Unprecedented overmetabolism of a porphyrinogen substrate by coproporphyrinogen oxidase.
Harderoporphyrinogen-I is metabolized by avian hemolysate preparations of coproporphyrinogen oxidase to give a trivinylic product; this unprecedented 'overmetabolism' of the porphyrinogen substrate provides strong support for a proposed model of the active site of this poorly understood enzyme.
Lash
Timothy D
TD
Department of Chemistry, Illinois State University, Normal, IL 61790-4160, USA. tdlash@ilstu.edu
Keck
Anna-Sigrid I M
AS
Mani
Ukti N
UN
Jones
Marjorie A
MA
D000818:Animals; D001665:Binding Sites; D002645:Chickens / Q000378:metabolism*; D003304:Coproporphyrinogen Oxidase / Q000378:metabolism*; D003305:Coproporphyrinogens / Q000138:chemical synthesis* / Q000378:metabolism*; D006418:Heme / Q000378:metabolism*; D007202:Indicators and Reagents; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D015394:Molecular Structure; D011165:Porphyrinogens / Q000737:chemistry / Q000378:metabolism*; D011166:Porphyrins / Q000737:chemistry / Q000378:metabolism; D014753:Vinyl Compounds / Q000737:chemistry
D003305:Coproporphyrinogens; D007202:Indicators and Reagents; D011165:Porphyrinogens; D011166:Porphyrins; D014753:Vinyl Compounds; C028026:coproporphyrinogen III; C018563:harderoporphyrinogen; D006418:Heme; D003304:Coproporphyrinogen Oxidase