Literature summary for 2.3.1.1 extracted from

Yang, X.; Wu, L.; Ran, Y.; Xu, A.; Zhang, B.; Yang, X.; Zhang, R.; Rao, Z.; Li, J.
Crystal structure of L-glutamate N-acetyltransferase ArgA from Mycobacterium tuberculosis (2017), Biochim. Biophys. Acta, 1865, 1800-1807 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with with AcCoA and L-glutamate. The overall structure adopts a classic fold of the GCN5-related N-acetyltransferase family, characterized by a V-shaped cleft and beta-bulge. Activity depends on dimerization to form a deep, vast pocket for L-glutamate binding. L-glutamate binds at a site far away from AcCoA. A one-step sequential mechanism is proposed for enzymatic catalysis	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	O33289	-	-
Mycobacterium tuberculosis H37Rv	O33289	-	-

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Release 2023.1 (January 2023)