Inhibition of lysyl hydroxylase by catechol analogs.
Journal Article (Journal Article)
Catechol analogs inhibit the activity of lysyl hydroxylase (peptidyllysine, 2-oxyglutarate: oxygen 5-oxidoreductase, EC 1.14.11.4), a microsomal enzyme which catalyzes the transformation of certain lysyl residues in collagen to hydroxylysine. Chick embryo lysyl hydroxylase activity was measured by specific tritium release as tritiated water from an L-[4,5-3H]lysine-labelled unhydroxylated collagen substrate prepared from chick calvaria. Catechol analogs did not bind irreversibly to either enzyme or substrate, as full activity was restored with dialysis. Addition of excess cofactor, Fe2+, ascorbic acid, or alpha-ketoglutarate, did not affect inhibition. Kinetic analysis revealed that with respect to collagen substrate, catechol demonstrated a noncompetitive type of inhibition with a Ki of 15 muM.
Full Text
Duke Authors
Cited Authors
- Murray, JC; Cassell, RH; Pinnell, SR
Published Date
- March 15, 1977
Published In
Volume / Issue
- 481 / 1
Start / End Page
- 63 - 70
PubMed ID
- 402945
International Standard Serial Number (ISSN)
- 0006-3002
Digital Object Identifier (DOI)
- 10.1016/0005-2744(77)90137-1
Language
- eng
Conference Location
- Netherlands