title: Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases.
abstract: Prolyl 4-hydroxylases catalyze the formation of 4-hydroxyproline in collagens and other proteins with an appropriate collagen-like stretch of amino acid residues. The enzyme requires Fe(II), 2-oxoglutarate, molecular oxygen, and ascorbate. This review concentrates on recent progress toward understanding the detailed mechanism of 4-hydroxylase action, including: (a) occurrence and function of the enzyme in animals; (b) general molecular properties; (c) intracellular sites of hydroxylation; (d) peptide substrates and mechanistic roles of the cosubstrates; (e) insights into the development of antifibrotic drugs; (f) studies of the enzyme's subunits and their catalytic function; and (g) mutations that lead to Ehlers-Danlos Syndrome. An account of the regulation of collagen hydroxylase activities is also provided.
authors.affiliation: Collagen Research Unit, Biocenter, University of Oulu, Finland.
authors.forename: K I
authors.initials: KI
authors.lastname: Kivirikko
authors.forename: T
authors.initials: T
authors.lastname: Pihlajaniemi
mesh_terms: D000595:Amino Acid Sequence; D004535:Ehlers-Danlos Syndrome / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D011347:Procollagen / Q000378:metabolism*; D008240:Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase / Q000235:genetics / Q000378:metabolism*; D011393:Procollagen-Proline Dioxygenase / Q000235:genetics / Q000378:metabolism*; D019704:Protein Disulfide-Isomerases / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid
chemical_list: D011347:Procollagen; D011393:Procollagen-Proline Dioxygenase; D008240:Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase; C030606:proline, 2-oxoglutarate 3-dioxygenase; D019704:Protein Disulfide-Isomerases