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EC Number Metals/Ions Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.15Ca2+ - 683084
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.15Co2+ 0.2 mM, 4fold stimulation. When the sample is preincubated with 0.2 mM Co2+ ions and subjected to gel filtration, only 10% of the activity remains, while addition of Co2+ (0.2 mM) to the reaction mixture completely restores enzyme activity. Co2+ions could not be replaced with other divalent (Ca2+, Cd2+, Cu2+, Fe2+, Mg2+, Mn2+, Ni2+, or Zn2+) or monovalent cations (Na+or K+) when used at concentrations of up to 0.2 mM 722515
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.15Co2+ 1 mM, 2.4fold activation 723211
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.15Co2+ 25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited 665081
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.15Co2+ 800-900% activation by 0.5 mM 647039
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.15Co2+ for spectroscopic studies the enzyme containing magnetically and spectroscopically silent Zn(II) ion is substituted with Co(II) 683745
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.15Co2+ metallopeptidase, strongly activated by Co2+ 665019
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.15Co2+ required 647037, 647039
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.15Cu2+ can partly replace Co2+ 647037
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.15KCl the enzyme is optimally active at salt concentration between 0.075 and 0.25 M KCl. More than 70% of the activity is maintained at 2 M KCl 721716
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