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Results 1 - 7 of 7
EC Number Metals/Ions Commentary Reference
Show all pathways known for 3.5.1.116Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.116Ca2+ slight increase of activity 34479
Show all pathways known for 3.5.1.116Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.116Fe2+ slight increase of activity 34479
Show all pathways known for 3.5.1.116Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.116Mg2+ slight increase of activity 34479
Show all pathways known for 3.5.1.116Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.116Mn2+ activates, maximal activity at 0.2 mM 34479
Show all pathways known for 3.5.1.116Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.116Mn2+ Mn2+ is required for maximum catalytic activity. The bimetal reaction center of the enzyme is located at the pocket enclosed by the catalytic domain, dimerization domain, and other structural elements from a different subunit, structure, overview 734481
Show all pathways known for 3.5.1.116Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.116Mn2+ substrate (S)-ureidoglycine is bound to the Mn2+ ion at the active site of homooctameric enzyme. The Mn2+ ion acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction 734179
Show all pathways known for 3.5.1.116Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.116Zn2+ activates 34479
Results 1 - 7 of 7