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Information on EC 1.3.3.3 - coproporphyrinogen oxidase
for references in articles please use BRENDA:EC1.3.3.3
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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
The enzyme appears in viruses and cellular organisms
- 1.3.3.3
- heme
- protoporphyrinogen
- coproporphyria
- protoporphyrin
- porphyria
-
ferrochelatase
- uroporphyrinogen
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5-aminolevulinic
- porphobilinogen
- tetrapyrrole
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porphyrinogens
- medicine
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oxygen-independent
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coproporphyrinuria
- mg-protoporphyrin
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ala-pdt
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delta-aminolaevulinic
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uroporphyrin
-
cutanea
- analysis
showSynonyms
coproporphyrinogen oxidase, coproporphyrinogen iii oxidase, hem13, cpox4, copro'gen oxidase, klhem13, coprogen oxidase, oxygen-dependent coproporphyrinogen iii oxidase, sll1185, hemn1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
copro'gen oxidase
Coprogen oxidase
coproporphyrinogen III oxidase
coproporphyrinogen oxidase
coproporphyrinogenase
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COX
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CPO
CPOX
HemF
LIN2
oxygen-dependent coproporphyrinogen III oxidase
Coprogen oxidase
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coproporphyrinogen III oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
substrate binding at the active site, structure and mechanism, catalytic mechanism
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
2 possible catalytic pathways of the reaction, overview, Tyrp274 is catalytically important, the following residues are not important for enzyme activity: Cys167, Tyr135, Tyr160, Tyr170, Tyr213, Tyr240, Tyr276, Trp36, Trp123, Trp166, and Trp198
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
active site structure
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
substrate binding at the active site, structure and mechanism, catalytic mechanism
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
analysis of catalytic mechanism, modeling of active site structure
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
reaction starts by O2 addition to the pyrrole substrate yielding a hydroperoxide, which then abstracts a proton from the reactive propionate substituent, and the reaction may then proceed through H2O elimination, followed by decarboxylation
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
reaction mechanism, substrate docking study and binding mode, involving residues H131, R135, D274, and R275, and active site analysis using crystal structures, molecular dynamics simulations, overview. Selectivity of the active site, formed by His131, Asn133, and Ser117, toward substituted tetrapyrroles, nonoccurrence of catalysis on the C and D rings of the tetrapyrrole. The carbonyl oxygen of G276 intervenes in the substrate anchoring by hydrogen bonding of the ring D pyrrole NH group. The pyrrole ring is very unlikely to undergo deprotonation during the catalytic cycle
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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oxidative decarboxylation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
3,8-divinyl-chlorophyllide a biosynthesis I (aerobic, light-dependent), 3,8-divinyl-chlorophyllide a biosynthesis III (aerobic, light independent), heme b biosynthesis I (aerobic), heme b biosynthesis V (aerobic)
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SYSTEMATIC NAME
IUBMB Comments
coproporphyrinogen:oxygen oxidoreductase (decarboxylating)
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CAS REGISTRY NUMBER
COMMENTARY
9076-84-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
17-(3-carboxypropyl)-5,10,15,20,22,24-hexahydro-3,7,13,18-tetramethyl-21H,23H-porphine-2,8,12-tripropanoic acid + O2
? + CO2
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Substrates: generates a vinyl group on ring-A
Products: -
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?
17-ethylharderoporphyrinogen-III + O2 + 2 H+
17-ethylprotoporphyrinogen-IX + 2 CO2 + 2 H2O
2,4-bis-(beta-hydroxypropionic acid) deuteroporphyrinogen IX + O2
protoporphyrinogen IX + CO2
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Substrates: one sixth of the rate compared to coproporhyrinogen-III
Products: -
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?
2-beta-hydroxypropionic acid-4-propionic acid deuteroporphyrinogen IX + O2
protoporphyrinogen IX + CO2
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Substrates: 80% of the activity compared to coproporphyrinogen-III
Products: -
Products: -
?
2-propionic acid-4-beta-hydroxypropionic acid deuteroporphyrinogen IX + O2
protoporphyrinogen IX + CO2
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Substrates: 8% of the activity compared to coproporphyrinogen-III
Products: -
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?
3-[7,13-di(2-carboxy-ethyl)-17-benzyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13-(2-carboxy-ethyl)-17-benzyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
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Substrates: -
Products: -
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?
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
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Substrates: -
Products: -
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?
3-[7,17-di(2-carboxy-ethyl)-13-benzyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-17-(2-carboxy-ethyl)-13-benzyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
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Substrates: -
Products: -
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?
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
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Substrates: -
Products: -
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?
3-[7-(2-carboxy-ethyl)-13,17-di-tert-butyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13,17-di-tert-butyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
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Substrates: -
Products: -
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?
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
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Substrates: -
Products: -
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?
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-diisopropyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13,17-diisopropyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
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Substrates: -
Products: -
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?
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
-
Substrates: -
Products: -
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?
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
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Substrates: -
Products: -
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?
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
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Substrates: -
Products: -
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?
3-[7-vinyl-17-(2-carboxy-ethyl)-13-benzyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[2,7-divinyl-13-benzyl-3,8,12,18-tetramethyl-porphyrinogen-17-yl]-propionic acid + CO2
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Substrates: -
Products: -
Products: -
?
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
5,10,15,20,22,24-hexahydro-3,7,13,18-tetramethyl-21H,23H-porphine-2,8,12,17-tripropanoic acid 17-methyl ester + O2
? + CO2
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Substrates: very poor substrate
Products: -
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?
coproporphyrinogen-III + O2 + 2 H+
harderoporphyrinogen + CO2 + 2 H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
harderoporphyrinogen + O2 + 2 H+
protoporphyrinogen + CO2 + H2O
Substrates: substrate undergoes only the second decarboxylation
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?
harderoporphyrinogen + O2 + 2 H+
protoporphyrinogen-IX + CO2 + 2 H2O
Substrates: -
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?
harderoporphyrinogen + O2 + H+
protoporphyrinogen IX + CO2 + H2O2
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Substrates: -
Products: -
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r
harderoporphyrinogen-VII + O2 + 2 H+
?
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Substrates: a monovinyl intermediate in the metabolism of coproporphyrinogen-IV
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?
isoharderoporphyrinogen + O2 + 2 H+
?
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Substrates: very low activity
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mesoporphyrinogen-VI + O2 + 2 H+
protoaetioporphyrin + 2 CO2 + 2 H2O
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Substrates: similar oxidation rate compared to coproporphyrinogen-III
Products: -
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?
mesoporphyrinogen-VI + O2 + H+
? + CO2 + H2O
Substrates: substrate undergoes only the first oxidative decarboxylation
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?
pentacarboxylate porphyrinogen 5dab + O2
dehydroisocoproporphyrinogen
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Substrates: poorer substrate than coproporphyrinogen-III
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?
pentacarboxylate porphyrinogen III + O2
dehydroisocoproporphyrinogen + CO2
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Substrates: half of the activity compared to coproporphyrinogen oxidase-III
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?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
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Substrates: -
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?
protoporphyrinogen-IX + O2
protoporphyrin IX + CO2
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Substrates: capacity to oxidize not only coproporphyrinogen-III but also protoporphyrinogen-IX
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?
protoporphyrinogen-IX + O2
protoporphyrin-IX + CO2
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Substrates: capacity to oxidize not only coproporphyrinogen-III but also protoporphyrinogen-IX
Products: -
Products: -
?
17-ethylharderoporphyrinogen-III + O2 + 2 H+
17-ethylprotoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
17-ethylharderoporphyrinogen-III + O2 + 2 H+
17-ethylprotoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
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Substrates: -
Products: major product is a monovinylporphyrinogen, but some divinyl product is also generated. The incubation products are converted into the corresponding porphyrin methyl esters, and characterized by proton NMR spectroscopy and mass spectrometry
Products: major product is a monovinylporphyrinogen, but some divinyl product is also generated. The incubation products are converted into the corresponding porphyrin methyl esters, and characterized by proton NMR spectroscopy and mass spectrometry
?
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
-
Substrates: -
Products: 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
Products: 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
coproporphyrin III + H2O
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Substrates: -
Products: -
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?
coproporphyrinogen III + O2
coproporphyrin III + H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
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?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
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?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
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?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
Substrates: recombinant Sll1185 shows CPO activity under both aerobic and anaerobic conditions
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
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?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
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Substrates: 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
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coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: via harderoporphyrinogen intermediate production, overall reaction
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?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
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?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
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coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
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?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: 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
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Products: -
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coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + H+
protoporphyrinogen IX + CO2 + H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + H+
protoporphyrinogen IX + CO2 + H2O
Substrates: -
Products: -
Products: -
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coproporphyrinogen-III + 2 NADP+
protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+
-
Substrates: oxidation under anaerobic conditions strictly requires NADP+ as electron acceptor
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coproporphyrinogen-III + 2 NADP+
protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+
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Substrates: oxidation under anaerobic conditions strictly requires NADP+ as electron acceptor
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coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
Substrates: anaerobic oxidation only in the presence of ATP, NADP+, Mg2+, L-Met, 5-10% of the aerobic activity
Products: -
Products: -
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coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
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Substrates: anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
Products: -
Products: -
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
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Substrates: anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
Products: -
Products: -
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
Substrates: anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
Products: -
Products: -
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
Substrates: -
Products: -
Products: -
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: essential enzyme, catalyzes the 6th step in heme biosynthesis
Products: -
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: O2-dependent enzyme Hem13p
Products: -
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
Substrates: enzyme is involved in heme and chlorophyll biosynthesis
Products: -
Products: -
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
Substrates: -
Products: -
Products: -
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: step in heme biosynthesis
Products: -
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: HemF is absolutely dependent on oxygen
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
Substrates: -
Products: -
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: pathway overview
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: coproporphyrinogen analogues with modified propionate side chains bearing methyl substitutents are moderate substrates for the enzyme giving divinylic products, overview
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Products: -
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: 6th step in heme biosynthesis, pathway overview
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Products: -
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: pathway overview
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: key enzyme in the biosynthesis of heme, metabolism overview
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Products: -
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: conversion of 2 propionate groups to 2 vinyl groups by oxidative decarboxylation
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Products: -
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: sequential oxidative decarboxylations at the A and B rings, synthetic coproporphyrinogen analogues with modified methylated propionate side chains are moderate substrates for the enzyme giving divinylic products, overview
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Products: -
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coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: coproporphyrinogen conversion via tripropionate intermediate harderoporphyrinogen, selective conversion of propionate residues at the A and B rings into vinyl moieties by oxidation and decarboxylation resulting in a trivinylic compound
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: enzyme is involved in heme and chlorophyll biosynthesis
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: 6th step in heme biosynthesis
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: 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
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: highly specific for oxygen as electron acceptor
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: highly specific for oxygen as electron acceptor
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: highly specific for oxygen as electron acceptor
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: oxygen-independent enzyme has also an aerobic function
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: acts on analogues which possess normal substituents on ring-A to generate a vinyl group on that ring, not active if the ring-A propionate group is changed
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: small amount of the monovinyl intermediate
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: CPO converts coproporphyrinogen III to protoporphyrinogen IX through harderoporphyrinogen IX
Products: -
Products: -
ir
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: 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
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Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: sixths enzyme in heme biosynthetic pathway
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: 6th enzyme in heme biosynthetic pathway
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: step-wise decarboxylation of 2- and 4-propionate substituents, both decarboxylations take place at the same active centre
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: highly specific for oxygen as electron acceptor
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: sixths enzyme in heme biosynthetic pathway
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: 6th enzyme in heme biosynthetic pathway
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: same activity under aerobic and anaerobic conditions
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: aerobic and anaerobic oxidation catalyzed by the same enzyme
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: sixths enzyme in heme biosynthetic pathway
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: 6th enzyme in heme biosynthetic pathway
Products: -
Products: -
?
coproporphyrinogen-IV + O2
?
-
Substrates: synthetic coproporphyrinogen analogues with modified propionate side chains
Products: -
Products: -
?
coproporphyrinogen-IV + O2
?
-
Substrates: synthetic coproporphyrinogen analogues with modified propionate side chains
Products: -
Products: -
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
Substrates: monovinyl intermediate that accumulates before being converted to an isomer
Products: -
Products: -
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
Substrates: 30% higher activity compared to coproporphyrinogen-III
Products: -
Products: -
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
Substrates: intermediate of coproporphyrinogen-III, that is also a substrate
Products: -
Products: -
?
harderoporphyrinogen-VII + O2 + 2 H+
? + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
harderoporphyrinogen-VII + O2 + 2 H+
? + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
isoharderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
Substrates: 3% of the activity compared to coproporphyrinogen-III
Products: -
Products: -
?
isoharderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
Substrates: intermediate of coproporphyrinogen-III that is also a substrate
Products: -
Products: -
?
isoharderoporphyrinogen + O2 + 2 H+
? + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
isoharderoporphyrinogen + O2 + 2 H+
? + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
mesoproporphyrinogen-VI + O2
?
-
Substrates: synthetic coproporphyrinogen analogues with modified propionate side chains
Products: -
Products: -
?
mesoproporphyrinogen-VI + O2
?
-
Substrates: synthetic coproporphyrinogen analogues with modified propionate side chains
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity of HemF with protoporphyrinogen-IX and coporphyrinogen-III
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity with diverse coproporphyrinogen-derived compounds, overview, alterations of substituents involved in secondary binding interactions have a comparable affect to modifying the side chain that undergoes degradation at the catalytic site, porphyrinogen carboxylic acids are unstable, no hyroxylated products
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity with diverse coproporphyrinogen-derived compounds, overview, alterations of substituents involved in secondary binding interactions have a comparable affect to modifying the side chain that undergoes degradation at the catalytic site, no hyroxylated products
Products: -
Products: -
?
additional information
?
-
-
Substrates: a nonnatural type I isomer of harderoporphyrinogen is also a substrate of CPO, no activity with 13-ethyl harderoporphyrinogen-III, substrate specificity with vinylic porphyrinogen derivatives, harderoporphyrinogen derivatives, and reaction mechanism, detailed overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: pentacarboxylate porphyrinogens 5abc, 5abd, and 5acd are not metabolized
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with S-adenosylmethionine or without O2
Products: -
Products: -
?
additional information
?
-
-
Substrates: deleterious enzyme mutations can cause hereditary coproporphyria
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: no anaerobic activity is detected using NADP+ and S-adenosylmethionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no anaerobic activity is detected using NADP+ and S-adenosylmethionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: HemJ is functionally coupled with the enzyme
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
coproporphyrinogen-III + O2
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: essential enzyme, catalyzes the 6th step in heme biosynthesis
Products: -
Products: -
?
mesoporphyrinogen-VI + O2 + 2 H+
protoaetioporphyrin + 2 CO2 + 2 H2O
-
Substrates: similar oxidation rate compared to coproporphyrinogen-III
Products: -
Products: -
?
pentacarboxylate porphyrinogen III + O2
dehydroisocoproporphyrinogen + CO2
-
Substrates: half of the activity compared to coproporphyrinogen oxidase-III
Products: -
Products: -
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
Substrates: -
Products: -
Products: -
?
protoporphyrinogen-IX + O2
protoporphyrin-IX + CO2
-
Substrates: capacity to oxidize not only coproporphyrinogen-III but also protoporphyrinogen-IX
Products: -
Products: -
?
additional information
?
-
-
Substrates: deleterious enzyme mutations can cause hereditary coproporphyria
Products: -
Products: -
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: via harderoporphyrinogen intermediate production, overall reaction
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + H+
protoporphyrinogen IX + CO2 + H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen III + O2 + H+
protoporphyrinogen IX + CO2 + H2O
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + 2 NADP+
protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+
-
Substrates: oxidation under anaerobic conditions strictly requires NADP+ as electron acceptor
Products: -
Products: -
?
coproporphyrinogen-III + 2 NADP+
protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+
-
Substrates: oxidation under anaerobic conditions strictly requires NADP+ as electron acceptor
Products: -
Products: -
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
Substrates: anaerobic oxidation only in the presence of ATP, NADP+, Mg2+, L-Met, 5-10% of the aerobic activity
Products: -
Products: -
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
Substrates: anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
Products: -
Products: -
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
Substrates: anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
Products: -
Products: -
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
Substrates: anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
Substrates: enzyme is involved in heme and chlorophyll biosynthesis
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: step in heme biosynthesis
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: pathway overview
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: 6th step in heme biosynthesis, pathway overview
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: pathway overview
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: key enzyme in the biosynthesis of heme, metabolism overview
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: enzyme is involved in heme and chlorophyll biosynthesis
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: 6th step in heme biosynthesis
Products: -
Products: -
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
Substrates: 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
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: highly specific for oxygen as electron acceptor
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: highly specific for oxygen as electron acceptor
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
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?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: highly specific for oxygen as electron acceptor
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
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?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: oxygen-independent enzyme has also an aerobic function
Products: -
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?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: acts on analogues which possess normal substituents on ring-A to generate a vinyl group on that ring, not active if the ring-A propionate group is changed
Products: -
Products: -
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coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
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coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: 6th enzyme in heme biosynthetic pathway
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
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coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: step-wise decarboxylation of 2- and 4-propionate substituents, both decarboxylations take place at the same active centre
Products: -
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coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: highly specific for oxygen as electron acceptor
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: 6th enzyme in heme biosynthetic pathway
Products: -
Products: -
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
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?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: same activity under aerobic and anaerobic conditions
Products: -
Products: -
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coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: aerobic and anaerobic oxidation catalyzed by the same enzyme
Products: -
Products: -
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coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
Substrates: 6th enzyme in heme biosynthetic pathway
Products: -
Products: -
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
Products: -
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coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
Substrates: -
Products: -
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harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
Substrates: 30% higher activity compared to coproporphyrinogen-III
Products: -
Products: -
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
Substrates: intermediate of coproporphyrinogen-III, that is also a substrate
Products: -
Products: -
?
isoharderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
Substrates: 3% of the activity compared to coproporphyrinogen-III
Products: -
Products: -
?
isoharderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
Substrates: intermediate of coproporphyrinogen-III that is also a substrate
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
only anaerobic activity, 30% of the activity compared to NADP+
NADP+
-
only anaerobic enzyme, maximum activity together with NADH
additional information
enzyme contains a covalently bound porphyrin compound
-
additional information
-
enzyme contains a covalently bound porphyrin compound
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Cu2+
Fe2+
Mn2+
additional information
Fe2+
0.09-1.25 mol per mol of polypeptide for the recombinant wild-type enzyme, 0.2 mol per mol of polypeptide for the selenomethionine-labeled variant
Fe2+
-
enhanced activity by increasing concentrations up to 0.5 mM, beyond inhibitory
Mn2+
-
required, bound to the enzyme, stimulates, restores the enzyme inactivated by metal chelators, coordinated by residues His96, His106, His145, and His175
additional information
-
metal ions Cu2+, Mg2+, Mn2+, Fe2+ and Zn2+ at up to 0.500 mM concentration have no effect on CPO activity
additional information
-
30% activation of aerobic oxidation by divalent ions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2-bipyridyl
-
77% inhibition of anaerobic reaction at 1.5 mM
bis(sulfosuccinimidyl) suberate
-
56% residual activity as compared to not cross-linked enzyme
diethyl dicarbonate
-
concentration-dependent inhibition, complete inactivation at 50 mM
GSH
-
slight inhibition of aerobic, 41% inhibition of anaerobic enzyme at 5 mM
GSSG
-
31% inhibition of anerobic, 25% inhibition of aerobic enzyme at 5 mM
p-hydroxymercuribenzoate
-
44% inhibition of anaerobic, 23% inhibition of aerobic enzyme at 0.5 mM
Phenylglyoxal
-
concentration-dependent inhibition, complete inactivation at 50 mM
sulfosuccinimidyl 4-(N-maleimidomethyl) cyclohexane-1-carboxylate
-
40% residual activity as compared to not cross-linked enzyme
1,10-phenanthroline
-
90% inhibition of anaerobic reaction at 0.17 mM
1,10-phenanthroline
-
25% inhibition of aerobic, 53% inhibition of anaerobic enzyme at 10 mM
EDTA
-
16% inhibition of aerobic, 41% inhibition of anaerobic enzyme at 10 mM
N-bromosuccinimide
-
concentration-dependent inhibition, complete inactivation at 50 mM
N-ethylmaleimide
-
86% inhibition of anaerobic, 54% inhibition of aerobic enzyme at 20 mM
Tetranitromethane
-
60% decrease of Vmax at 1.6 mol modified tyrosine per mol enzyme, Km not affected
additional information
-
mutation of the nucleotide binding motif GGGXXTP does not affect the enzyme activity
-
additional information
-
decreased activity at high ionic strength
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methotrexate
-
causes a 3fold accumulation of CPO at both the mRNA and protein levels
phosphatidyl glycerol
-
activation in intact and sonicated mitochondria up to 135%
L-methionine
-
strictly required for anaerobic oxidation, optimal activation at 5 mM
oxygen
-
levels of hemF protein are much higher in cells grown aerobically than in anaerobically grown cells, amount correlates with gene dosage
Phospholipids
-
effective in decreasing the amount of intermediate accumulation, oxidation of 2,4-bis(beta-hydroxypropionic acid) deuteroporphyrinogen IX not activated
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
3-[7,13-di(2-carboxy-ethyl)-17-benzyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
-
0.000011
3-[7,13-di(2-carboxy-ethyl)-17-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.00088
3-[7,17-di(2-carboxy-ethyl)-13-benzyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
-
0.00085
3-[7,17-di(2-carboxy-ethyl)-13-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.0001
3-[7-(2-carboxy-ethyl)-13,17-di-tert-butyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
-
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 - 0.00099
3-[7-(2-carboxy-ethyl)-13,17-diethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
0.00035
3-[7-(2-carboxy-ethyl)-13,17-diisopropyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
-
0.011
3-[7-(2-carboxy-ethyl)-13,17-dipropyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.001
3-[7-(2-carboxy-ethyl)-3,8,12,13,17,18-hexamethyl-porphyrinogen-2-yl]-propionic acid
-
-
0.00056
3-[7-(2-carboxy-ethyl)-13,17-diethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
at 37°C
0.00099
3-[7-(2-carboxy-ethyl)-13,17-diethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid
-
-
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, 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
0.0031
Coproporphyrinogen-III
recombinant wild-type enzyme, pH 7.0, 37°C
0.0032
Coproporphyrinogen-III
-
same value for aerobic and anaerobic oxidation
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
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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
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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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.4 - 8.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2 genesAtCPO-1 and AtCPO-2, the latter being a pseudogene
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
higher enzyme expression in spongy tissue caused by internal breakdown
brenda
additional information
-
expression of oxygen-independent and oxygen-dependent enzymes
brenda
-
-
brenda
additional information
not in seeds, expression analysis, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
human enzyme is imported in isolated rat mitochondria, heme inhibits the mitochondrial import of the enzyme completely at 0.02 mM concentration
brenda
-
in digitonin-treated mitochondria from animals exposed to hexachlorobenzene, coproporphyrinogen oxidase is free in the mitochondrial intermembrane space, whereas in normal mitochondria, 30%-50% remain anchored to the inner membrane
brenda
-
highest recovery of enzyme activity by digitonin treatment of mitochondria
brenda
additional information
no activity in mitochondrion and cytosol
-
brenda
additional information
no activity in mitochondrion and cytosol
-
brenda
additional information
-
PfCPO does not carry an obvious N-terminal leader targeting sequence, subcellular localization study, overview. No measurable activity in the solubilized parasite membrane fraction
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
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
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
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
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
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
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
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
-
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
-
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
-
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
metabolism
-
CPOX is a mitochondrial enzyme in the heme biosynthetic pathway that catalyzes the conversion of coproporphyrinogen III to protoporphyrinogen IX
metabolism
-
oxygen-dependent coproporphyrinogen III oxidase catalyzes the sequential decarboxylation of the propionate substituents present on the A and B rings of coproporphyrinogen III in the heme biosynthetic pathway
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
metabolism
LIN2 encodes coproporphyrinogen III oxidase, CPO, a key enzyme of the tetrapyrrole biosynthesis pathway
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
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
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
metabolism
-
the enzyme plays an important role in the biosynthesis of tetrapyrrole and light-dependent-defense in soybean
metabolism
-
LIN2 encodes coproporphyrinogen III oxidase, CPO, a key enzyme of the tetrapyrrole biosynthesis pathway
-
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
-
physiological function
-
CPOX is a mitochondrial enzyme in the heme biosynthetic pathway that catalyzes the conversion of coproporphyrinogen III to protoporphyrinogen IX
physiological function
in filamentous fungi, enzyme CPO functions as a regulatory step preventing hazardous levels of intracellular heme
physiological function
coproporphyrinogen oxidase (CPO) is a rate-limiting enzyme in the heme pathway responsible for the conversion of coproporphyrinogen III into protoporphyrin IX
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
physiological function
-
in filamentous fungi, enzyme CPO functions as a regulatory step preventing hazardous levels of intracellular heme
-
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
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
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
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
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
-
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
-
Show AA Sequence and Transmembrane Helices (13535 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
35390
2 * 35000, recombinant enzyme, SDS-PAGE, 2 * 35390, recombinant enzyme, mass spectrometry, 2 * 35718, recombinant selenomethionine-labeled enzyme, mass spectrometry
35718
2 * 35000, recombinant enzyme, SDS-PAGE, 2 * 35390, recombinant enzyme, mass spectrometry, 2 * 35718, recombinant selenomethionine-labeled enzyme, mass spectrometry
37000
37500
38000
61000
70000
74000
77000
-
minimum catalytic activity, also aggregation to 154000 kDa catalytic activity, gel filtration
35000
2 * 35000, recombinant enzyme, SDS-PAGE, 2 * 35390, recombinant enzyme, mass spectrometry, 2 * 35718, recombinant selenomethionine-labeled enzyme, mass spectrometry
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
additional information
dimer
2 * 35000, recombinant enzyme, SDS-PAGE, 2 * 35390, recombinant enzyme, mass spectrometry, 2 * 35718, recombinant selenomethionine-labeled enzyme, mass spectrometry
additional information
enzyme consists of 26% alpha-helices and 31% beta-sheets
additional information
-
enzyme consists of 26% alpha-helices and 31% beta-sheets
additional information
-
central flat seven-stranded antiparallel sheet flanked by alpha-helices
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
25 mg/ml purified recombinant His-tagged enzyme in 20 mM Tris, pH 7.5, 5% v/v glycerol, sitting drop method, 21°C, for C-form crystals: equal volume of protein and reservoir solution, the latter containing 20% PEG 3000, 0.1 M HEPES, pH 7.5, and 0.2 M sodium acetate, optimized sulfur anomalous scattering, for form 1 crystals: sitting drops of protein and reservoir solution, the latter containing 18% PEG 8000, 0.1 M HEPES, pH 7.5, 2% isopropanol, and 0.2 M sodium acetate at 4°C, 13°C, or 21°C, for form II crystals: sitting drops of protein and reservoir solution in a 2:1 mixture, the latter containing 2.2 M ammonium sulfate, 0.1 M Tris, pH 8.5, 21°C, 10% v/v glycerol as cryoprotectant, X-ray diffraction structure determination and anaylsis at 2.0 A and 2.4 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C167S
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
G127V
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
P133A
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
T132A
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
W123L
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
W124R
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
W166L
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
W298L
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
W36L
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
Y160F
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
Y170F
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
Y213F
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
Y240F
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
Y276F
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
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
G279R
novel nucleotide transition found, is unstable, and produces ca. 2-5% of activity compared with the wild-type CPO
G402A
-
less than 1% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
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
K404H
site-directed mutagenesis, the mutant produces a high level of harderoporphyrinogen with low production of protoporphyrinogen similar to mutant K404E
K404N
-
61% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
K404Q
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
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
mutation results in decreased kcat values and increased Km values. No product formation is detected with sunstrate mesoporphyrogen-VI
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
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
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
H158A
-
complete loss of activity, decreased stability, no copper content
additional information
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
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
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
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
R401W
-
75% of residual activity compared with wild-type CPO, causes substantial accumulation of harderoporphyrinogen
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
spontaneous lesion formation mutant lin2-2
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
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
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
-
additional information
-
HemF- mutant strain, unable to grow under aerobic condition
additional information
-
18-somite stage cloche homozygous mutant embryos, development of hematopoietic and endothelial lineages is severely impaired, cpo is downregulated
additional information
-
knockdown of zebrafish CPO using anti-sense morpholinos leads to a significant suppression of hemoglobin production without apparent reduction of blood cells, injection of human CPO RNA, but not a mutant CPO RNA similar to a mutant responsible for a hereditary coproporphyria, restores hemoglobin production in the CPO-MO-injected embryos, expression of CPO in the ICM is severely suppressed in both vlad tepes/gata1 mutants and in biklf-MO-injected embryos
additional information
-
mutation of the nucleotide binding motif GGGXXTP does not affect the enzyme activity
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
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
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
-
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
-
identification of diverse deleterious enzyme mutations in hereditary coproporphyria, structural effects of mutations, overview
additional information
-
construction of enzyme-deficient DELTA sll1185 mutant, which fails to grow under aerobic conditions, with accumulation of coproporphyrin III. This growth defect is restored by cultivation under micro-oxic conditions
additional information
construction of enzyme-deficient DELTA sll1185 mutant, which fails to grow under aerobic conditions, with accumulation of coproporphyrin III. This growth defect is restored by cultivation under micro-oxic conditions
additional information
seedlings homozygous for a null mutation in the cpx1 gene completely lack chlorophyll and develop necrotic lesions in the light
additional information
seedlings homozygous for a null mutation in the cpx1 gene completely lack chlorophyll and develop necrotic lesions in the light
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
56
a 2 minute incubation of the protein at 56°C leads to a total loss of enzymatic activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
tends to aggregate during prolonged storage at 4C
when incubated with 3 M urea, the enzyme is slowly denatured at pH 6.3 and much faster at pH 7.6
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1% (w/v) NaN3 (100 mM Tris, pH 7.6), several years, no loss of activity
25°C, 1% (w/v) NaN3 (100 mM Tris, pH 7.6), several months, no loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and Ultrogel Ac44 gel filtration
by Ni2+ affinity chromatography
partial
recombinant enzyme from Escherichia coli, 3-step procedure, 119fold to homogeneity
-
recombinant HA-tagged wild-type enzyme and His-tagged mutant enzyme from Escherichia coli by nickel and heparin affinity chromatography, respectively
recombinant hemF oxygen-dependent enzyme form to homogeneity by affinity chromatography, the tag protein is cleaved off by thrombin, recombinant wild-type and mutant enzymes
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli, cleavage of the tag
-
recombinant terminally Strep-tagged HemF from Escherichia coli to homogeneity
separation of coproporphyrinogen oxidase, EC 1.3.3.3, from uroporphyrinogen decarboxylase, EC 4.1.1.37, by coproporphyrinogen-III-resin affinity chromatography, elution in a salt gradient
-
separation of uroporphyrinogen decarboxylase, EC 4.1.1.37, from coproporphyrinogen oxidase using porphyrin-affinity chromatography
-
to homogeneity, chromatography steps
to homogeneity, recombinant enzyme
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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
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 of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene AtCPO-1, chromosome I, DNA and amino acid sequence determination and analysis, complementation of an enzyme-deletion Saccharomyces cerevisiae hem13 mutant, expression as GFP-fusion protein in transgenic Arabidopsis thaliana plants via Agrobacterium tumefaciens tranbsformation
gene AtCPO-2, DNA sequence determination and analysis, no complementation of an enzyme-deletion Saccharomyces cerevisiae hem13 mutant, possibly a pseudogene
gene CPO, located on chromosome 3q11.2, DNA and amino acid sequence determination and analysis, genotyping of an Italian population
-
gene hemF, recombinant overexpression in Aspergillus niger, subcloning in Escherichia coli strain DH5alpha, complementation of a hemF deletion strain
gene LIN2, construction of transgenic plants expressing the mutant LIN2 gene using Agrobacterium tumefaciens strain GV3101 transfection
gene sll1185, overexpression of N-terminally Strep-tagged HemF in Escherichia coli
into pAB24, expression in Saccharomyces cerevisiae BY4743(hem13::kanMX4), wild-type Saccharomyces cerevisiae and Rox1p and Mga2p mutants transformed with an episomic plasmid derived from YEP365, in which KlHEM13 promoter is fused in frame to lacZ
into the MscI site of pUI1087, generating pKS7, moving of the hemF sequences from pKS7 into pBBR1MCS2, creating pKS9, BamHI DNA fragment deleted from pKS9, omega Sp-St resistance cassette inserted at the remaining unique BamHI site, generating pKS11, from pKS11 3135-bp SmaI fragment containing delta hemF::omegaSpr-Str moved into pSUP202, replacing the vector sequences contained on a 1,348-bp ScaI fragment and creating pKS13, hemF::lacZ transcription reporter plasmid pJZ84 constructed by first inserting a 717-bp SmaI-NcoI DNA fragment from pKS9 into pUI1087, using the flanking PstI-XbaI vector restriction sites, the hemFequences are positioned and correctly oriented in front of a promoterless lacZ gene in plasmid vector pCF1010
-
into vector PCRII-TOPO, transferred into vector pcDNA3.1(-), and transfection of LNCaP cells and Cos-7 cells
-
mature form of wild-type CPOX cloned into pET-22, wild-type and mutant protein expressed in Escherichia coli BL21(DE3)plysS
over 200fold overexpression in Escherichia coli strain BL21(DE3), reduction of the toxicity of product protoporphyrin-IX for the bacterial cells by decrease of growth temperature to 20°C
-
overexpression of hemF oxygen-dependent enzyme form as N-terminally fusion protein with calmodulin-binding-peptide, overexpression of wild-type and mutant enzymes in strain BL21(DE3)
-
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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cystathionine gamma-lyase deficient mice exhibit elevated enzyme expression in the liver
-
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
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
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
first patient with porphyria where both CPO and delta-aminolaevulinic acid dehydratase are deficient at the molecular level
medicine
-
CPOX4 polymorphism may affect susceptibility for specific neurobehavioral functions associated with mercury exposure in human subjects
medicine
-
abnormal route for heme biosynthesis in humans suffering from porphyria cutanea tarda or related syndromes such as hexachlorobenzene poisoning
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
-
function of CPO in heme biosynthesis is apparently conserved between zebrafish and human, suggesting that CPO-MO-injected zebrafish embryos might be a useful in vivo assay system to measure the biological activity of human CPO mutations
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
-
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
medicine
-
chronic exposure of rats to hexachlorobenzene produces an experimental model for human porphyria cutanea tarda. In digitonin-treated hexachlorobenzene mitochondria, coproporphyrinogen oxidase is free in the mitochondrial intermembrane space, whereas in normal mitochondria, 30%-50% remain anchored to the inner membrane
medicine
the regulation of the enzyme is important in differentiation therapy for cancer treatment
additional information
cpx1 and cpx2 genes encode almost identical, catalytically active enzymes with distinctive N-terminal peptide sequences, cpx1 encodes a plastid transit peptide, whereas this region is deleted from the cpx2 gene, the 5' regions of both messenger RNAs are highly similar, but the cpx2 gene has an open-reading frame that can encode a new targeting signal
additional information
cpx1 and cpx2 genes encode almost identical, catalytically active enzymes with distinctive N-terminal peptide sequences, cpx1 encodes a plastid transit peptide, whereas this region is deleted from the cpx2 gene, the 5' regions of both messenger RNAs are highly similar, but the cpx2 gene has an open-reading frame that can encode a new targeting signal
additional information
-
cpx1 and cpx2 genes encode almost identical, catalytically active enzymes with distinctive N-terminal peptide sequences, cpx1 encodes a plastid transit peptide, whereas this region is deleted from the cpx2 gene, the 5' regions of both messenger RNAs are highly similar, but the cpx2 gene has an open-reading frame that can encode a new targeting signal
additional information
cloned KlHEM13 is functional and able to replace its homologous gene in Saccharomyces cerevisiae
additional information
-
cloned KlHEM13 is functional and able to replace its homologous gene in Saccharomyces cerevisiae
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sorianello, E.M.; Mazzetti, M.B.
Function and structure of rat hepatic coproporphyrinogen oxidase
Comp. Biochem. Physiol. B
127
155-164
2000
Rattus sp.
brenda
Jones, M.A.; He, J.; Lash, T.D.
Kinetic studies of novel di- and tri-propionate substrates for the chicken red blood cell enzyme coproporphyrinogen oxidase
J. Biochem.
131
201-205
2002
Gallus gallus
brenda
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
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brenda
Moghe, A.; Ramanujam, V.M.S.; Phillips, J.D.; Desnick, R.J.; Anderson, K.E.
Harderoporphyria Case of lifelong photosensitivity associated with compound heterozygous coproporphyrinogen oxidase (CPOX) mutations
Mol. Genet. Metab. Rep.
19
100457
2019
Homo sapiens
brenda
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