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摘要: Prolylhydroxylase catalyses the conversion of selected proline (Pro) residues into 4-hydroxyproline (Hyp). Only those Pro residues which occur in position 3 of the typical collagen triplet,-Gly-R2-R3-, are hydroxylated by the enzyme and the extent of hydroxylation is apparently governed by the nature of the residues adjoining the-Pro-Gly-segment (1). Since the unhydroxylated collagen molecule is found to be structurally and functionally defective (1), the understanding of the conformational aspects of Hyp incorporation in collagen is very important.