Literature summary extracted from

Bellinzoni, M.; Haouz, A.; Grana, M.; Munier-Lehmann, H.; Shepard, W.; Alzari, P.M.
The crystal structure of Mycobacterium tuberculosis adenylate kinase in complex with two molecules of ADP and Mg2+ supports an associative mechanism for phosphoryl transfer (2006), Protein Sci., 15, 1489-1493.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
2.7.4.3	in complex with two molecules of ADP and Mg2+. Structure reveals significant conformational changes of the LID and NMP-binding domain upon substrate binding. The ternary complex represents the enzyme at the start of ATP synthesis reaction, is consistent with nucleophilic attack of a terminal oxygen from the acceptor ADP on the beta-phosphate from the donor substrate, and hints to an associative mechanism for phosphoryl transfer	Mycobacterium tuberculosis

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.7.4.3	Mycobacterium tuberculosis	-	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
2.7.4.3	ATP + AMP = 2 ADP	associative mechanism for phosphoryl transfer	Mycobacterium tuberculosis	a

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Release 2023.1 (January 2023)