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Literature summary extracted from

  • Podust, L.M.; von Kries, J.P.; Eddine, A.N.; Kim, Y.; Yermalitskaya, L.V.; Kuehne, R.; Ouellet, H.; Warrier, T.; Altekoester, M.; Lee, J.S.; Rademann, J.; Oschkinat, H.; Kaufmann, S.H.; Waterman, M.R.
    Small-molecule scaffolds for CYP51 inhibitors identified by high-throughput screening and defined by X-ray crystallography (2007), Antimicrob. Agents Chemother., 51, 3915-3923.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.14.14.154 drug development CYP51 is a key target for fungal antibiotic therapy Mycobacterium tuberculosis
1.14.14.154 pharmacology CYP51 is a key target for fungal antibiotic therapy Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.14.154 recombinant mutant C37L/C442A in complex with alpha-ethyl-N-4-pyridinyl-benzeneacetamide, protein is mixed with a ligand dissolved in DMSO at a 100 mM concentration to obtain a final protein concentration of 0.2 mM and a final ligand concentration of 1 to 5 mM, 15-30% PEG 4000, 2-12% isopropanol, 0.1 M HEPES, pH 7.5, X-ray diffraction at 1.53 A resolution Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.154 C37L/C442A site-directed mutagenesis, structure determination Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.154 2-(benzo[d]-2,1,3-thiadiazole-4-sulfonyl)-2-amino-2-phenyl-N-(pyridinyl-4)-acetamide binding structure, overview Mycobacterium tuberculosis
1.14.14.154 alpha-ethyl-N-4-pyridinyl-benzeneacetamide binds to the non-heme iron, binding structure involving residues H259 and Y76, overview Mycobacterium tuberculosis
1.14.14.154 additional information specific inhibitor screening Mycobacterium tuberculosis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.14.154 membrane
-
 Mycobacterium tuberculosis 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.14.154 Fe2+ a cytochrome P450 enzyme, non-heme iron Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.154 additional information Mycobacterium tuberculosis CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy ?
-
 ?
1.14.14.154 additional information Mycobacterium tuberculosis H37Rv CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.154 Mycobacterium tuberculosis P9WPP9
-
-
1.14.14.154 Mycobacterium tuberculosis H37Rv P9WPP9
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.154 additional information CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy Mycobacterium tuberculosis ?
-
 ?
1.14.14.154 additional information CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy Mycobacterium tuberculosis H37Rv ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.14.154 CYP51
-
 Mycobacterium tuberculosis
1.14.14.154 sterol 14alpha-demethylase
-
 Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.154 cytochrome P450 a cytochrome P450 enzyme Mycobacterium tuberculosis