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Literature summary for 2.7.7.23 extracted from

  • Han, X.; Chen, C.; Yan, Q.; Jia, L.; Taj, A.; Ma, Y.
    Action of dicumarol on glucosamine-1-phosphate acetyltransferase of GlmU and Mycobacterium tuberculosis (2019), Front. Microbiol., 10, 1799 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
additional information dicumarol is unable to inhibit the N-acetylglucosamine-1-phosphate uridyltransferase activity of GlmU Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Mycobacterium tuberculosis
-
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Mycobacterium tuberculosis ATCC 25177
-
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis A5U161
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
Mycobacterium tuberculosis diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
Mycobacterium tuberculosis ATCC 25177 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
?

Synonyms

Synonyms Comment Organism
GlmU bifunctional enzyme with glucosamine-1-phosphate acetyltransferase activity and N-acetylglucosamine-1-phosphate uridyltransferase activity Mycobacterium tuberculosis
N-acetylglucosamine-1-phosphate uridyltransferase
-
Mycobacterium tuberculosis