2.7.2.4: aspartate kinase
This is an abbreviated version!
For detailed information about aspartate kinase, go to the full flat file.
Word Map on EC 2.7.2.4
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2.7.2.4
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corynebacterium
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glutamicum
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threonine-sensitive
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l-lysine
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l-threonine
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dihydrodipicolinate
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i-homoserine
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diaminopimelate
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semialdehyde
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feedback-resistant
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aspartate-derived
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feedback-insensitive
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aec
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l-isoleucine
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s-2-aminoethyl-l-cysteine
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lysine-producing
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flavum
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thialysine
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meso-diaminopimelate
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ectoine
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synthesis
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agriculture
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medicine
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nutrition
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food industry
- 2.7.2.4
- corynebacterium
- glutamicum
-
threonine-sensitive
- l-lysine
- l-threonine
- dihydrodipicolinate
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i-homoserine
- diaminopimelate
- semialdehyde
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feedback-resistant
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aspartate-derived
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feedback-insensitive
- aec
- l-isoleucine
- s-2-aminoethyl-l-cysteine
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lysine-producing
- flavum
- thialysine
- meso-diaminopimelate
- ectoine
- synthesis
- agriculture
- medicine
- nutrition
- food industry
Reaction
Synonyms
AK, AK II, AK III, AK-HSDH, AK-HSDH I, AK-HSDH1, AK-HSDH2, AK-HseDH, AK-R7, AK-ts31d, AK1, AK2, AK3, AKbeta, AKII, AKIII, AKsyn, Ask, ASK1, ASK2, Ask_Ect, Ask_LysC, Asp kinase-homoserine dehydrogenase, aspartate kinase, aspartate kinase (phosphorylating), aspartate kinase 1, aspartate kinase 2, aspartate kinase 3, aspartate kinase beta, aspartate kinase I, aspartate kinase II, aspartate kinase III, aspartic kinase, aspartokinase, aspartokinase 1-homoserine dehydrogenase 1, aspartokinase 2, aspartokinase 3, aspartokinase I, aspartokinase II, aspartokinase III, aspartokinase-homoserine dehydrogenase, beta-aspartokinase, bifunctional aspartate kinase-homoserine dehydrogenase, BT, BTT, CgAK, dap-aspartokinase, HOM3 product, HOM3-R7 product, HOM3-ts31d product, HseDH, LT-aspartokinase, lysC, lysine-sensitive aspartokinase 3, More, MtbAKbeta, nspJ, Thr-sensitive aspartate kinase, thrA, thrA1, thrA2, TM_0547, XbAK
ECTree
2.7.2.4 aspartate kinaseAdvanced search results
results (
results (Subunits
Subunits on EC 2.7.2.4 - aspartate kinase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
heterodimer
heterotetramer
hexamer
homodimer
homopentamer or homohexamer
monomer
monomer or dimer
aspartate kinase beta is present in equilibrium between a monomer and dimer, ultracentrifugation
oligomer
pentamer
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glutathione-S-transferase fusion protein, in the presence of threonine, gel filtration
tetramer
additional information
dimer
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alpha2, 2 * 43900, gel filtration, calculated from nucleotide sequence
dimer
dynamic light-scattering, addition of increasing levels of guanidine-HCl up to 2000 mM
dimer
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alpha2, 2 * 43900, gel filtration, calculated from nucleotide sequence
heterodimer
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1 * 44108 + 1 * 18145, ask alpha and ask beta, SDS-PAGE
heterodimer
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1 * 44108 + 1 * 18145, ask alpha and ask beta, SDS-PAGE
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heterotetramer
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crystal structure, heterotetramer composed of two alpha subunits and two beta subunits
heterotetramer
dimer of dimers, alpha2beta2-type structure, 2 * 47000, alpha-subunit + 2 * 18000, beta-subunit, SDS-PAGE, each dimer contains two lysine binding sites, in which one site is exclusively found in the dimer with A and B chains located at the interface between alpha and beta subunits
homodimer
regulatory subunit of an alpha2beta2-type AK, crystallography
homodimer
AKbeta is the regulatory subunit of the alpha2beta2 heterotetramer and contains two ACT domain motifs per monomer
homodimer
crystal structure, dimerization involves only the catalytic domain
homodimer
aspartate kinase beta in complex with L-threonine, X-ray crystallography
homopentamer or homohexamer
5 or 6 * 81433, calculated from amino acid sequence
homopentamer or homohexamer
x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
homopentamer or homohexamer
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x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
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homopentamer or homohexamer
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x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
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homopentamer or homohexamer
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x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
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monomer
dynamic light-scattering, addition up to 4000 mM guanidine-HCl
oligomer
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? * 60000, high-speed sedimentation equilibrium in 6.0 mM guanidinium chloride
tetramer
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alpha2, beta2, 2 * 42700 + 2 * 18000, gel filtration, ultracentrifugation, calculated from nucleotide sequence
tetramer
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alpha2, beta2, 2 * 43700 + 2 * 18500, calculated from nucleotide sequence
tetramer
4 * 48030, dimer of dimers, sequence calculation and structure comparisons, three tetramers of CaAK comprise six homodimers which exhibits essentially identical overall dimeric architecture, T-state homodimeric architecture of CaAK, overview
tetramer
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4 * 80000-120000, sedimentation in sucrose gradient in absence of threonine
tetramer
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4 * 80000, aspartokinase-homoserine dehydrogenase complex, sedimentation equlibrium performed on guanidinium chloride dissolved complex
tetramer
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4 * 80000, aspartokinase-homoserine dehydrogenase complex, sedimentation equlibrium performed on guanidinium chloride dissolved complex
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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
tetramer
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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
Paenibacillus polymyxa 63 / ATCC 25901
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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
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tetramer
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alpha2, beta2, 2 * 42700 + 2 * 18000, gel filtration, ultracentrifugation, calculated from nucleotide sequence
tetramer
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alpha2, beta2, 2 * 43200 + 2 * 18000, gel filtration, ultracentrifugation, calculated from nucleotide sequence
tetramer
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native AK Late isoform is a tetramer which dissociates into active dimers during native gradient PAGE
additional information
the enzyme is composed of two domains: an N-terminal catalytic domain (kinase) domain and a C-terminal regulatory domain further comprised of two small domains belonging to the ACT domain family. Bending regions are in the vicinity of ATP binding site involved in domain movements between the catalytic and regulatory domains. Tetramer formation, overview
additional information
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the enzyme is composed of two domains: an N-terminal catalytic domain (kinase) domain and a C-terminal regulatory domain further comprised of two small domains belonging to the ACT domain family. Bending regions are in the vicinity of ATP binding site involved in domain movements between the catalytic and regulatory domains. Tetramer formation, overview
additional information
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The regulatory subunit of AK is a monomer in the absence of Thr but becomes a dimer by adding Thr
additional information
The regulatory subunit of AK is a monomer in the absence of Thr but becomes a dimer by adding Thr
additional information
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at 37°C, but not at 25°C, the active form of aspartokinase dissociates into lower molecular weight units which have markedly lower affinity for L-aspartate than the native enzyme
