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Literature summary extracted from

  • Henriksson, L.M.; Unge, T.; Carlsson, J.; Aqvist, J.; Mowbray, S.L.; Jones, T.A.
    Structures of Mycobacterium tuberculosis 1-deoxy-D-xylulose-5-phosphate reductoisomerase provide new insights into catalysis (2007), J. Biol. Chem., 282, 19905-19916.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.267 expression in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.267 wild-type and mutant D151N/E222Q in various complexes with Mn2+, NADPH, and inhibotr fosmidomycin. Asymmetric unit corresponds to biological homodimer. Crystal contacts stabilize an open active site in the B molecule, the A molecule displays closed conformation Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.267 D151N/E222Q loss of catalytic ability, loss of binding of Mn2+. Crystallization data Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.267 fosmidomycin
-
 Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.267 41700
-
 2 * 41700, calculated and crystallization data Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.267 Mycobacterium tuberculosis P9WNS1
-
-
1.1.1.267 Mycobacterium tuberculosis H37Rv P9WNS1
-
-

Subunits

EC Number Subunits Comment Organism
1.1.1.267 dimer 2 * 41700, calculated and crystallization data Mycobacterium tuberculosis

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.1.1.267 0.00008
-
 pH 7.5, 22°C Mycobacterium tuberculosis fosmidomycin