Metabolism of analogues of coproporphyrinogen-III with modified side chains: implications for binding at the active site of coproporphyrinogen oxidase.
Porphyrinogens with modified propionate side chains bearing methyl substituents were found to be modest substrates for coproporphyrinogen oxidase; the results indicate that alteration of the substituents involved in secondary binding interactions has a comparable affect to modifying the side chain that undergoes degradation at the catalytic site.
Lash
Timothy D
TD
Department of Chemistry, Illinois State University, 61790-4160, Normal, IL, USA
Kaprak
Todd A
TA
Shen
Lan
L
Jones
Marjorie A
MA
D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D003304:Coproporphyrinogen Oxidase / Q000187:drug effects*; D003305:Coproporphyrinogens / Q000737:chemistry*; D004912:Erythrocytes / Q000187:drug effects / Q000201:enzymology; D066298:In Vitro Techniques; D007700:Kinetics; D008745:Methylation; D011485:Protein Binding; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D003305:Coproporphyrinogens; C028026:coproporphyrinogen III; D003304:Coproporphyrinogen Oxidase