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Literature summary for 1.3.1.9 extracted from

  • Dias, M.V.; Vasconcelos, I.B.; Prado, A.M.; Fadel, V.; Basso, L.A.; de Azevedo, W.F.; Santos, D.S.
    Crystallographic studies on the binding of isonicotinyl-NAD adduct to wild-type and isoniazid resistant 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis (2007), J. Struct. Biol., 159, 369-380.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with NAD and isoniazid, hanging drop vapour diffusion method,in 50 mM HEPES, pH 7.2, sodium citrate buffer and 5-10% 2-methyl-2,4-pentanediol Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
I21V isoniazid-resistant mutant, loss of van der Waals interaction between NADH and the CD1 atom present in the valine residue leads to decrease of stability in binding of NADH in the active site of the protein Mycobacterium tuberculosis
S94A isoniazid-resistant mutant, alteration in the binding network involving a conserved water molecule and O9 atom of molecule of NADH leads to increase of the flexibility of the conserved water molecule and decrease of the affinity of NADH by protein Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
isoniazid
-
Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WGR1
-
-
Mycobacterium tuberculosis H37Rv P9WGR1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Mycobacterium tuberculosis

Subunits

Subunits Comment Organism
tetramer x-ray crystallography Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
2-trans-enoyl-ACP (CoA) reductase
-
Mycobacterium tuberculosis
InhA
-
Mycobacterium tuberculosis
NADH-dependent enoyl-acyl carrier protein reductase
-
Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NADH
-
Mycobacterium tuberculosis