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Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.122 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.122 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

EC Number Organism UniProt Comment Textmining
2.3.1.122 Mycobacterium tuberculosis
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.122 2 alpha,alpha-trehalose 6-mycolate
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Mycobacterium tuberculosis alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
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?
2.3.1.122 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

EC Number Synonyms Comment Organism
2.3.1.122 ag85C
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Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.3.1.122 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