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Literature summary extracted from

  • 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 (2011), Acta Crystallogr. Sect. F, 67, 380-385.
    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 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 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
-
-
-

Purification (Commentary)

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

Synonyms

EC Number Synonyms Comment Organism
2.7.2.4 aspartokinase
-
 Mycobacterium tuberculosis