Inhibition of lysyl hydroxylase by catechol analogs.
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.
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Related Subject Headings
- Tyrosine
- Structure-Activity Relationship
- Pyrogallol
- Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase
- Phenylephrine
- Mixed Function Oxygenases
- Kinetics
- Ketoglutaric Acids
- Ferrous Compounds
- Epinephrine
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Tyrosine
- Structure-Activity Relationship
- Pyrogallol
- Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase
- Phenylephrine
- Mixed Function Oxygenases
- Kinetics
- Ketoglutaric Acids
- Ferrous Compounds
- Epinephrine