01 mM, mutant G135A, activity 110%, mutant R150A, activity 115%
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 OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
expression in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
SwissProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17720
17720
full-length beta subunit (Met1Ala161) with a His6-tag extension at the C-terminal end, calculated
17720
beta subunit (Met1-Ala161), calculated from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
aspartate kinase beta in complex with L-threonine, X-ray crystallography
monomer or dimer
aspartate kinase beta is present in equilibrium between a monomer and dimer, ultracentrifugation
dimer
-
alpha2, 2 * 43900, gel filtration, calculated from nucleotide sequence
tetramer
tetramer
-
alpha2, beta2, 2 * 42700 + 2 * 18000, gel filtration, ultracentrifugation, calculated from nucleotide sequence
tetramer
-
alpha2, beta2, 2 * 43200 + 2 * 18000, gel filtration, ultracentrifugation, calculated from nucleotide sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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.
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
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
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 70°C at pH 10.0
642320
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
91.7
the melting temperature in the absence of any additive is at 91.7°C
70
70 - 85
-
very heat stable, not inactivated after 30 min at 70°C, 30% of the original activity is lost after 30 min at 80°C, rapid inactivation above 85°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified enzyme stable for at least 2 weeks in gel filtration buffer
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
functional recombinant expression of His-tagged chimeric mutant BT3 in Escherichia coli strain BL21(DE3)
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
2 subunits, alpha and beta, encoded by an inframe overlapping gene, askAB genes cloned and expressed in Escherichia coli GT3
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saiki, T.; Yamazumi, K.; Arima, K.
Aspartokinase of an extreme thermophile Thermus flavus partial purification and some properties
Agric. Biol. Chem.
41
1651-1655
1977
Thermus thermophilus, Thermus thermophilus AT-62
-
Kobashi, N.; Nishiyama, M.; Tanokura, M.
Kinetic and mutation analyses of aspartate kinase from Thermus flavus
J. Biosci. Bioeng.
87
739-745
1999
Thermus thermophilus
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
Yoshida, A.; Tomita, T.; Kuzuyama, T.; Nishiyama, M.
Purification, crystallization and preliminary X-ray analysis of the regulatory subunit of aspartate kinase from Thermus thermophilus
Acta Crystallogr. Sect. F
63
96-98
2007
Thermus thermophilus (P61489), Thermus thermophilus
Yoshida, A.; Tomita, T.; Kono, H.; Fushinobu, S.; Kuzuyama, T.; Nishiyama, M.
Crystal structures of the regulatory subunit of Thr-sensitive aspartate kinase from Thermus thermophilus
FEBS J.
276
3124-3136
2009
Thermus thermophilus (P61489), 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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