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Information on EC 2.7.2.4 - aspartate kinase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57991
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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: Methanocaldococcus jannaschii
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
L-aspartate binds to this recombinant enzyme in two different orientations
-
-
?
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
L-aspartate binds to this recombinant enzyme in two different orientations
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
stabilizes the negative charge density on the terminal phosphoryl group and lowers the barrier towards transfer to the beta-carboxyl group of L-aspartate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-threonine
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
additional information
L-lysine has no effect on activity at concentrations up to 10 mM, not inhibited by L-isoleucine and L-methionine
-
additional information
-
L-lysine has no effect on activity at concentrations up to 10 mM, not inhibited by L-isoleucine and L-methionine
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Methanococcus jannaschii has only a single, monofunctional form of AK; pET-41a vector and Rosetta (DE3) Escherichia coli cells for protein expression
UniProt
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58000
dynamic light-scattering, addition up to 4000 mM guanidine-HCl leads to dissociation of the AK dimers into monomers
83000
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dynamic light-scattering, addition of increasing levels of guanidine-HCl up to 2000 mM
monomer
dynamic light-scattering, addition up to 4000 mM guanidine-HCl
tetramer
tetramer
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by anion-exchange chromatography and gel filtration, more than 99% pure
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into pET-41a expression vector and expression in Escherichia coli Rosetta (DE3) cells
pET-41a vector and Rosetta (DE3) Escherichia coli cells for protein expression
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
The absence of the aspartate biosynthetic pathway in humans makes it a good target for new pesticides and antibiotics.
additional information
-
The absence of the aspartate biosynthetic pathway in humans makes it a good target for new pesticides and antibiotics.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Faehnle, C.R.; Liu, X.; Pavlovsky, A.; Viola, R.E.
The initial step in the archaeal aspartate biosynthetic pathway catalyzed by a monofunctional aspartokinase
Acta Crystallogr. Sect. F
62
962-966
2006
Methanocaldococcus jannaschii (Q57991), Methanocaldococcus jannaschii
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