Literature summary 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.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.4.2.18	anthranilate	substrate inhibition	Mycobacterium tuberculosis

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.4.2.18	Mycobacterium tuberculosis	P9WFX5	-	-

Substrates and Products (Substrate)

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

Synonyms

EC Number	Synonyms	Comment	Organism
2.4.2.18	AnPRT	-	Mycobacterium tuberculosis

General Information

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

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Release 2023.1 (January 2023)