Molecular mechanism of ATP versus GTP selectivity of adenylate kinase was written by Rogne, Per; Rosselin, Marie; Grundstroem, Christin; Hedberg, Christian; Sauer, Uwe H.; Wolf-Watz, Magnus. And the article was included in Proceedings of the National Academy of Sciences of the United States of America on March 20,2018.Recommanded Product: (2R,3S,4R,5R)-2-(Hydroxymethyl)-5-(9H-purin-9-yl)tetrahydrofuran-3,4-diol The following contents are mentioned in the article:
Enzymic substrate selectivity is critical for the precise control of metabolic pathways. In cases where chem. related substrates are present inside cells, robust mechanisms of substrate selectivity are required. Here, we report the mechanism utilized for catalytic ATP vs. GTP selectivity during adenylate kinase (Adk)-mediated phosphorylation of AMP. Using NMR spectroscopy we found that while Adk adopts a catalytically competent and closed structural state in complex with ATP, the enzyme is arrested in a catalytically inhibited and open state in complex with GTP. X-ray crystallog. experiments revealed that the interaction interfaces supporting ATP and GTP recognition, in part, are mediated by coinciding residues. The mechanism provides an at. view on how the cellular GTP pool is protected from Adk turnover, which is important because GTP has many specialized cellular functions. In further support of this mechanism, a structure-function anal. enabled by synthesis of ATP analogs suggests that a hydrogen bond between the adenine moiety and the backbone of the enzyme is vital for ATP selectivity. The importance of the hydrogen bond for substrate selectivity is likely general given the conservation of its location and orientation across the family of eukaryotic protein kinases. This study involved multiple reactions and reactants, such as (2R,3S,4R,5R)-2-(Hydroxymethyl)-5-(9H-purin-9-yl)tetrahydrofuran-3,4-diol (cas: 550-33-4Recommanded Product: (2R,3S,4R,5R)-2-(Hydroxymethyl)-5-(9H-purin-9-yl)tetrahydrofuran-3,4-diol).
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