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Literature summary for 2.7.4.3 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.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
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Reaction

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