1.3.3.3: coproporphyrinogen oxidase
This is an abbreviated version!
For detailed information about coproporphyrinogen oxidase, go to the full flat file.
Word Map on EC 1.3.3.3
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1.3.3.3
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heme
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protoporphyrinogen
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coproporphyria
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protoporphyrin
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porphyria
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ferrochelatase
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uroporphyrinogen
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5-aminolevulinic
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porphobilinogen
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tetrapyrrole
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porphyrinogens
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medicine
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oxygen-independent
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coproporphyrinuria
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mg-protoporphyrin
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ala-pdt
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delta-aminolaevulinic
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uroporphyrin
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cutanea
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analysis
- 1.3.3.3
- heme
- protoporphyrinogen
- coproporphyria
- protoporphyrin
- porphyria
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ferrochelatase
- uroporphyrinogen
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5-aminolevulinic
- porphobilinogen
- tetrapyrrole
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porphyrinogens
- medicine
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oxygen-independent
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coproporphyrinuria
- mg-protoporphyrin
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ala-pdt
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delta-aminolaevulinic
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uroporphyrin
-
cutanea
- analysis
Reaction
Synonyms
copro'gen oxidase, Coprogen oxidase, coproporphyinogen oxidase, coproporphyrinogen III oxidase, coproporphyrinogen oxidase, coproporphyrinogen-III oxidase, coproporphyrinogenase, COX, CPgen oxidase, CPGox, CPO, CPO III oxidase, CPOX, CPOX4, CPX, CPX1, CPX2, HEM13, Hem13p, HemF, HEMN1, KlHEM13, LIN2, LMM2, O2-dependent coproporphyrinogen III oxidase, oxygen-dependent coproporphyrinogen III oxidase, oxygen-dependent coproporphyrinogen-III oxidase, Sll1185
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Application
Application on EC 1.3.3.3 - coproporphyrinogen oxidase
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analysis
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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
medicine
additional information
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abnormal route for heme biosynthesis in humans suffering from porphyria cutanea tarda or related syndromes such as hexachlorobenzene poisoning
medicine
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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
medicine
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CPOX4 polymorphism may affect susceptibility for specific neurobehavioral functions associated with mercury exposure in human subjects
medicine
first patient with porphyria where both CPO and delta-aminolaevulinic acid dehydratase are deficient at the molecular level
medicine
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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
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
medicine
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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
medicine
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patients with the specific mutation K404E have a unifying syndrome in which hematological disorders predominate, the so called harderoporphyria, harderoporphyric patients exhibit iron overload secondary to dyserythropoiesis
medicine
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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
medicine
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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
medicine
the regulation of the enzyme is important in differentiation therapy for cancer treatment
cloned KlHEM13 is functional and able to replace its homologous gene in Saccharomyces cerevisiae
additional information
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cloned KlHEM13 is functional and able to replace its homologous gene in Saccharomyces cerevisiae
additional information
cpx1 and cpx2 genes encode almost identical, catalytically active enzymes with distinctive N-terminal peptide sequences, cpx1 encodes a plastid transit peptide, whereas this region is deleted from the cpx2 gene, the 5' regions of both messenger RNAs are highly similar, but the cpx2 gene has an open-reading frame that can encode a new targeting signal
additional information
cpx1 and cpx2 genes encode almost identical, catalytically active enzymes with distinctive N-terminal peptide sequences, cpx1 encodes a plastid transit peptide, whereas this region is deleted from the cpx2 gene, the 5' regions of both messenger RNAs are highly similar, but the cpx2 gene has an open-reading frame that can encode a new targeting signal
additional information
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cpx1 and cpx2 genes encode almost identical, catalytically active enzymes with distinctive N-terminal peptide sequences, cpx1 encodes a plastid transit peptide, whereas this region is deleted from the cpx2 gene, the 5' regions of both messenger RNAs are highly similar, but the cpx2 gene has an open-reading frame that can encode a new targeting signal