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Information on EC 2.7.2.4 - aspartate kinase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WPX3

for references in articles please use BRENDA:EC2.7.2.4
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IUBMB 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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Mycobacterium tuberculosis
UNIPROT: P9WPX3
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AK
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aspartate kinase (phosphorylating)
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aspartic kinase
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aspartokinase
beta-aspartokinase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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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 hide
9012-50-4
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
MtbAKbeta, crystal structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
using Ni-NTA chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli as a His-tagged fusion protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schuldt, L.; Suchowersky, R.; Veith, K.; Mueller-Dieckmann, J.; Weiss, M.S.
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the regulatory domain of aspartokinase (Rv3709c) from Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
67
380-385
2011
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Yang, Q.; Yu, K.; Yan, L.; Li, Y.; Chen, C.; Li, X.
Structural view of the regulatory subunit of aspartate kinase from Mycobacterium tuberculosis
Protein Cell
2
745-754
2011
Mycobacterium tuberculosis (P9WPX3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPX3)
Manually annotated by BRENDA team