title: Effect of divalent metal ions on collagenase from Clostridium histolyticum.
abstract: The collagenase from Clostridium histolyticum (EC 3.4.24.3) degrades type IV collagen with Km 32 nM, indicating a high affinity for this substrate. Ferrous and ferric ions can inhibit Clostridium collagenase. Inhibition by Fe++ was of the mixed, non-competitive type, with Ki 90 microM. The inhibitory effect of Fe++ may be due to Zn++ displacement from the intrinsic functional center of this metalloprotease, since in the presence of excess amounts of Zn++ enzyme activity is retained. This inhibitory effect of Fe++ may be common for all types of collagenases, since this ion can also inhibit type IV collagenase purified from Walker 256 carcinoma, with IC50 80 microM. Cu++ can only partially inhibit Clostridium collagenase, while other divalent metal ions such as Cd++, Co++, Hg++, Mg++, Ni++ or Zn++ are devoid of any inhibitory effect on the enzyme.
authors.affiliation: Department of Pharmacology, University of Patras Medical School, Greece.
authors.forename: G
authors.initials: G
authors.lastname: Karakiulakis
authors.forename: E
authors.initials: E
authors.lastname: Papadimitriu
authors.forename: E
authors.initials: E
authors.lastname: Missirlis
authors.forename: M E
authors.initials: ME
authors.lastname: Maragoudakis
mesh_terms: D000595:Amino Acid Sequence; D002277:Carcinoma / Q000378:metabolism; D002413:Cations, Divalent / Q000494:pharmacology*; D003300:Copper / Q000494:pharmacology; D004492:Edetic Acid; D005290:Ferric Compounds / Q000494:pharmacology; D005296:Ferrous Compounds / Q000494:pharmacology; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008670:Metals / Q000494:pharmacology*; D003012:Microbial Collagenase / Q000737:chemistry / Q000502:physiology*; D008969:Molecular Sequence Data; D013997:Time Factors
chemical_list: D002413:Cations, Divalent; D005290:Ferric Compounds; D005296:Ferrous Compounds; D008670:Metals; D003300:Copper; D004492:Edetic Acid; D003012:Microbial Collagenase; D008274:Magnesium