EC Number   |
Application |
Reference |
|---|
    1.3.3.3 | analysis |
mass spectrometric assay for the two-step decarboxylative oxidation of coproporphyrinogen III to protoporphyrinogen IX catalyzed by CPO in mitochondria from human lymphocytes. The assay shows good reproducibility, uses simple workup by liquid-liquid extraction of enzymatic products, and employs commercially available substrates and internal standard. It was developed for use in clinical diagnostics of the inherited disorder hereditary coproporphyria |
684418 |
| 1.3.3.3 | medicine |
abnormal route for heme biosynthesis in humans suffering from porphyria cutanea tarda or related syndromes such as hexachlorobenzene poisoning |
672533 |
| 1.3.3.3 | medicine |
chronic exposure of rats to hexachlorobenzene produces an experimental model for human porphyria cutanea tarda. In digitonin-treated hexachlorobenzene mitochondria, coproporphyrinogen oxidase is free in the mitochondrial intermembrane space, whereas in normal mitochondria, 30%-50% remain anchored to the inner membrane |
698371 |
| 1.3.3.3 | medicine |
COPX4 polymorphism is associated with the atypical keto-isocoproporphyrin, utility of urinary porphyrin changes as a biomarker of exposure and potential toxicity in subjects with mercury exposure |
677201 |
| 1.3.3.3 | medicine |
CPOX4 polymorphism may affect susceptibility for specific neurobehavioral functions associated with mercury exposure in human subjects |
676196 |
| 1.3.3.3 | medicine |
first patient with porphyria where both CPO and delta-aminolaevulinic acid dehydratase are deficient at the molecular level |
672827 |
| 1.3.3.3 | medicine |
function of CPO in heme biosynthesis is apparently conserved between zebrafish and human, suggesting that CPO-MO-injected zebrafish embryos might be a useful in vivo assay system to measure the biological activity of human CPO mutations |
673851 |
| 1.3.3.3 | medicine |
His158 may have a role in the active site of CPO, none of the conserved histidine residues of the enzyme are essential for catalytic activity although changes in histidines are implicated in the disease state hereditary coproporphyria |
675777 |
| 1.3.3.3 | medicine |
increase of severity of porphyrias with monovinyl accumulation, ability of the increased levels of C-IV to compete with the authentic substrate has important implications for clinical porphyrias |
675776 |
| 1.3.3.3 | medicine |
natural polymorphism A814C leading to mutation N272H results in twofold decrease in affinity for coproporphyrinogen-III. Specific activity in liver samples is 40-50% lower than in wild-type, mutation may predispose to impaired heme biosynthesis |
701321 |
