  3.5.99.8 | more |
the enzyme is a metalloprotease family member, it can use several divalent transition metals for catalysis. The metal in 5NAA-A is labile but readily loaded in the presence of substrate. Adjacent to the 5NAA binding site is a triad of residues (His86-Glu196-Asn124) in a location equivalent to that of the corresponding M20 metalloprotease His2-Glu2-Asp metal binding motif. 5NAA-A requires metal ions for hydrolysis, and several transition metal ions are suitable. Fastest rates are observed in the presence of Mn2+, Fe2+ facilitates turnover but data cannot be fit to the Michaelis-Menten equation, like Cu2+, metal binding analysis, overview |
757730 |
