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Literature summary extracted from

  • Franken, A.C.; Werner, E.R.; Haas, H.; Lokman, B.C.; van den Hondel, C.A.; Ram, A.F.; de Weert, S.; Punt, P.J.
    The role of coproporphyrinogen III oxidase and ferrochelatase genes in heme biosynthesis and regulation in Aspergillus niger (2013), Appl. Microbiol. Biotechnol., 97, 9773-9785 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.3.3 gene hemF, recombinant overexpression in Aspergillus niger, subcloning in Escherichia coli strain DH5alpha, complementation of a hemF deletion strain Aspergillus niger

Protein Variants

EC Number Protein Variants Comment Organism
1.3.3.3 additional information construction of a hemF and hemH deletion plasmids by transforming the linearized disruption vectors pDELTAhemF and pDELTAhemH into strain AB4.1, strain N402 genomic DNA is used as a template. Deletion of hemF (CPO) or hemH (FC) is conditionally lethal, and despite supplementation of hemin, DELTAhemF and DELTAhemH strains are still extremely impaired in growth. Co-overexpression of hemH, hemF, and the aminolevulinic acid synthase encoding hemA, increases the cellular accumulation of porphyrin intermediates suggesting regulatory mechanisms operating in the final steps of the fungal heme biosynthesis pathway. Gene hemF deletion strain displays a specific pigmented phenotype due to coproporphyrinogen III accumulation. Phenotypes, overview Aspergillus niger

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.3.3 mitochondrion
-
 Aspergillus niger 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.3.3 coproporphyrinogen III + O2 + 2 H+ Aspergillus niger
-
 protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
 ?
1.3.3.3 coproporphyrinogen III + O2 + 2 H+ Aspergillus niger N402
-
 protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.3.3 Aspergillus niger G3XZT7
-
-
1.3.3.3 Aspergillus niger N402 G3XZT7
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.3.3 hypha
-
 Aspergillus niger
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.3.3 coproporphyrinogen III + O2 + 2 H+
-
 Aspergillus niger protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
 ?
1.3.3.3 coproporphyrinogen III + O2 + 2 H+
-
 Aspergillus niger N402 protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.3.3 coproporphyrinogen III oxidase
-
 Aspergillus niger
1.3.3.3 CPO
-
 Aspergillus niger
1.3.3.3 HemF
-
 Aspergillus niger

General Information

EC Number General Information Comment Organism
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 Aspergillus niger
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 Aspergillus niger
1.3.3.3 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 Aspergillus niger
1.3.3.3 physiological function in filamentous fungi, enzyme CPO functions as a regulatory step preventing hazardous levels of intracellular heme Aspergillus niger