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Literature summary extracted from

  • Tan, L.P.; Wu, H.; Yang, P.Y.; Kalesh, K.A.; Zhang, X.; Hu, M.; Srinivasan, R.; Yao, S.Q.
    High-throughput discovery of Mycobacterium tuberculosis protein tyrosine phosphatase B (MptpB) inhibitors using click chemistry (2009), Org. Lett., 11, 5102-5105.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.3.48 drug development MptpB is a promising target for anti-tuberculosis drug development Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.48 F1S-6C-W11
-
 Mycobacterium tuberculosis
3.1.3.48 H1-5C-W11
-
 Mycobacterium tuberculosis
3.1.3.48 additional information PTP bidentate inhibitor library synthesis and screening, overview. The bidentate inhibitors have three components: 1. the warheads, alkyne-containing N-phenyloxamic acids that are cell-permeable, potent bioisosteric phosphotyrosine mimics, 2. a variety of different types of building blocks that act as the secondary-site binders, and 3. azide-containing linkers of different lengths joining the warhead and the building blocks, overview Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.48 Mycobacterium tuberculosis
-
-
-

Synonyms

EC Number Synonyms Comment Organism
3.1.3.48 More the enzyme is a member of the PTP family Mycobacterium tuberculosis
3.1.3.48 MPtpB
-
 Mycobacterium tuberculosis
3.1.3.48 protein tyrosine phosphatase B
-
 Mycobacterium tuberculosis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.3.48 0.00015
-
 F1S-6C-W11
-
 Mycobacterium tuberculosis
3.1.3.48 0.00017
-
 H1-5C-W11
-
 Mycobacterium tuberculosis