The enzymic hydroxylation of protocollagen models.
1. Synthetic polymers of l-prolyl-l-prolylglycine of defined chain length, (Pro-Pro-Gly)(n), were found to be substrates for the enzyme protocollagen-proline hydroxylase, with optimum chain length n=5. Boiling the polymer (Pro-Pro-Gly)(15) increased its activity as a substrate but had no effect on (Pro-Pro-Gly)(5). 2. Protection of both or one of the N- and C-terminal groups made (Pro-Pro-Gly)(3) a better substrate, and collagenase digestion of hydroxylated tert.-pentyloxy-carbonyl-(Pro-Pro-Gly)(3) benzyl ester indicated that the central prolyl residues were the major points of hydroxylation. 3. The results suggest that the long-chain peptides are optimum substrates but that a triple-stranded structure is inhibitory for hydroxylation.
D000818:Animals; D002642:Chick Embryo; D003094:Collagen / Q000096:biosynthesis*; D004952:Esters; D005998:Glycine; D006358:Hot Temperature; D066298:In Vitro Techniques; D003012:Microbial Collagenase; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism*; D011392:Proline
D004952:Esters; D010455:Peptides; D003094:Collagen; D011392:Proline; D006899:Mixed Function Oxygenases; D003012:Microbial Collagenase; D005998:Glycine