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- W2493264927 abstract "This chapter focuses on the structural chemistry and the biological aspects of aminopeptidase yscCo-II (APCo-II). ApCO-II has a native molecular mass of 290 kDa, being a hexameric enzyme made up of six identical subunits (48 kDa). The optimum pH of APCo-II is 7 and enzyme activity is only detected in the presence of Co 2+ ions. APCo-II expresses itself primarily in the exponential phase of cell growth. APCo-II activity is strictly dependent on Co 2+ . If it is replaced by another divalent metal (Ca 2+ , Cu 2+ , Cr 2+ , Mn 2+ , Mg 2+ or Zn 2+ ), the percentage of recovery of the activity is minimal (2–10%). In the presence of Co 2+ , APCo-II activity is totally inhibited by Cu 2+ , and levels of inhibition are 83%, 70% and 40% for Cr 2+ , Zn 2+ and Ni 2+ , respectively. It is interesting to observe how Zn 2+ , which is a structural part of several enzymes, for example, APysc-I and APysc-Y, behave toward others as an inhibitor, for example, thiol-AP. Studies on the effect of protease inhibitors on APCo-II activity show 100% inhibition for 1,10-phenanthroline, bestatin and PMSF, and 80% inhibition for Lys-hydroxamate and TLCK." @default.
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- W2493264927 date "2004-01-01" @default.
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- W2493264927 title "Aminopeptidase yscCo-II" @default.
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- W2493264927 doi "https://doi.org/10.1016/b978-0-12-079611-3.50321-9" @default.
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