Information on EC 1.3.3.15 - coproporphyrinogen III oxidase (coproporphyrin-forming)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.3.15
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RECOMMENDED NAME
GeneOntology No.
coproporphyrinogen III oxidase (coproporphyrin-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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heme b biosynthesis IV (Gram-positive bacteria)
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Metabolic pathways
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Porphyrin and chlorophyll metabolism
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SYSTEMATIC NAME
IUBMB Comments
coproporphyrinogen-III:oxygen oxidoreductase (coproporphyrin-forming)
Contains FAD. The enzyme, present in Gram-positive bacteria, participates in heme biosynthesis. It can also catalyse the reaction of EC 1.3.3.4, protoporphyrinogen oxidase, at a lower level.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
coproporphyrinogen III + O2
coproporphyrin III + H2O
show the reaction diagram
mesoporphyrinogen IX + O2
mesoporphyrin IX + H2O
show the reaction diagram
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-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
coproporphyrinogen III + O2
coproporphyrin III + H2O
show the reaction diagram
mesoporphyrinogen IX + O2
mesoporphyrin IX + H2O
show the reaction diagram
-
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acifluorfen
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bilirubin
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competitive inhibitor
Biliverdin
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competitive inhibitor
Hemin
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competitive inhibitor
methylacifluorfen
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weajk inhibition at 0.1 mM
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protoporphyrinogen IX
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acts as a competitive inhibitor of the coproporphyrinogen III to coproporphyrin oxidase activity of HemY
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00529 - 0.0067
Coproporphyrinogen III
0.00429
mesoporphyrinogen IX
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at pH 8.7 and 37°C
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0.001
protoporphyrinogen IX
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at pH 8.7 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.46
Coproporphyrinogen III
Staphylococcus aureus
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at pH 8.0 and 37°C
0.44
protoporphyrinogen IX
Staphylococcus aureus
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at pH 8.0 and 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03774
acifluorfen
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wild type enzyme at pH 7.5, temperature not specified in the publication
0.0003
protoporphyrinogen IX
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at pH 7.2 and 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with acifluorfen, sitting drop vapor diffusion method, using 2.4 M ammonium phosphate dibasic, 0.1 M Tris-HCl pH 7.5
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cobalt chelate column chromatography
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Ni-NTA column chromatography and S200 gel filtration
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Ni2+ affinity column chromatography
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Ni2+ Sepharose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) pLysS cells
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expressed in Escherichia coli BL21STAR DE3 pLysS cells
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the enzyme gene is fused in its 3'-end to a polynucleotide encoding six histidine residues and expressed in both Escherichia coli BL21(DE3) cells and Bacillus subtilis 168A cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F227R
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the mutant exhibits slight decrease in catalysis compared to the wild type enzyme
I176A
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the mutation leads to about 30fold decrease in catalytic efficiency compared to the wild type enzyme
K71A
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the mutation leads to about 50fold decrease in catalytic efficiency compared to the wild type enzyme
P64A
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the mutant exhibits a 14fold decrease in catalysis compared to the wild type enzyme
Y366N
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the mutation leads to about 100fold decrease in catalytic efficiency compared to the wild type enzyme
K71A
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the mutation leads to about 50fold decrease in catalytic efficiency compared to the wild type enzyme
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