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Literature summary for 2.3.1.122 extracted from

  • Backus, K.M.; Boshoff, H.I.; Barry, C.S.; Boutureira, O.; Patel, M.K.; DHooge, F.; Lee, S.S.; Via, L.E.; Tahlan, K.; Barry, C.E.; Davis, B.G.
    Uptake of unnatural trehalose analogs as a reporter for Mycobacterium tuberculosis (2011), Nat. Chem. Biol., 7, 228-235.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
additional information design and synthesis of a trehalose analogue library for identification of Ag85 inhibitors, modifications of the trehalose scaffold, overview Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 alpha,alpha-trehalose 6-mycolate Mycobacterium tuberculosis
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 alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
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 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 alpha,alpha-trehalose 6-mycolate
-
 Mycobacterium tuberculosis alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
-
 ?
additional information evaluation of the substrate tolerance of Ag85 isoforms, development of a broad Ag85 substrate, overview. Modifications on every position of the sugar scaffold are tolerated, including even C-1 methyl groups at the crowded anomeric linkages, positive charges, such as in the 2-amino-trehalose and even stereochemically incorrect 2,2'-di-fluoro-alpha,beta-mannotrehalose. Even a previously reported inhibitor 6-azido-trehalose, and putative tetrahedral intermediate analogs, such as trehalose-6-phosphate, are also processed. 2,2'-dideoxy-lyxo-trehalose is no substrate Mycobacterium tuberculosis ?
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 ?

Synonyms

Synonyms Comment Organism
ag85C
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 Mycobacterium tuberculosis

General Information

General Information Comment Organism
evolution members of the Ag85 family, Ag85A, Ag85B, and Ag85C, share high sequence and structural homology characterized by an alpha,beta-hydrolase fold and a hydrophobic fibronectin-binding domain. Their active sites are highly conserved, featuring a histidine, aspartic acid or glutamic acid and serine catalytic triad, a hydrophobic tunnel for the lipids and two trehalose binding sites Mycobacterium tuberculosis