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

abstract

• 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

publisher

• Elsevier  Publisher

published in

• Biochemical and Biophysical Research Communications  Journal

keywords

• Carbon Isotopes
• Collagen
• Hydroxylation
• Mixed Function Oxygenases
• Peptides
• Procollagen-Proline Dioxygenase

Digital Object Identifier (DOI)

• 10.1016/0006-291x(71)90203-8

start page

• 1591

end page

• 1596

volume

• 45

issue

• 6

URL

• http://dx.doi.org/10.1016/0006-291x(71)90203-8