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Results 1 - 10 of 35 > >>
EC Number Metals/Ions Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.50Ca2+ can partially replace Mg2+ in activation 643480
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.50Co2+ 30% of the activity with Mg2+ 695159
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.50K+ stimulates, maximal activation at 6 mM KCl 643480
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.50Mg2+ - 209891, 643470, 690946
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.50Mg2+ 10 mM used in assay conditions 761967
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.50Mg2+ 25% of the activity with Mn2+ 643466
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.50Mg2+ both reaction steps are dependent on divalent metal ions 695159
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.50Mg2+ can partially replace Mn2+ in activation 643466, 643475, 643476
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.50Mg2+ enzyme-GMP intermediate formation is strictly dependent on divalent cations, satisfied by Mn2+ or Mg2+, Mn2+ is slightly preferred 643486, 643490
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.50Mg2+ magnesium binding likely activates the lysine nucleophile by increasing its acidity and by biasing the deprotonated nucleophile into conformations conducive to intermediate formation 721658
Results 1 - 10 of 35 > >>