Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.2.4 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

EC Number Inhibitors Comment Organism Structure
2.7.2.4 threonine
-
 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.4 Mycobacterium tuberculosis P9WPX3
-
-
2.7.2.4 Mycobacterium tuberculosis H37Rv P9WPX3
-
-

Purification (Commentary)

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

Subunits

EC Number Subunits Comment Organism
2.7.2.4 homodimer MtbAKbeta, crystal structure Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.7.2.4 aspartate kinase
-
 Mycobacterium tuberculosis
2.7.2.4 MtbAKbeta
-
 Mycobacterium tuberculosis