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Results 1 - 10 of 10
EC Number Metals/Ions Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B57Ca2+ 1 mM, enhances activity. An increase in CaCl2 concentration did not affect further the enzyme activity 727459
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B57Ca2+ bound at the high-affinity Ca1 site and low-affinity Ca2 site 731311
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B57Ca2+ required for enzyme stability at higher temperatures, bound Ca2+ increases the thermostability of the subtilases or protects them from autolysis 732679
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B57Ca2+ the enzyme contains seven Ca2+ ions. Four of them (Ca2-Ca5) are responsible for folding of Tk-subtilisin. Ca6 and Ca7 ions are not important for activity. The Ca1 ion is required for the maximal activity of Tk-subtilisin. Ca1, Ca6, and Ca7 ions, especially the Ca1 ion, contribute to the hyperthermostabilization of Tk-subtilisin 726988
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B57Ca2+ the enzyme requires Ca2+ for folding and assumes a molten globule-like structure in the absence of Ca2+ even in the presence of Tk-propeptide. Tk-subtilisin contains seven Ca2+-binding sites. Four of them are located within a long loop, which mostly consists of a unique insertion sequence of this protein 707480
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B57Ca2+ two Ca2+ ions bind to the beta-jelly roll domain 728144
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B57CaCl2 highest activity in the presence of 5 mM CaCl2. The enzyme exhibits 70% and 80% of the maximal activity in the presence of 1 and 100 mM CaCl2, respectively 726706
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B57CaCl2 maximum enhancement of the purified pernisine activity is observed at around 1 mM CaCl2. Further increasing the CaCl2 above 1 mM leads to a gradual decline in this enhanced activity. In the presence of 1 mM CaCl2, the proteolytic activity of pernisine is enhanced, to reach around 75% greater activity, with the maximum activity at 105.0°C 728576
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B57more NaCl and CaCl2 together do not show any cumulative effects, as they appear to separately affect the activity 728576
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B57NaCl the maximal activity of the purified pernisine seen for 20 mM NaCl in the absence of 1 mM CaCl2 increases to more than 2fold after the addition of CaCl2, with even larger relative enhancement by CaCl2 at higher NaCl concentrations 728576
Results 1 - 10 of 10