Synthesis and enzymic hydroxylation of protocollagen model peptide containing a hydroxyproline residue.
1. Two protocollagen model peptides, Z-Gly-Pro-Hyp-Gly-(Pro-Pro-Gly)(5) (Z, benzyloxycarbonyl) and AOC-(Pro-Pro-Gly)(6) (AOC, tert.-pentyloxycarbonyl), were synthesized and hydroxylated with protocollagen proline hydroxylase. 2. The two model peptides were hydroxylated equally. The results suggest that the hydroxyl group of hydroxyproline contained in the N-terminal region of the peptide has no effect on the enzymic hydroxylation of the model peptide.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002642:Chick Embryo; D002850:Chromatography, Gel; D003094:Collagen / Q000138:chemical synthesis* / Q000378:metabolism*; D004586:Electrophoresis; D006900:Hydroxylation; D006909:Hydroxyproline; D006899:Mixed Function Oxygenases / Q000378:metabolism; D008956:Models, Chemical; D010455:Peptides / Q000032:analysis / Q000138:chemical synthesis* / Q000378:metabolism*; D013329:Structure-Activity Relationship
D000596:Amino Acids; D010455:Peptides; D003094:Collagen; D006899:Mixed Function Oxygenases; D006909:Hydroxyproline