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Literature summary for 2.3.1.301 extracted from

  • Sachdeva, S.; Musayev, F.; Alhamadsheh, M.; Scarsdale, J.; Wright, H.; Reynolds, K.
    Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH (2008), Chem. Biol., 15, 402-412 .
    View publication on PubMed
Search for more literature for 2.3.1.301

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type and mutant A246F in complex with inhibitors Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
A246F mutation introduces a large obstructive group into the pantetheinate channel, no detectable catalytic activity Mycobacterium tuberculosis
C112A mutation of active site residue, no detectable activity Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
1-([[(2-hydroxyethyl)disulfanyl]carbonyl]oxy)octane
-
 Mycobacterium tuberculosis
11-[[(decyldisulfanyl)carbonyl]oxy]undecanoic acid
-
 Mycobacterium tuberculosis
11-[[(decyloxy)carbonyl]disulfanyl]undecanoic acid
-
 Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WNG3
-
-
Mycobacterium tuberculosis ATCC 25618 P9WNG3
-
-

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0024
-
 pH 7.4, 23°C Mycobacterium tuberculosis 11-[[(decyloxy)carbonyl]disulfanyl]undecanoic acid
0.0027
-
 pH 7.4, 23°C Mycobacterium tuberculosis 11-[[(decyldisulfanyl)carbonyl]oxy]undecanoic acid
0.0038
-
 pH 7.4, 23°C Mycobacterium tuberculosis 1-([[(2-hydroxyethyl)disulfanyl]carbonyl]oxy)octane

General Information

General Information Comment Organism
metabolism ordering or closing of the FabH on the substrate or inhibitor is required for efficient reaction with the active site cysteine. The acyl-CoA reactant, in principle, could synchronously bind to both arms of the exposed substrate binding site. Movement to the closed form, and reaction with Cys112, would follow. CoA product released from the mouth of the pantetheinate channel would then complete the first stage of the reaction Mycobacterium tuberculosis