3.4.24.84 Co2+ restores Ste24 CAAX proteolytic activity after 1,10-phenanthroline treatment, reactivation with 0.25 mM Co2+ is 25% of that seen with 0.25 mM Zn2+ 638977 3.4.24.84 additional information - 638974, 638976 3.4.24.84 additional information C-terminal proteolytic activity of Ste24 requires metall ions 638976 3.4.24.84 additional information Ste24 has a characteristic zinc metalloprotease motif, HEXXH 638974 3.4.24.84 additional information zinc metalloprotease motif HEXXH 638978 3.4.24.84 additional information Zn-metalloprotease consensus motif HEXXH 638973 3.4.24.84 Zn2+ - 638977 3.4.24.84 Zn2+ contains zinc 753395, 755334 3.4.24.84 Zn2+ probably Zn2+-dependent metalloprotease 653884 3.4.24.84 Zn2+ the in vitro N-terminal proteolysis of a-factor requires Zn2+ as metal cofactor, inhibition at higher Zn2+ concentrations e.g. 2 mM 638976 3.4.24.84 Zn2+ Zn-dependent protease 654005 3.4.24.84 Zn2+ Zn2+-dependent active site 667497