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Results 1 - 10 of 57 > >>
EC Number Metals/Ions Commentary Reference
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23Co2+ activates to 72% of the activity with Mg2+ 670775
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23Co2+ can partially replace Mg2+, causes increase in Km 657286
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23Co2+ can substitute the physiological cofactor Mg2+, however the kcat is significantly reduced compared to dUTP-Mg2+ 696412
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23Co2+ strictly dependent on a bivalent metal cation like Co2+ 718787
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23Mg2+ - 667399, 667783, 669790, 669804, 670909, 685380, 686744, 689949
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23Mg2+ 0.5 mM, stimulates by 7% 209977
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23Mg2+ 5 mM used in assay conditions 756317
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23Mg2+ activates 696282, 699236
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23Mg2+ activates, phosphate chain coordination involves Mg2+, binding structure, overview. Mg2+ probably dissociates from the enzyme with the product PPi and not with dUMP 695290
Show all pathways known for 3.6.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.23Mg2+ best divalent cation, bound at the center of the trimeric enzyme structure 670091
Results 1 - 10 of 57 > >>