1998/01/01 by K.I. Kivirikko, Taina Pihlajaniemi · 2 citations
Biochemistry, Genetics and Molecular Biology · #Cancer-related gene regulation #Fibroblast Growth Factor Research #Microbial metabolism and enzyme function
paper · doi:10.1002/9780470123188.ch9
openalex publication_date 1998/01/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/29
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.