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Literature summary for 2.4.2.18 extracted from

  • Cookson, T.V.; Castell, A.; Bulloch, E.M.; Evans, G.L.; Short, F.L.; Baker, E.N.; Lott, J.S.; Parker, E.J.
    Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis (2014), Biochem. J., 461, 87-98.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
anthranilate substrate inhibition Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate Mycobacterium tuberculosis
-
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WFX5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
Mycobacterium tuberculosis anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
?

Synonyms

Synonyms Comment Organism
AnPRT
-
Mycobacterium tuberculosis

General Information

General Information Comment Organism
physiological function the enzyme is essential for the virulence of Mycobacterium tuberculosis Mycobacterium tuberculosis