title: The second zinc atom in the matrix metalloproteinase catalytic domain is absent in the full-length enzymes: a possible role for the C-terminal domain.
abstract: Domain deletion mutants of the matrix metalloproteinases consisting of the catalytic domain only contain two zinc atoms per molecule. One is essential for catalysis, while the other may fulfil a structural role. We have analysed the zinc contents of both the full-length and the truncated mutants of prostromelysin-1 and progelatinase A and report that the second zinc atom is not present in the full-length form of the proenzymes. Thus it seems likely that the role proposed for this zinc atom in maintaining the structure of the enzyme catalytic domain is performed by the C-terminal domain in the full-length enzyme.
authors: Department of Biochemistry, Queen Mary & Westfield College, University of London, UK.
authors: F
authors: F
authors: Willenbrock
authors: G
authors: G
authors: Murphy
authors: I R
authors: IR
authors: Phillips
authors: K
authors: K
authors: Brocklehurst
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002384:Catalysis; D004792:Enzyme Precursors / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D014407:Tumor Cells, Cultured; D015032:Zinc / Q000032:analysis*
chemical_list: D004792:Enzyme Precursors; D008666:Metalloendopeptidases; C048047:prostromelysin; D015032:Zinc