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Literature summary extracted from

  • Warrier, T.; Tropis, M.; Werngren, J.; Diehl, A.; Gengenbacher, M.; Schlegel, B.; Schade, M.; Oschkinat, H.; Daffe, M.; Hoffner, S.; Eddine, A.N.; Kaufmann, S.H.
    Antigen 85C inhibition restricts Mycobacterium tuberculosis growth through disruption of cord factor biosynthesis (2012), Antimicrob. Agents Chemother., 56, 1735-1743.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.122 recombinant expression as C-terminally His-tagged enzyme Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.122 2-amino-6-propyl-4,5,6,7-tetrahydro-1-benzothiophene-3-carbonitrile i.e. I3-AG85, enzyme inhibition leads to accumulation of trehalose monomycolate and disruption of the bacterial envelope, I3-AG85 also inhibits Mycobacterium tuberculosis survival in infected primary macrophages. Binding of I3-AG85 to Ag85C is similar to its binding to the artificial substrate octylthioglucoside, overview Mycobacterium tuberculosis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.122 Mycobacterium tuberculosis P9WQN9 and clinical isolates MT103 and MYC1554, dru-resistant Ag85C mutants
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2.3.1.122 Mycobacterium tuberculosis H37Rv P9WQN9 and clinical isolates MT103 and MYC1554, dru-resistant Ag85C mutants
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Synonyms

EC Number Synonyms Comment Organism
2.3.1.122 ag85C
-
Mycobacterium tuberculosis
2.3.1.122 mycoloyl transferase
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Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.3.1.122 malfunction inhibition of Ag85 protein family enzymes through substrate analogs hinders growth of mycobacteria and inhibition of Ag85C leads to accumulation of trehalose monomycolate Mycobacterium tuberculosis
2.3.1.122 physiological function the mycoloyl transferase activity of antigen 85 (Ag85) protein family, consisting of Ag85A, -B, and -C, generates trehalose dimycolate, an envelope lipid essential for Mycobacterium tuberculosis virulence, and cell wall arabinogalactan-linked mycolic acids Mycobacterium tuberculosis