EC Number   |
General Information |
Reference |
|---|
    1.3.3.3 | malfunction |
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 |
764783 |
| 1.3.3.3 | 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 |
745239 |
| 1.3.3.3 | malfunction |
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 |
746121 |
| 1.3.3.3 | malfunction |
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 |
-, 726153 |
| 1.3.3.3 | 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 |
-, 744139 |
| 1.3.3.3 | 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 |
-, 726153 |
| 1.3.3.3 | 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 |
-, 744139 |
| 1.3.3.3 | 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 |
745755 |
| 1.3.3.3 | metabolism |
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 |
713258 |
| 1.3.3.3 | metabolism |
CPOX is a mitochondrial enzyme in the heme biosynthetic pathway that catalyzes the conversion of coproporphyrinogen III to protoporphyrinogen IX |
697204 |
