Inhibition of lysyl hydroxylase by catechol analogs.

Published

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

Pubmed Central 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