Asymmetry in the hydroxylation of (Pro-Pro-Gly) 5 by protocollagen proline hydroxylase. Academic Article uri icon


  • Peptides of the structure (Pro-Pro-Gly)5 and labeled with [14C]proline in individual triplets were synthesized and used as substrates for the synthesis of hydroxyproline by protocollagen proline hydroxylase. The results indicated that the enzyme hydroxylated the peptide asymmetrically in that the fourth triplet from the NH2-terminal end was hydroxylated to a greater extent than any other triplet. 1971.

published proceedings

  • Biochem Biophys Res Commun

author list (cited authors)

  • Kivirikko, K. I., Suga, K., Kishida, Y., Sakakibara, S., & Prockop, D. J.

citation count

  • 18

complete list of authors

  • Kivirikko, KI||Suga, K||Kishida, Y||Sakakibara, S||Prockop, DJ

publication date

  • January 1971