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Information on EC 1.3.3.3 - coproporphyrinogen oxidase and Organism(s) Mus musculus and UniProt Accession P36552

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EC Tree
     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.3 With oxygen as acceptor
                1.3.3.3 coproporphyrinogen oxidase
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This record set is specific for:
Mus musculus
UNIPROT: P36552 not found.
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
coproporphyrinogen oxidase, coproporphyrinogen iii oxidase, hem13, cpox4, copro'gen oxidase, coprogen oxidase, klhem13, oxygen-dependent coproporphyrinogen iii oxidase, sll1185, hemn1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
coproporphyrinogen oxidase
-
Coprogen oxidase
-
-
-
-
coproporphyrinogen III oxidase
coproporphyrinogenase
-
-
-
-
COX
-
-
-
-
CPOX
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
coproporphyrinogen:oxygen oxidoreductase (decarboxylating)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9076-84-0
-
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 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
-
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
NATURAL SUBSTRATE
NATURAL 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 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
-
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
1.05 atoms per enzyme
Fe2+
-
trace amounts
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5-dithiobis(2-nitrobenzoic acid)
-
significant inhibition, IC50: 0.05 mM
sodium cholate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lecithin
Non-ionic detergents
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.047 - 0.32
Coproporphyrinogen-III
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
5,5-dithiobis(2-nitrobenzoic acid)
Mus musculus
-
significant inhibition, IC50: 0.05 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.06
-
-
0.28
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
nude mice
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
physiological function
coproporphyrinogen oxidase (CPO) is a rate-limiting enzyme in the heme pathway responsible for the conversion of coproporphyrinogen III into protoporphyrin IX
metabolism
-
the enzyme is required for heme biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HEM6_MOUSE
443
0
49715
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
2 * 35000, SDS-PAGE
37000
-
x * 37000, SDS-PAGE
70000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 37000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H158A
-
complete loss of activity, decreased stability, no copper content
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
tends to aggregate during prolonged storage at 4°C
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity, chromatography steps
-
to homogeneity, recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, the murine CPO gene upstream region contains many competent C/EBP binding sites
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in subcutaneous A431 tumors in mice, pretreatment with vitamin D induces the expression of CCAAT-enhancer binding proteins (C/EBPbeta) isoforms, and of coproporphyrinogen oxidase (CPO). Vitamin D leads to strong accumulation of protoporphyrinogen-IX, PpIX. The murine CPO gene upstream region contains many competent C/EBP binding sites, analysis of C/EBPbeta and enzyme CPO interaction analysis, binding site analysis, overview. All C/EBP sites in murine CPO are asymmetric, with wide divergence between the two half-sites, fifteen functional C/EBP binding motifs in the mCPO promoter are found
addition of NaHS suppresses enzyme promoter activity
-
cystathionine gamma-lyase deficient mice exhibit elevated enzyme expression in the liver
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoshinaga, T.
Purification and properties of coproporphyrinogen III oxidase from bovine liver
Methods Enzymol.
281
355-367
1997
Bos taurus, Mus musculus
Manually annotated by BRENDA team
Kohno, H.; Furukawa, T.; Yoshinaga, T.; Tokunaga, R.; Taketani, S.
Coproporhyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation
J. Biol. Chem.
268
21359-21363
1993
Bos taurus, Mus musculus
Manually annotated by BRENDA team
Kohno, H.; Furukawa, T.; Tokunaga, R.; Taketani, S.; Yoshinaga, T.
Mouse coprophorphyrinogen oxidase is a copper-containing enzyme: expression in E. coli and site-directed mutagenesis
Biochim. Biophys. Acta
1292
156-162
1996
Mus musculus
Manually annotated by BRENDA team
Bogard, M.; Camadro, J.M.; Labbe, P.
Purification and properties of mouse liver coproporphyrinogen oxidase
Eur. J. Biochem.
181
417-421
1989
Mus musculus
Manually annotated by BRENDA team
Anand, S.; Rollakanti, K.R.; Brankov, N.; Brash, D.E.; Hasan, T.; Maytin, E.V.
Fluorouracil enhances photodynamic therapy of squamous cell carcinoma via a p53-independent mechanism that increases protoporphyrin IX levels and tumor cell death
Mol. Cancer Ther.
16
1092-1101
2017
Homo sapiens (P36551), Mus musculus (P36552), Mus musculus
Manually annotated by BRENDA team
Modis, K.; Ramanujam, V.; Govar, A.; Lopez, E.; Anderson, K.; Wang, R.; Szabo, C.
Cystathionine-gamma-lyase (CSE) deficiency increases erythropoiesis and promotes mitochondrial electron transport via the upregulation of coproporphyrinogen III oxidase and consequent stimulation of heme biosynthesis
Biochem. Pharmacol.
169
113604
2019
Mus musculus
Manually annotated by BRENDA team