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Literature summary for 1.8.4.10 extracted from

  • Paritala, H.; Suzuki, Y.; Carroll, K.
    Design, synthesis and evaluation of Fe-s targeted adenosine 5'-phosphosulfate reductase inhibitors (2015), Nucleosides Nucleotides Nucleic Acids, 34, 199-220 .
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
virtual ligand docking simulations with inhibitors. For 2-[(2R,3S,4R,5R)-3,4-dihydroxy-5-[6-[(2-sulfanylethyl)amino]-9H-purin-9-yl]oxolan-2-yl]ethyl phosphate, the AMP scaffold binds within the substrate-binding pocket and establishes interactions with key active site residues Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
2-[(2R,3S,4R,5R)-3,4-dihydroxy-5-[6-[(2-sulfanylethyl)amino]-9H-purin-9-yl]oxolan-2-yl]ethyl phosphate best inhibitor analyzed. The S atom is capable of establishing favorable interactions with the Fe-S cluster Mycobacterium tuberculosis
additional information analysis of inhibitors and molecular docking shows a clearly defined spacing requirement between the Fe-S targeting group and adenosine scaffold. Smaller Fe-S targeting groups are better tolerated. The S atom of the most potent inhibitor may establish a favorable interaction with an S atom in the cluster Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
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Cofactor

Cofactor Comment Organism Structure
[4Fe-4S]-center
-
 Mycobacterium tuberculosis