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Literature summary extracted from

  • Dhiman, H.; Dhanjal, J.K.; Sharma, S.; Chacko, S.; Grover, S.; Grover, A.
    Resisting resistant Mycobacterium tuberculosis naturally: mechanistic insights into the inhibition of the parasites sole signal peptidase Leader peptidase B (2013), Biochem. Biophys. Res. Commun., 433, 552-557.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.22.46 (2S,3R,4R)-2-{[2-(2,3-dihydroxyphenyl)-5,8-dihydroxy-4-oxo-4H-chromen-7-yl]oxy}-4-hydroxy-4-(hydroxymethyl)tetrahydrofuran-3-yl alpha-D-galactopyranoside
-
Mycobacterium tuberculosis
3.4.22.46 2-(3,4-dihydroxyphenyl)ethyl 4-O-[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]-6-O-alpha-L-lyxopyranosyl-beta-D-glucopyranoside
-
Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.46 Mycobacterium tuberculosis P9WKA1
-
-
3.4.22.46 Mycobacterium tuberculosis H37Rv P9WKA1
-
-

Synonyms

EC Number Synonyms Comment Organism
3.4.22.46 leader peptidase B
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Mycobacterium tuberculosis
3.4.22.46 LepB
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Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
3.4.22.46 malfunction the inhibition of LepB results in repressing the cleavage of the signal peptide from the preproteins which would lead to arresting the folding of proteins which are essential for the growth and pathogenesis of Mycobacterium tuberculosis into their active mature conformation Mycobacterium tuberculosis