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Literature summary for 2.7.2.4 extracted from

  • Yang, Q.; Yu, K.; Yan, L.; Li, Y.; Chen, C.; Li, X.
    Structural view of the regulatory subunit of aspartate kinase from Mycobacterium tuberculosis (2011), Protein Cell, 2, 745-754.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
threonine
-
Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WPX3
-
-
Mycobacterium tuberculosis H37Rv P9WPX3
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Mycobacterium tuberculosis

Subunits

Subunits Comment Organism
homodimer MtbAKbeta, crystal structure Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
aspartate kinase
-
Mycobacterium tuberculosis
MtbAKbeta
-
Mycobacterium tuberculosis