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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General Information
General Information on EC 1.3.3.3 - coproporphyrinogen oxidase
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malfunction
metabolism
physiological function
additional information
spontaneous lesion formation mutant lin2-2. The lin2-2 mutation confers growth inhibition, enhanced powdery mildew resistance, and powdery mildew (Golovinomyces cichoracearum strain UCSC1)-induced cell death, as well as spontaneous cell death dependent on salicylic acid, in Arabidopsis thaliana, phenotye, detailed overview. The lin2-2 mutant also displays enhanced resistance to Hyaloperonospora arabidopsidis Noco2, and lin2-2 mutants exhibit enhanced ethylene-induced senescence. The edr1 mutation enhances the lin2-2 phenotype
malfunction
the lin2-2 mutant exhibits enhanced ethylene-induced senescence. Additionally, the chlorophyll level is significantly lower in lin2-2 than in the wild type when treated with ethylene for 3 days
malfunction
partial deficiency of the enzyme coproporphyrinogen oxidase (CPOX) causes hereditary coproporphyria (HCP), an autosomal dominant-inherited disease of heme biosynthesis. Patients suffering HCP show 50% of normal activity and those with the rare autosomal recessive harderoporphyria accumulate harderoporphyrinogen, an intermediate porphyrin of the CPOX reaction. As only patients with mutation K404E in this region develop harderoporphyria, the K404E mutation leads to diminishment of the second step of the decarboxylation reaction during the conversion of coproporphyrinogen to protoporphyrinogen, implying that the active site of the enzyme involved in the second step of decarboxylation is encoded in exon 6
malfunction
the lethal phenotype of deletion of hemF can be remediated by heme supplementation confirming that Aspergillus niger is capable of hemin uptake. The hemF gene deletion mutant shows an extremely impaired growth even with hemin supplementation which can be slightly improved by media modifications and the use of hemoglobin as heme source. The hyphae of the mutant strains display pinkish coloration and red autofluorescence under UV indicative of cellular porphyrin accumulation. The mutant shows accumulation of specific porphyrins, thereby confirming the function of the protein in heme biosynthesis. Gene hemF deletion strain displays a specific pigmented phenotype due to coproporphyrinogen III accumulation. Phenotypes, overview
malfunction
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enzyme knockout leads to necrotic spots on developing leaves. The enzyme defect decreases the chlorophyll content by disrupting tetrapyrrole biosynthesis and enhances resistance to Phytophthora sojae
malfunction
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plants carrying enzyme mutant alleles show defects in gametophyte development, including nonviable pollen and embryo sacs with unfused polar nuclei. Improper differentiation of the central cell leads to defects in endosperm development. Consequently, embryo development is arrested at the globular stage
malfunction
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spontaneous lesion formation mutant lin2-2. The lin2-2 mutation confers growth inhibition, enhanced powdery mildew resistance, and powdery mildew (Golovinomyces cichoracearum strain UCSC1)-induced cell death, as well as spontaneous cell death dependent on salicylic acid, in Arabidopsis thaliana, phenotye, detailed overview. The lin2-2 mutant also displays enhanced resistance to Hyaloperonospora arabidopsidis Noco2, and lin2-2 mutants exhibit enhanced ethylene-induced senescence. The edr1 mutation enhances the lin2-2 phenotype
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malfunction
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the lin2-2 mutant exhibits enhanced ethylene-induced senescence. Additionally, the chlorophyll level is significantly lower in lin2-2 than in the wild type when treated with ethylene for 3 days
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malfunction
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the lethal phenotype of deletion of hemF can be remediated by heme supplementation confirming that Aspergillus niger is capable of hemin uptake. The hemF gene deletion mutant shows an extremely impaired growth even with hemin supplementation which can be slightly improved by media modifications and the use of hemoglobin as heme source. The hyphae of the mutant strains display pinkish coloration and red autofluorescence under UV indicative of cellular porphyrin accumulation. The mutant shows accumulation of specific porphyrins, thereby confirming the function of the protein in heme biosynthesis. Gene hemF deletion strain displays a specific pigmented phenotype due to coproporphyrinogen III accumulation. Phenotypes, overview
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CPO catalyzes the oxidative decarboxylation of coproporphyrinogen III to form protoporphyrinogen IX in heme biosynthesis and is shared in chlorophyll biosynthesis in photosynthetic organisms. HemF plays an essential role under aerobic growth the photosynthetic organism, overview
metabolism
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CPOX is a mitochondrial enzyme in the heme biosynthetic pathway that catalyzes the conversion of coproporphyrinogen III to protoporphyrinogen IX
metabolism
LIN2 encodes coproporphyrinogen III oxidase, CPO, a key enzyme of the tetrapyrrole biosynthesis pathway
metabolism
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oxygen-dependent coproporphyrinogen III oxidase catalyzes the sequential decarboxylation of the propionate substituents present on the A and B rings of coproporphyrinogen III in the heme biosynthetic pathway
metabolism
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separation of uroporphyrinogen decarboxylase, URO-D, EC 4.1.1.37, associated with the cytoplasm, and coproporphyrinogen oxidase, CPO, found in the mitochondria. They show in vitro competitive action of both on the same diacetate porphyrinogen substrate provides additional perspectives on the potential existence of abnormal pathways for heme biosynthesis. Porphyrinogen 3,3'-[13,17-bis(carboxymethyl)-3,8,12,18-tetramethyl-5,10,15,20,22,24-hexahydroporphyrin-2,7-diyl]dipropanoic acid is a reasonable substrate for URO-D but appears to be a comparatively poor substrate for CPO
metabolism
coproporphyrinogen III oxidase, CPO, is the sixth enzyme within the heme biosynthesis pathway, and is responsible for the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX. Heme biosynthesis pathway, overview
metabolism
coproporphyrinogen oxidase (CPO) is an enzyme involved in the heme pathway responsible for the conversion of 5-aminolevulinic acid into protoporphyrin IX, coproporphyrinogen oxidase (CPO) is the sixth enzyme in the cascade
metabolism
coproporphyrinogen oxidase (CPO) is an enzyme involved in the heme pathway responsible for the conversion of 5-aminolevulinic acid into protoporphyrin IX, coproporphyrinogen oxidase (CPO) is the sixth enzyme in the cascade
metabolism
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the enzyme plays an important role in the biosynthesis of tetrapyrrole and light-dependent-defense in soybean
metabolism
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LIN2 encodes coproporphyrinogen III oxidase, CPO, a key enzyme of the tetrapyrrole biosynthesis pathway
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metabolism
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coproporphyrinogen III oxidase, CPO, is the sixth enzyme within the heme biosynthesis pathway, and is responsible for the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX. Heme biosynthesis pathway, overview
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CPOX is a mitochondrial enzyme in the heme biosynthetic pathway that catalyzes the conversion of coproporphyrinogen III to protoporphyrinogen IX
physiological function
coproporphyrinogen oxidase (CPO) is a rate-limiting enzyme in the heme pathway responsible for the conversion of coproporphyrinogen III into protoporphyrin IX
physiological function
coproporphyrinogen oxidase (CPO) is a rate-limiting enzyme in the heme pathway responsible for the conversion of coproporphyrinogen III into protoporphyrin IX. The efficacy of photodynamic therapy for epithelial cancers is increased when photodynamic therapy is combined with calcitriol (Vit D), a form of differentiation therapy, underlying mechanism, overview. Differentiation therapy is associated with upregulation of C/EBPs, CPO gene expression, and PpIX production in tumors in vivo. Differentiation-promoting agents are known to upregulate CCAAT-enhancer binding proteins (C/EBPs), powerful regulators of cellular differentiation, and coproporphyrinogen oxidase (CPO). Cooperative interactions between regularly spaced C/EBP sites appear critical for CPO transcriptional regulation by differentiation therapy, mechanistic rationale for DT/PDT combination therapy for cancer
physiological function
in filamentous fungi, enzyme CPO functions as a regulatory step preventing hazardous levels of intracellular heme
physiological function
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in filamentous fungi, enzyme CPO functions as a regulatory step preventing hazardous levels of intracellular heme
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hereditary coproporphyria is a disorder due to the reduced activity of coproporphyrinogen III oxidase, and is an autosomal dominant disease classified as acute hepatic porphyria, overview
additional information
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active-site models for substrate binding by coproporphyrinogen oxidase, overview. The invariant amino acids aspartate 400, arginine 262, and arginine 401 are essential for significant catalytic activity
additional information
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active-site models for substrate binding by coproporphyrinogen oxidase, overview. The invariant amino acids aspartate 400, arginine 262, and arginine 401 are essential for significant catalytic activity
additional information
overexpression of hemH, but not hemF or the aminolevulinic acid synthase encoding hemA, modestly increases the cellular heme content, which is apparently insufficient to increase activity of endogenous peroxidase and cytochrome P450 enzyme activities. Overexpression of all three genes increases the cellular accumulation of porphyrin intermediates suggesting regulatory mechanisms operating in the final steps of the fungal heme biosynthesis pathway
additional information
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overexpression of hemH, but not hemF or the aminolevulinic acid synthase encoding hemA, modestly increases the cellular heme content, which is apparently insufficient to increase activity of endogenous peroxidase and cytochrome P450 enzyme activities. Overexpression of all three genes increases the cellular accumulation of porphyrin intermediates suggesting regulatory mechanisms operating in the final steps of the fungal heme biosynthesis pathway
additional information
the active site of the enzyme involved in the second step of decarboxylation is encoded in exon 6. Aspartic acid at position 400 can be a prerequisite for dimerization of enzyme CPOX
additional information
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the active site of the enzyme involved in the second step of decarboxylation is encoded in exon 6. Aspartic acid at position 400 can be a prerequisite for dimerization of enzyme CPOX
additional information
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overexpression of hemH, but not hemF or the aminolevulinic acid synthase encoding hemA, modestly increases the cellular heme content, which is apparently insufficient to increase activity of endogenous peroxidase and cytochrome P450 enzyme activities. Overexpression of all three genes increases the cellular accumulation of porphyrin intermediates suggesting regulatory mechanisms operating in the final steps of the fungal heme biosynthesis pathway
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