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Literature summary for 2.3.1.4 extracted from

  • Li, Y.; Zhou, Y.; Ma, Y.; Li, X.
    Design and synthesis of novel cell wall inhibitors of Mycobacterium tuberculosis GlmM and GlmU (2011), Carbohydr. Res., 346, 1714-1720.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
2-amino-2,3-dideoxy-3-fluoro-alpha-D-glucopyranosyl phosphate inhibition of acetyltransferase activity. Compound cannot substitute the natural substrate GlcN-1-P. Uncompetitive inhibition, compound interacts with the enzyme–substrate complex. Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
bifunctional glucosamine-1-phosphate acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase
-

Synonyms

Synonyms Comment Organism
GlmU
-
Mycobacterium tuberculosis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
18.7
-
2-amino-2,3-dideoxy-3-fluoro-alpha-D-glucopyranosyl phosphate pH 7.5, 37°C Mycobacterium tuberculosis

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
12.84
-
pH 7.5, 37°C Mycobacterium tuberculosis 2-amino-2,3-dideoxy-3-fluoro-alpha-D-glucopyranosyl phosphate