Any feedback?
Information on EC 1.3.3.3 - coproporphyrinogen oxidase and Organism(s) Homo sapiens and UniProt Accession P36551
for references in articles please use BRENDA:EC1.3.3.3Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.3.3.3 coproporphyrinogen oxidaseSpecify your search results
Word Map
- 1.3.3.3
- heme
- protoporphyrinogen
- coproporphyria
- protoporphyrin
- porphyria
-
ferrochelatase
- uroporphyrinogen
-
5-aminolevulinic
- porphobilinogen
- tetrapyrrole
-
porphyrinogens
- medicine
-
oxygen-independent
-
coproporphyrinuria
- mg-protoporphyrin
-
ala-pdt
-
delta-aminolaevulinic
-
uroporphyrin
-
cutanea
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
coproporphyrinogen oxidase, coproporphyrinogen iii oxidase, hem13, cpox4, copro'gen oxidase, klhem13, coprogen oxidase, oxygen-dependent coproporphyrinogen iii oxidase, sll1185, hemn1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Coprogen oxidase
-
-
-
-
coproporphyrinogen III oxidase
coproporphyrinogenase
-
-
-
-
COX
-
-
-
-
CPO
coproporphyrinogen III oxidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
CPO catalyzes two sequential oxidative decarboxylations of propionate moieties on coproporphyrinogen-III forming protoporphyrinogen-IX through the monovinyl intermediate harderoporphyrinogen
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
coproporphyrinogen:oxygen oxidoreductase (decarboxylating)
-
CAS REGISTRY NUMBER
COMMENTARY
9076-84-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
harderoporphyrinogen + O2 + 2 H+
protoporphyrinogen + CO2 + H2O
substrate undergoes only the second decarboxylation
-
-
?
harderoporphyrinogen + O2 + H+
protoporphyrinogen IX + CO2 + H2O2
-
-
-
r
mesoporphyrinogen-VI + O2 + 2 H+
protoaetioporphyrin + 2 CO2 + 2 H2O
-
-
-
r
mesoporphyrinogen-VI + O2 + H+
? + CO2 + H2O
substrate undergoes only the first oxidative decarboxylation
-
-
?
17-ethylharderoporphyrinogen-III + O2 + 2 H+
17-ethylprotoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
3-[7,13-di(2-carboxy-ethyl)-17-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13-(2-carboxy-ethyl)-17-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + 3-[7,13-divinyl-17-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
-
?
3-[7,17-di(2-carboxy-ethyl)-13-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-17-(2-carboxy-ethyl)-13-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
-
?
3-[7-(2-carboxy-ethyl)-13,17-dibutyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13,17-dibutyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
-
?
3-[7-(2-carboxy-ethyl)-13,17-diethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13,17-diethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
-
?
3-[7-(2-carboxy-ethyl)-13,17-dipropyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13,17-dipropyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
-
?
3-[7-(2-carboxy-ethyl)-3,8,12,13,17,18-hexamethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-3,8,12,13,17,18-hexamethyl-porphyrinogen-2-yl]-propionic acid + CO2 + CO2
-
-
-
-
?
4,4'-[7,12-bis(2-carboxyethyl)-3,8,13,17-tetramethyl-5,10,15,20,22,24-hexahydroporphyrin-2,18-diyl]dibutanoic acid + O2 + 2 H+
? + 2 CO2 + 2 H2O
-
-
major product is a monovinylporphyrinogen, but some divinyl products are also generated. The incubation products are converted into the corresponding porphyrin methyl esters, and characterized by proton NMR spectroscopy and mass spectrometry
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
monovinyl intermediate that accumulates before being converted to an isomer
-
-
?
mesoporphyrinogen-VI + O2 + 2 H+
protoaetioporphyrin + 2 CO2 + 2 H2O
-
-
-
?
pentacarboxylate porphyrinogen 5dab + O2
dehydroisocoproporphyrinogen
-
poorer substrate than coproporphyrinogen-III
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
via harderoporphyrinogen intermediate production, overall reaction
-
-
?
coproporphyrinogen-III + O2 + 2 H+
harderoporphyrinogen + CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
harderoporphyrinogen + CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
harderoporphyrinogen + O2 + 2 H+
protoporphyrinogen-IX + CO2 + 2 H2O
-
-
-
?
harderoporphyrinogen + O2 + 2 H+
protoporphyrinogen-IX + CO2 + 2 H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
two oxidative decarboxylations sequentially to give a monovinylporphyrinogen intermediate. Regiospecific generation of harderoporphyrinogen as an intermediate by first converting the A ring side chain to a vinyl unit. Type isomers of coproporphyrinogen, overview
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
6th step in heme biosynthesis
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
enzyme catalyzes the 6th step in heme biosynthesis, heme might be a feed-back regulator of its synthesis by inhibiting the import of th enzyme into mitochondria
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Arg400, Arg262 and Arg401 are active amino acids critical for substrate binding and/or catalysis, Arg262 and 401 may coordinate carboxylate groups of coproporphyrinogen-III, while Asp400 may initiate deprotonation of substrate, resulting in oxidative decarboxylation
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
small amount of the monovinyl intermediate
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
CPO converts coproporphyrinogen III to protoporphyrinogen IX through harderoporphyrinogen IX
-
-
ir
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
O2 is added to the (preferentially deprotonated) pyrrole substrate (yielding a hydroperoxide, which then abstracts a proton from the reactive propionate substituent), the reaction may then proceed through HO2- elimination, followed by decarboxylation
-
-
?
coproporphyrinogen-III + O2 + 2H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen-III + O2 + 2H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
CPO catalyzes the conversion of coproporphyrinogen-III to protoporphyrinogen-IX, a divinyl product, via two sequential oxidative decarboxylations of the A and B ring propionates
-
-
?
additional information
?
-
-
pentacarboxylate porphyrinogens 5abc, 5abd, and 5acd are not metabolized
-
-
?
additional information
?
-
-
porphyrinogen 3,3'-[13,17-bis(carboxymethyl)-3,8,12,18-tetramethyl-5,10,15,20,22,24-hexahydroporphyrin-2,7-diyl]dipropanoic acid proves to be a relatively poor substrate for CPO compared to the natural substrate coproporphyrinogen-III, and only the A ring propionate moiety is processed to a significant extent. Substrate recognition and catalysis, overview
-
-
?
additional information
?
-
-
the 17-ethyl analogue of harderoporphyrinogen-III, but not its 13-ethyl isomer, is an excellent substrate for the enzyme in accord with a proposed model for the active site of the enzyme. Harderoporphyrinogen-VII, the monovinyl intermediate in the metabolism of coproporphyrinogen-IV, is an equally good substrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
via harderoporphyrinogen intermediate production, overall reaction
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
6th step in heme biosynthesis
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
enzyme catalyzes the 6th step in heme biosynthesis, heme might be a feed-back regulator of its synthesis by inhibiting the import of th enzyme into mitochondria
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bis(sulfosuccinimidyl) suberate
-
56% residual activity as compared to not cross-linked enzyme
sulfosuccinimidyl 4-(N-maleimidomethyl) cyclohexane-1-carboxylate
-
40% residual activity as compared to not cross-linked enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methotrexate
-
causes a 3fold accumulation of CPO at both the mRNA and protein levels
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000011
3-[7,13-di(2-carboxy-ethyl)-17-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.00085
3-[7,17-di(2-carboxy-ethyl)-13-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.011
3-[7-(2-carboxy-ethyl)-13,17-dibutyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.00056
3-[7-(2-carboxy-ethyl)-13,17-diethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.011
3-[7-(2-carboxy-ethyl)-13,17-dipropyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.00034
Coproporphyrinogen-III
wild-type, divinyl product, 37°C, pH not specified in the publication
0.00078
Coproporphyrinogen-III
mutant D400A, total product, 37°C, pH not specified in the publication
0.00079
Coproporphyrinogen-III
wild-type, total product, 37°C, pH not specified in the publication
0.00096
Coproporphyrinogen-III
mutant R401A, divinyl product, 37°C, pH not specified in the publication
0.0029
Coproporphyrinogen-III
mutant R401A, total product, 37°C, pH not specified in the publication
0.0051
Coproporphyrinogen-III
mutant R262A, divinyl product, 37°C, pH not specified in the publication
0.0087
Coproporphyrinogen-III
mutant R262A, total product, 37°C, pH not specified in the publication
0.00056
mesoporphyrinogen-VI
wild-type, monovinyl product, 37°C, pH not specified in the publication
0.002
mesoporphyrinogen-VI
mutant R401A, monovinyl product, 37°C, pH not specified in the publication
0.000066
Coproporphyrinogen III
-
in 250 mM Tris-HCl, 2.5 mM EDTA, pH 7.15, at 37°C
0.00054
Coproporphyrinogen III
-
pH and temperature not specified in the publication
0.00034
Coproporphyrinogen-III
wild-type, production to intermediate divinyl
0.00096
Coproporphyrinogen-III
mutant R401A, production to intermediate divinyl
0.0051
Coproporphyrinogen-III
mutant R262A, production to intermediate divinyl
0.00056
mesoporphyrinogen-VI
wild-type, production to intermediate monovinyl
0.002
mesoporphyrinogen-VI
mutant R401A, production to intermediate monovinyl
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
3-[7,13-di(2-carboxy-ethyl)-17-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.0283
3-[7,17-di(2-carboxy-ethyl)-13-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.000006
3-[7-(2-carboxy-ethyl)-13,17-dibutyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.0063
3-[7-(2-carboxy-ethyl)-13,17-diethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.000165
3-[7-(2-carboxy-ethyl)-13,17-dipropyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.017
Coproporphyrinogen III
-
pH and temperature not specified in the publication
0.000002
Coproporphyrinogen-III
mutant D400A, total product, 37°C, pH not specified in the publication
0.000012
Coproporphyrinogen-III
mutant R262A, divinyl product, 37°C, pH not specified in the publication
0.00042
Coproporphyrinogen-III
mutant R262A, total product, 37°C, pH not specified in the publication
0.00167
Coproporphyrinogen-III
mutant R401A, divinyl product, 37°C, pH not specified in the publication
0.02
Coproporphyrinogen-III
mutant R401A, total product, 37°C, pH not specified in the publication
0.02667
Coproporphyrinogen-III
wild-type, divinyl product, 37°C, pH not specified in the publication
0.045
Coproporphyrinogen-III
wild-type, total product, 37°C, pH not specified in the publication
0.002
mesoporphyrinogen-VI
mutant R401A, monovinyl product, 37°C, pH not specified in the publication
0.0063
mesoporphyrinogen-VI
wild-type, monovinyl product, 37°C, pH not specified in the publication
0.00167
Coproporphyrinogen-III
mutant R401A, production to intermediate divinyl
0.0267
Coproporphyrinogen-III
wild-type, production to intermediate divinyl
0.002
mesoporphyrinogen-VI
mutant R401A, production to intermediate monovinyl
0.0063
mesoporphyrinogen-VI
wild-type, production to intermediate monovinyl
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.5
Coproporphyrinogen III
-
pH and temperature not specified in the publication
0.000003
Coproporphyrinogen-III
mutant R262A, divinyl product, 37°C, pH not specified in the publication
0.000027
Coproporphyrinogen-III
mutant D400A, total product, 37°C, pH not specified in the publication
0.000048
Coproporphyrinogen-III
mutant R262A, total product, 37°C, pH not specified in the publication
0.00183
Coproporphyrinogen-III
mutant R401A, divinyl product, 37°C, pH not specified in the publication
0.00683
Coproporphyrinogen-III
mutant R401A, total product, 37°C, pH not specified in the publication
0.0567
Coproporphyrinogen-III
wild-type, total product, 37°C, pH not specified in the publication
0.07
Coproporphyrinogen-III
wild-type, divinyl product, 37°C, pH not specified in the publication
0.001
mesoporphyrinogen-VI
mutant R401A, monovinyl product, 37°C, pH not specified in the publication
0.0113
mesoporphyrinogen-VI
wild-type, monovinyl product, 37°C, pH not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
-
human enzyme is imported in isolated rat mitochondria, heme inhibits the mitochondrial import of the enzyme completely at 0.02 mM concentration
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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. 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
metabolism
physiological function
-
CPOX is a mitochondrial enzyme in the heme biosynthetic pathway that catalyzes the conversion of coproporphyrinogen III to protoporphyrinogen IX
additional information
metabolism
-
CPOX is a mitochondrial enzyme in the heme biosynthetic pathway that catalyzes the conversion of coproporphyrinogen III to protoporphyrinogen IX
metabolism
-
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
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
-
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
-
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HEM6_HUMAN
454
0
50152
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37500
38000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D400A
G279R
novel nucleotide transition found, is unstable, and produces ca. 2-5% of activity compared with the wild-type CPO
H148A
retains 39% of wild type enzyme activity for the overall conversion of coproporphyrinogen-III to protoporphyrinogen-IX
H158A
the mutant exhibits approximately 50fold lower activity than wild type recombinant CPO for the conversion of coproporphyrinogen-III to protoporphyrinogen-IX
H197A
the mutant exhibits approximately 50fold lower activity for the overall conversion of coproporphyrinogen-III to protoporphyrinogen-IX than wild type recombinant CPO, but the second oxidative decarboxylation step is not impaired, with mutant enzyme H197A retaining 100% of the wild type activity using harderoporphyrinogen as substrate
H227A
catalyzes the conversion of coproporphyrinogen-III to protoporphyrinogen-IX at a rate almost 2fold that of the wild type enzyme
K404E
a naturally occuring mutant derived from patients with harderoporphyria, the mutant produces less harderoporphyrinogen. The K404E mutation leads to diminishment of the second step of the decarboxylation reaction during the conversion of coproporphyrinogen to protoporphyrinogen. The mutant enzyme forms dimers
K404H
site-directed mutagenesis, the mutant produces a high level of harderoporphyrinogen with low production of protoporphyrinogen similar to mutant K404E
K404Q
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
R262A
R401A
A203T
-
natural mutation due to single nucleotide substitution 607G>A, identified in a patient with hereditary coproporphyria
C991T/C1339T
-
identification of 2 coexisting mutations, C991T and C1339T, on a single allele in the enzyme' gene in Swedish patients with hereditary coproporphyria, biochemical analysis of the patients carrying the mutations, overview
D400A
D400R
-
less than 1% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
F395G
-
4% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
F405G
-
1% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
G188W
-
a naturally occuring frameshift mutation p.Gly188TrpfsX45 in hereditary coproporphyria patient from Italian population, phenotype, overview
G242C
G402A
-
less than 1% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
K404E
K404N
-
61% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
L288W
-
the mutation is associated with hereditary coproporphyria with posterior reversible encephalopathy
L398P
N272H
-
natural polymorphism, twofold decrease in affinity for coproporphyrinogen-III. Specific activity in liver samples is 40-50% lower than in wild-type
R262A
R401A
R401D
-
45% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
R401K
-
63% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
R401W
-
75% of residual activity compared with wild-type CPO, causes substantial accumulation of harderoporphyrinogen
S245F
T403N
-
31% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
Y399L
-
81% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
additional information
D400A
the mutation impairs the catalytic ability of CPO relative to the wild type enzyme, not able to form divinyl products, but the Km value for coproporphyrinogen-III does not change significantly compared to the wild-type enzyme
D400A
site-directed mutagenesis, the inactive mutant D400A remains in a monomeric form
D400A
mutation severely impaires the catalytic activity, mutant performs, on average, less than a single turnover
R262A
poor catalyst for the production of a divinyl product with a catalytic efficiency less than 0.01% compared to wild-type, including a 15fold higher Km for coproporphyrinogen-III
R262A
mutation results in decreased kcat values and increased Km values. No product formation is detected with sunstrate mesoporphyrogen-VI
R401A
the efficiency of divinyl product formation is about 3% compared to the wild type enzyme
R401A
mutation results in decreased kcat values and increased Km values. The mutant is able to convert mesoporphyrogen-VI to monovinyl product, although over 10fold less efficiently than wild-type
D400A
impaired catalytic ability, with 0.047% of wild-type total product efficiency
D400A
the mutant produces no divinyl product, the Km value for coproporphyrinogen-III does not change significantly compared to the wild-type enzyme
G242C
-
natural mutation due to single nucleotide substitution 724G>T, identified in a patient with hereditary coproporphyria
G242C
-
a naturally occuring missense mutation in hereditary coproporphyria patient from Italian population, phenotype, overview
K404E
-
66% of residual activity compared with wild-type CPO, causes substantial accumulation of harderoporphyrinogen
L398P
-
natural mutation due to single nucleotide substitution 1193T>C, identified in a patient with hereditary coproporphyria
L398P
-
a naturally occuring missense mutation in hereditary coproporphyria patient from Italian population, phenotype, overview
R262A
impaired catalytic ability, with 0.00036% of wild-type total product efficiency
R262A
the mutant CPO is a poor catalyst for the production of a divinyl product, with a catalytic efficiency less than 0.01% compared to the wild type enzyme including a 15fold higher Km for coproporphyrinogen-III
R401A
impaired catalytic ability, with 44% of wild-type total product efficiency
R401A
the efficiency of divinyl product formation for mutant enzyme R401A is about 3% compared to wild type CPO, with a 3fold increase in the Km value for coproporphyrinogen-III
S245F
-
natural mutation due to single nucleotide substitution 734C>T, identified in a patient with hereditary coproporphyria
S245F
-
a naturally occuring missense mutation in hereditary coproporphyria patient from Italian population, phenotype, overview
additional information
enzyme engineering of mutant homodimer and heterodimer of coproporphyinogen oxidase. The His-tagged mutant enzyme forms a heterodimer in association with the HA-tagged wild-type enzyme, The monomeric form of mutated CPOX does not show any activity and homodimeric enzymes derived from hereditary coproporphyria (HCP) mutant show low activity (about 20% of the control). The chimeric heterodimers with wild-type and mutated subunits from HCP patients show low protoporphyrinogen producing activity. Some mutations of amino acids 401-404 are associated with marked accumulation of reaction intermediate harderoporphyrinogen, with a decrease in the production of protoporphyrinogen, whereas K404E derived from patients with harderoporphyria produces less harderoporphyrinogen. Functional analysis of heterodimer of mutant/wild-type complex, heterophilic forms of His-R388W/HA-wild-type, His-R391W/HA-wild-type, His-D400A/HA-wild-type, His-R401W/HA-wild-type, His-G402D/HA-wild-type and His-K404E/HA-wild-type, overview
additional information
-
enzyme engineering of mutant homodimer and heterodimer of coproporphyinogen oxidase. The His-tagged mutant enzyme forms a heterodimer in association with the HA-tagged wild-type enzyme, The monomeric form of mutated CPOX does not show any activity and homodimeric enzymes derived from hereditary coproporphyria (HCP) mutant show low activity (about 20% of the control). The chimeric heterodimers with wild-type and mutated subunits from HCP patients show low protoporphyrinogen producing activity. Some mutations of amino acids 401-404 are associated with marked accumulation of reaction intermediate harderoporphyrinogen, with a decrease in the production of protoporphyrinogen, whereas K404E derived from patients with harderoporphyria produces less harderoporphyrinogen. Functional analysis of heterodimer of mutant/wild-type complex, heterophilic forms of His-R388W/HA-wild-type, His-R391W/HA-wild-type, His-D400A/HA-wild-type, His-R401W/HA-wild-type, His-G402D/HA-wild-type and His-K404E/HA-wild-type, overview
additional information
loss of inducibility due to the promoter mutations occur reproducibly with all C/EBP isoforms, arguing that CPO promoter activity depends upon C/EBP site location, and not simply upon inherent binding affinity, hypothetical modeling, overview
additional information
-
a duplication of a T in position 561 of the coding sequence, i.e.561dupT in exon 2 results in a frameshift that gives rise to a stop codon 45 residues downstream Glycine at position 188, i.e. p.Gly188TrpfsX45. Mutation identified in a patient with hereditary coproporphyria
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant HA-tagged wild-type enzyme and His-tagged mutant enzyme from Escherichia coli by nickel and heparin affinity chromatography, respectively
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, eighteen functional C/EBP binding motifs in the mCPO promoter are found, all are predicted to bind C/EBPs with moderate or higher affinity
mature form of wild-type CPOX cloned into pET-22, wild-type and mutant protein expressed in Escherichia coli BL21(DE3)plysS
recombinant coexpression of HA-tagged wild-type enzyme from healthy donors and of His-tagged mutant enzyme from HCP patients in Escherichia coli strain BL21, the His-enzyme forms a heterodimer in association with the HA-tagged enzyme, The monomeric form of mutated CPOX does not show any activity and homodimeric enzymes derived from HCP mutant show low activity (about 20% of the control). The chimeric heterodimers with wild-type and mutated subunits from HCP patients show low protoporphyrinogen producing activity. The active site of the enzyme involved in the second step of decarboxylation is encoded in exon 6
gene CPO, located on chromosome 3q11.2, DNA and amino acid sequence determination and analysis, genotyping of an Italian population
-
into vector PCRII-TOPO, transferred into vector pcDNA3.1(-), and transfection of LNCaP cells and Cos-7 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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. When MEL cells are incubated in 1% DMSO, large amounts of porphyrins are produced and under these conditions C/EBPbeta expression is upregulated. Concurrently, CPO expression is increased at both mRNA and protein levels, and higher levels of protoporphyrinogen-IX are generated in response to exogenously added 5-aminolevulic acid. LNCaP carcinoma lines respond to calcitriol with increases in enzyme CPO and protoporphyrinogen-IX levels concurrently. The human CPO gene upstream region contains many competent C/EBP binding sites, analysis of C/EBPbeta and enzyme CPO interaction analysis, binding site analysis, overview. Eighteen functional C/EBP binding motifs in the mCPO promoter are found, all are predicted to bind C/EBPs with moderate or higher affinity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
analysis
-
mass spectrometric assay for the two-step decarboxylative oxidation of coproporphyrinogen III to protoporphyrinogen IX catalyzed by CPO in mitochondria from human lymphocytes. The assay shows good reproducibility, uses simple workup by liquid-liquid extraction of enzymatic products, and employs commercially available substrates and internal standard. It was developed for use in clinical diagnostics of the inherited disorder hereditary coproporphyria
medicine
medicine
first patient with porphyria where both CPO and delta-aminolaevulinic acid dehydratase are deficient at the molecular level
medicine
His158 may have a role in the active site of CPO, none of the conserved histidine residues of the enzyme are essential for catalytic activity although changes in histidines are implicated in the disease state hereditary coproporphyria
medicine
the regulation of the enzyme is important in differentiation therapy for cancer treatment
medicine
-
abnormal route for heme biosynthesis in humans suffering from porphyria cutanea tarda or related syndromes such as hexachlorobenzene poisoning
medicine
-
COPX4 polymorphism is associated with the atypical keto-isocoproporphyrin, utility of urinary porphyrin changes as a biomarker of exposure and potential toxicity in subjects with mercury exposure
medicine
-
CPOX4 polymorphism may affect susceptibility for specific neurobehavioral functions associated with mercury exposure in human subjects
medicine
-
increase of severity of porphyrias with monovinyl accumulation, ability of the increased levels of C-IV to compete with the authentic substrate has important implications for clinical porphyrias
medicine
-
patients with the specific mutation K404E have a unifying syndrome in which hematological disorders predominate, the so called harderoporphyria, harderoporphyric patients exhibit iron overload secondary to dyserythropoiesis
medicine
-
natural polymorphism A814C leading to mutation N272H results in twofold decrease in affinity for coproporphyrinogen-III. Specific activity in liver samples is 40-50% lower than in wild-type, mutation may predispose to impaired heme biosynthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gross, U.; Puy, H.; Kuhnel, U.; Meissauer, U.; Deybach, J.C.; Jacob, K.; Martasek, P.; Nordmann, Y.; Doss, M.O.
Molecular, immunological, enzymatic and biochemical studies of coproporphyrinogen oxidase deficiency in a family with hereditary coproporphyria
Cell. Mol. Biol.
48
49-55
2002
Homo sapiens
Martasek, P.; Camadro, J.M.; Raman, R.S.; Lecomte, M.C.; Le Caer, J.P.; Demeler, B.; Grandchamp, B.; Labbe, P.
Human coproporphyrinogen oxidase. Biochemical characterization of recombinant normal and R231W mutated enzymes expressed in E. coli as soluble, catalytically active homodimers
Cell. Mol. Biol.
43
47-58
1997
Homo sapiens
Medlock, A.E.; Dailey, H.A.
Human coproporphyrinogen oxidase is not a metalloprotein
J. Biol. Chem.
271
32507-32510
1996
Homo sapiens
Susa, S.; Daimon, M.; Ono, H.; Li, S.; Yoshida, T.; Kato, T.
Heme inhibits the mitochondrial import of coproporphyrinogen oxidase. Comments
Blood
100
4678-4679
2002
Homo sapiens
Wiman, A.; Floderus, Y.; Harper, P.
Two novel mutations and coexistence of the 991C>T and the 1339C>T mutation on a single allele in the coproporphyrinogen oxidase gene in Swedish patients with hereditary coproporphyria
J. Hum. Genet.
47
407-412
2002
Homo sapiens
Stephenson, J.R.; Thomas, N.E.; Friesen, J.A.; Jones, M.A.
Use of crosslinking to assess subunit interaction of recombinant human coproporphyrinogen oxidase
Am. J. Biochem. Biotechnol.
1
103-106
2005
Homo sapiens
-
Cooper, C.L.; Stob, C.M.; Jones, M.A.; Lash, T.D.
Metabolism of pentacarboxylate porphyrinogens by highly purified human coproporphyrinogen oxidase: further evidence for the existence of an abnormal pathway for heme biosynthesis
Bioorg. Med. Chem.
13
6244-6251
2005
Homo sapiens
Sinha, A.K.; Anand, S.; Ortel, B.J.; Chang, Y.; Mai, Z.; Hasan, T.; Maytin, E.V.
Methotrexate used in combination with aminolaevulinic acid for photodynamic killing of prostate cancer cells
Br. J. Cancer
95
485-495
2006
Homo sapiens
Akagi, R.; Inoue, R.; Muranaka, S.; Tahara, T.; Taketani, S.; Anderson, K.E.; Phillips, J.D.; Sassa, S.
Dual gene defects involving delta-aminolaevulinate dehydratase and coproporphyrinogen oxidase in a porphyria patient
Br. J. Haematol.
132
237-243
2006
Homo sapiens (P36551)
Schmitt, C.; Gouya, L.; Malonova, E.; Lamoril, J.; Camadro, J.M.; Flamme, M.; Rose, C.; Lyoumi, S.; Da Silva, V.; Boileau, C.; Grandchamp, B.; Beaumont, C.; Deybach, J.C.; Puy, H.
Mutations in human CPO gene predict clinical expression of either hepatic hereditary coproporphyria or erythropoietic harderoporphyria
Hum. Mol. Genet.
14
3089-3098
2005
Homo sapiens
Cooper, C.L.; Lash, T.D.; Jones, M.A.
Kinetic evaluation of human cloned coproporphyrinogen oxidase using a ring isomer of the natural substrate
Med. Sci. Monit.
11
BR420-BR425
2005
Homo sapiens
Gitter, S.J.; Cooper, C.L.; Friesen, J.A.; Jones, M.A.
Investigation of the catalytic and structural roles of conserved histidines of human coproporphyrinogen oxidase using site-directed mutagenesis
Med. Sci. Monit.
13
BR1-BR10
2006
Homo sapiens (P36551), Homo sapiens
Echeverria, D.; Woods, J.S.; Heyer, N.J.; Rohlman, D.; Farin, F.M.; Li, T.; Garabedian, C.E.
The association between a genetic polymorphism of coproporphyrinogen oxidase, dental mercury exposure and neurobehavioral response in humans
Neurotoxicol. Teratol.
28
39-48
2006
Homo sapiens
Stephenson, J.R.; Stacey, J.A.; Morgenthaler, J.B.; Friesen, J.A.; Lash, T.D.; Jones, M.A.
Role of aspartate 400, arginine 262, and arginine 401 in the catalytic mechanism of human coproporphyrinogen oxidase
Protein Sci.
16
401-410
2007
Homo sapiens, Homo sapiens (P36551)
Heyer, N.J.; Bittner, A.C.; Echeverria, D.; Woods, J.S.
A cascade analysis of the interaction of mercury and coproporphyrinogen oxidase (CPOX) polymorphism on the heme biosynthetic pathway and porphyrin production
Toxicol. Lett.
161
159-166
2006
Homo sapiens
Wang, Y.; Gatti, P.; Sadilek, M.; Scott, C.R.; Turecek, F.; Gelb, M.H.
Direct assay of enzymes in heme biosynthesis for the detection of porphyrias by tandem mass spectrometry. Uroporphyrinogen decarboxylase and coproporphyrinogen III oxidase
Anal. Chem.
80
2599-2605
2008
Homo sapiens
Silva, P.J.; Ramos, M.J.
A comparative density-functional study of the reaction mechanism of the O2-dependent coproporphyrinogen III oxidase
Bioorg. Med. Chem.
16
2726-2733
2008
Homo sapiens, synthetic construct
Morgenthaler, J.B.; Barto, R.L.; Lash, T.D.; Jones, M.A.
Use of di- and tripropionate substrate analogs to probe the active site of human recombinant coproporphyrinogen oxidase
Med. Sci. Monit.
14
BR1-BR7
2008
Homo sapiens
Bjoerkman, L.; Vahter, M.
A cascade analysis of the interaction of mercury and coproporphyrinogen oxidase (CPOX) polymorphism on the heme biosynthetic pathway and porphyrin production by Heyer et al. [Toxicol. Lett. 161 (2006) 159-166]. Comment
Toxicol. Lett.
169
91-92
2007
Homo sapiens
Heyer, N.J.; Bittner, A.C.; Echeverria, D.; Woods, J.S.
A cascade analysis of the interaction of mercury and coproporphyrinogen oxidase (CPOX) polymorphism on the heme biosynthetic pathway and porphyrin production by Heyer et al. [Toxicol. Lett. 161 (2006) 159-166]. Reply
Toxicol. Lett.
169
93-94
2007
Homo sapiens
Aurizi, C.; Lupia Palmieri, G.; Barbieri, L.; Macri, A.; Sorge, F.; Usai, G.; Biolcati, G.
Four novel mutations of the coproporphyrinogen III oxidase gene
Cell. Mol. Biol.
55
15-18
2009
Homo sapiens
Li, T.; Woods, J.S.
Cloning, expression, and biochemical properties of CPOX4, a genetic variant of coproporphyrinogen oxidase that affects susceptibility to mercury toxicity in humans
Toxicol. Sci.
109
228-236
2009
Homo sapiens
Lash, T.D.; Mani, U.N.; Keck, A.S.; Jones, M.A.
Normal and abnormal heme biosynthesis. 6. Synthesis and metabolism of a series of monovinylporphyrinogens related to harderoporphyrinogen. Further insights into the oxidative decarboxylation of porphyrinogen substrates by coproporphyrinogen oxidase
J. Org. Chem.
75
3183-3192
2010
Saccharomyces cerevisiae, Gallus gallus, Homo sapiens
Lash, T.D.; Lamm, T.R.; Schaber, J.A.; Chung, W.H.; Johnson, E.K.; Jones, M.A.
Normal and abnormal heme biosynthesis. Part 7. Synthesis and metabolism of coproporphyrinogen-III analogues with acetate or butyrate side chains on rings C and D. Development of a modified model for the active site of coproporphyrinogen oxidase
Bioorg. Med. Chem.
19
1492-1504
2011
Gallus gallus, Homo sapiens
Kim, D.H.; Hino, R.; Adachi, Y.; Kobori, A.; Taketani, S.
The enzyme engineering of mutant homodimer and heterodimer of coproporphyinogen oxidase contributes to new insight into hereditary coproporphyria and harderoporphyria
J. Biochem.
154
551-559
2013
Homo sapiens (P36551), Homo sapiens
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
Stephenson, J.R.; Stacey, J.A.; Morgenthaler, J.B.; Friesen, J.A.; Lash, T.D.; Jones, M.A.
Role of aspartate 400, arginine 262, and arginine 401 in the catalytic mechanism of human coproporphyrinogen oxidase
Protein Sci.
16
401-410
2007
Homo sapiens (P36551), Homo sapiens
Lambie, D.; Florkowski, C.; Sies, C.; Raizis, A.; Siu, W.K.; Towns, C.
A case of hereditary coproporphyria with posterior reversible encephalopathy and novel coproporphyrinogen oxidase gene mutation c.863T>G (p.Leu288Trp)
Ann. Clin. Biochem.
55
616-619
2018
Homo sapiens
Maytin, E.V.; Anand, S.; Riha, M.; Lohser, S.; Tellez, A.; Ishak, R.; Karpinski, L.; Sot, J.; Hu, B.; Denisyuk, A.; Davis, S.C.; Kyei, A.; Vidimos, A.
5-Fluorouracil enhances protoporphyrin IX accumulation and lesion clearance during photodynamic therapy of actinic keratoses A mechanism-based clinical trial
Clin. Cancer Res.
24
3026-3035
2018
Homo sapiens
Loskove, Y.; Yasuda, M.; Chen, B.; Nazarenko, I.; Cody, N.; Desnick, R.J.
Acute hepatic porphyrias Identification of 46 hydroxymethylbilane synthase, 11 coproporphyrinogen oxidase, and 20 protoporphyrinogen oxidase novel mutations
Mol. Genet. Metab.
128
352-357
2019
Homo sapiens (P36551), Homo sapiens
EXTERNAL LINKS (specific for EC-Number 1.3.3.3)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
