Information on EC 1.3.3.3 - coproporphyrinogen oxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.3.3.3
-
RECOMMENDED NAME
GeneOntology No.
coproporphyrinogen oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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)
-
-
superpathway of heme b biosynthesis from uroporphyrinogen-III
-
-
heme metabolism
-
-
Porphyrin and chlorophyll metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
coproporphyrinogen:oxygen oxidoreductase (decarboxylating)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9076-84-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene LIN2
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
free- and symbiotic-living bacteria
-
-
Manually annotated by BRENDA team
Chromatium sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain NRRL-Y1140, strain MW190-9B
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Desulfovibrio vulgaris
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
generates a vinyl group on ring-A
-
?
17-ethyl harderoporphyrinogen-III + O2 + 2 H+
?
show the reaction diagram
-
-
-
-
?
17-ethylharderoporphyrinogen-III + O2 + 2 H+
17-ethylprotoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
2,4-bis-(beta-hydroxypropionic acid) deuteroporphyrinogen IX + O2
protoporphyrinogen IX + CO2
show the reaction diagram
-
one sixth of the rate compared to coproporhyrinogen-III
-
?
2-beta-hydroxypropionic acid-4-propionic acid deuteroporphyrinogen IX + O2
protoporphyrinogen IX + CO2
show the reaction diagram
-
80% of the activity compared to coproporphyrinogen-III
-
?
2-propionic acid-4-beta-hydroxypropionic acid deuteroporphyrinogen IX + O2
protoporphyrinogen IX + CO2
show the reaction diagram
-
8% of the activity compared to coproporphyrinogen-III
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
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
show the reaction diagram
-
very poor substrate
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
show the reaction diagram
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
show the reaction diagram
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
coproporphyrinogen III + O2 + H+
protoporphyrinogen IX + CO2 + H2O
show the reaction diagram
coproporphyrinogen-III + 2 NADP+
protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+
show the reaction diagram
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
show the reaction diagram
coproporphyrinogen-III + O2
protoporphyrinogen IX + CO2
show the reaction diagram
coproporphyrinogen-III + O2
protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2
show the reaction diagram
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
show the reaction diagram
coproporphyrinogen-IV + O2
?
show the reaction diagram
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
show the reaction diagram
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
show the reaction diagram
harderoporphyrinogen + O2
protoporphyrinogen-IX + CO2
show the reaction diagram
harderoporphyrinogen-III + O2 + 2 H+
?
show the reaction diagram
-
-
-
-
?
harderoporphyrinogen-IV + O2 + 2 H+
?
show the reaction diagram
-
-
-
-
?
harderoporphyrinogen-VII + O2 + 2 H+
?
show the reaction diagram
-
a monovinyl intermediate in the metabolism of coproporphyrinogen-IV
-
-
?
harderoporphyrinogen-VII + O2 + 2 H+
? + 2 CO2 + 2 H2O
show the reaction diagram
isoharderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
show the reaction diagram
isoharderoporphyrinogen + O2 + 2 H+
?
show the reaction diagram
-
very low activity
-
-
?
isoharderoporphyrinogen + O2 + 2 H+
? + 2 CO2 + 2 H2O
show the reaction diagram
mesoporphyrinogen-VI + O2
harderoporphyrinogen + CO2
show the reaction diagram
mesoporphyrinogen-VI + O2 + 2 H+
protoaetioporphyrin + 2 CO2 + 2 H2O
show the reaction diagram
mesoproporphyrinogen-VI + O2
?
show the reaction diagram
pentacarboxylate porphyrinogen 5dab + O2
dehydroisocoproporphyrinogen
show the reaction diagram
-
poorer substrate than coproporphyrinogen-III
-
-
?
pentacarboxylate porphyrinogen III + O2
dehydroisocoproporphyrinogen + CO2
show the reaction diagram
-
half of the activity compared to coproporphyrinogen oxidase-III
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
show the reaction diagram
-
-
-
-
?
protoporphyrinogen-IX + O2
protoporphyrin IX + CO2
show the reaction diagram
-
capacity to oxidize not only coproporphyrinogen-III but also protoporphyrinogen-IX
-
?
protoporphyrinogen-IX + O2
protoporphyrin-IX + CO2
show the reaction diagram
-
capacity to oxidize not only coproporphyrinogen-III but also protoporphyrinogen-IX
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
coproporphyrinogen III + O2
coproporphyrin III + H2O
show the reaction diagram
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
show the reaction diagram
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
coproporphyrinogen III + O2 + H+
protoporphyrinogen IX + CO2 + H2O
show the reaction diagram
coproporphyrinogen-III + 2 NADP+
protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+
show the reaction diagram
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
show the reaction diagram
coproporphyrinogen-III + O2
protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
-
essential enzyme, catalyzes the 6th step in heme biosynthesis
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2
show the reaction diagram
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
show the reaction diagram
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
show the reaction diagram
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
show the reaction diagram
isoharderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
show the reaction diagram
mesoporphyrinogen-VI + O2 + 2 H+
protoaetioporphyrin + 2 CO2 + 2 H2O
show the reaction diagram
-
similar oxidation rate compared to coproporphyrinogen-III
-
?
pentacarboxylate porphyrinogen III + O2
dehydroisocoproporphyrinogen + CO2
show the reaction diagram
-
half of the activity compared to coproporphyrinogen oxidase-III
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
show the reaction diagram
-
-
-
-
?
protoporphyrinogen-IX + O2
protoporphyrin-IX + CO2
show the reaction diagram
-
capacity to oxidize not only coproporphyrinogen-III but also protoporphyrinogen-IX
-
?
additional information
?
-
-
deleterious enzyme mutations can cause hereditary coproporphyria
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
additional information
enzyme contains a covalently bound porphyrin compound
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
50% activation of anaerobic enzyme at 5 mM
Fe3+
-
80% activation of anaerobic enzyme at 0.5 mM
Mg2+
-
50% activation of anaerobic enzyme at 5 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
1,4-Naphthoquinone
-
61% inhibition at 0.015 mM
2,2-bipyridyl
-
77% inhibition of anaerobic reaction at 1.5 mM
2,4,6-Trinitrobenzene
-
60% inhibition at 3.4 mM
2,4-dinitrophenol
5,5-dithiobis(2-nitrobenzoic acid)
Ag+
Chromatium sp.
-
67% inhibition at 1 mM
bis(sulfosuccinimidyl) suberate
-
56% residual activity as compared to not cross-linked enzyme
Cetyltrimethylammonium chloride
-
86% inhibition at 0.05%
Co2+
-
inhibition above 5 mM
coproporphyrin III
competitive inhibitor
coproporphyrinogen I
-
70% inhibition at 0.0195 mM
coproporphyrinogen II
-
61% inhibition at 0.0206 mM
Coproporphyrinogen III
-
52% inhibition at 0.0194 mM
coproporphyrinogen IV
-
30% inhibition at 0.0196 mM
Cu2+
-
inhibition at 0.1 mM
diethyl dicarbonate
-
concentration-dependent inhibition, complete inactivation at 50 mM
FAD
-
95% inhibition of anaerobic reaction at 0.03 mM
Fe2+
-
inhibition above 0.1 mM
FMN
-
95% inhibition of anaerobic reaction at 0.03 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
Harderoporphyrin
-
27% inhibition at 0.02 mM
iodoacetate
KCl
-
70% inhibition at 1 M
L-ethionine
-
inhibition of anaerobic enzyme, 48% at 5 mM
Mn2+
-
inhibition above 5 mM
N-Acetylimidazole
-
90% inhibition at 0.6 mM
N-bromosuccinimide
N-ethylmaleimide
NaCl
-
60% inhibition at 1 M
p-chloromercuribenzene sulfonate
-
40% inhibition at 20 mM
p-chloromercuribenzoate
-
60% inhibition at 1 mM
p-hydroxymercuribenzoate
-
44% inhibition of anaerobic, 23% inhibition of aerobic enzyme at 0.5 mM
p-hydroxyphenylglyoxal
-
55% inhibition at 0.1 mM
Pentacarboxylate porphyrin III
-
10% inhibition at 0.0198 mM
-
Phenylglyoxal
-
concentration-dependent inhibition, complete inactivation at 50 mM
protoporphyrin-IX
-
inhibition of HemF
riboflavin
-
95% inhibition of anaerobic reaction at 0.03 mM
S-adenosylethionine
-
marked inhibition of anaerobic reaction
S-adenosylhomocysteine
-
marked inhibition of anaerobic reaction
sodium cholate
-
-
sodium deoxycholate
sulfosuccinimidyl 4-(N-maleimidomethyl) cyclohexane-1-carboxylate
-
40% residual activity as compared to not cross-linked enzyme
Tetranitromethane
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
slight activation
cardiolipin
-
2.2fold activation at 0.5 mg/ml
DTT
-
slight activation
L-alpha-lysophosphatidylcholine
-
4.4fold activation at 0.5 mg/ml
L-alpha-lysophosphatidylethanolamine
-
3.4fold activation at 0.5 mg/ml
L-alpha-phosphatidyl-DL-glycerol
-
2.7fold activation at 0.5 mg/ml
L-alpha-phosphatidyl-L-serine
-
2.8fold activation at 0.5 mg/ml
L-alpha-phosphatidylcholine
L-alpha-Phosphatidylethanolamine
-
3.9fold activation at 0.5 mg/ml
L-methionine
lecithin
Lipids
-
bovine liver lipids, 3.6fold activation at 1 mg/ml
-
methotrexate
-
causes a 3fold accumulation of CPO at both the mRNA and protein levels
Non-ionic detergents
-
oxygen
phosphatidate
phosphatidyl glycerol
-
activation in intact and sonicated mitochondria up to 135%
Phospholipids
pyruvate
-
50% activation at 50 mM
S-adenosyl-L-methionine
Chromatium sp.
-
can replace NADP+-NADH in anaerobic reaction
Triton X-100
Tween 20
Tween 40
-
2.2fold activation at 0.2%, v/v
Tween 60
-
2.3fold activation at 0.2%, v/v
Tween 80
-
2fold activation at 0.2%, v/v
Tween 85
-
1.8 fold activation at 0.2%, v/v
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
0.000066 - 0.0151
Coproporphyrinogen III
0.0009
coproporphyrinogen IV
-
-
0.000066 - 0.32
Coproporphyrinogen-III
0.00065 - 0.00083
coproporphyrinogen-IV
0.00034 - 0.0051
Harderoporphyrin
0.00015 - 0.044
Harderoporphyrinogen
0.00056 - 0.002
mesoporphyrin-VI
0.00056 - 0.002
mesoporphyrinogen-VI
0.0013
pentacarboxylate porphyrinogen 5dab
-
monovinyl as product; total product
0.029
pentacarboxylate porphyrinogen III
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
0.00002 - 16
Coproporphyrinogen-III
0.01167 - 0.043
coproporphyrinogen-IV
0.0000123 - 0.027
Harderoporphyrin
0.000383 - 0.1317
Harderoporphyrinogen
0.002 - 0.00633
mesoporphyrin-VI
0.002 - 0.0063
mesoporphyrinogen-VI
0.009
pentacarboxylate porphyrinogen 5dab
-
monovinyl as product; total product
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5
Coproporphyrinogen III
-
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0076
Coproporphyrinogen-III
-
competitive inhibition
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
5,5-dithiobis(2-nitrobenzoic acid)
Mus musculus;
-
significant inhibition, IC50: 0.05 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0017
-
wild type enzyme, for mesoporphyrinogen-VI, at 37°C; wild-type, with mesoporphyrinogen-VI as substrate
0.0049
-
wild type enzyme, for coproporphyrinogen-III, at 37°C; wild-type, with coproporphyrinogen-III as substrate
0.0051
-
wild type enzyme, for harderoporphyrinogen, at 37°C; wild-type, with harderoporphyrinogen as substrate
0.009
-
-
0.00925
unpurified enzyme, at pH 7.6 and 25°C
0.06
-
-
0.07
-
-
0.08483
purified enzyme, at pH 7.6 and 25°C
0.12
-
-
0.26
-
-
0.28
-
-
0.375
-
-
0.7
-
-
0.72
-
-
37.5
purified recombinant wild-type and selenomethinonine enzymes
117.5
-
purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4
Chromatium sp.
-
-
6.6 - 6.8
-
mutant R231W does not affect optimum
7.2
-
-
7.3
-
aerobic activity
7.6 - 7.7
-
same value for anaerobic and aerobic oxidation
8.5
-
anaerobic reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
activity range, recombinant enzyme
6.4 - 8.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
-
activity range, recombinant enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
higher enzyme expression in spongy tissue caused by internal breakdown
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
highest specific activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
UNIPROT
ORGANISM
A0A0D5YE19
Acinetobacter baumannii;
P36551
Homo sapiens;
D0VX00
Leishmania donovani;
Leishmania major;
D0VWU6
Leishmania naiffi;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
2 * 30000, recombinant enzyme, SDS-PAGE
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
37500
-
1 * 37500, SDS-PAGE, absence of crosslinker; 2 * 37500, SDS-PAGE and cross-linking studies
37673
-
x * 37673, calculated from gene sequence
37700
-
37700, SDS-PAGE
40300
x * 40300, calculated from amino acid sequence
44000
-
gel filtration
50000
recombinant enzyme, gel filtration
52800
-
x * 52800, SDS-PAGE, oxygen-independent enzyme
58000
-
1 * 58000, recombinant enzyme, SDS-PAGE
61000
-
recombiinant enzyme, gel filtration; recombinant enzyme, gel filtration
71600
-
1 * 71600, SDS-PAGE
75000
-
gel filtration
76000
-
gel filtration
77000
-
minimum catalytic activity, also aggregation to 154000 kDa catalytic activity, gel filtration
80000
-
gel filtration
86000
-
3 * 86000, SDS-PAGE, presence of crosslinker
107000
-
4 * 107000, SDS-PAGE, presence of crosslinker
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
tetramer
-
4 * 107000, SDS-PAGE, presence of crosslinker
trimer
-
3 * 86000, SDS-PAGE, presence of crosslinker
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis
-
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
-
crystal structure analysis
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
-
irreversible inactivation below
390980
7.4
-
highest recovery of activity at 0.2 M KCl
390968
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
a 2 minute incubation of the protein at 56°C leads to a total loss of enzymatic activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme rather unstable, 2 days
-
tends to aggregate during prolonged storage at 4°C
when incubated with 3 M urea, the enzyme is slowly denatured at pH 6.3 and much faster at pH 7.6
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
GSH and dark conditions protect against autooxidation
-
390967
succinate protects against oxidation
-
390975
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.05 M Tris-HCl, pH 7.6, 20% glycerol, 3 months
-
-20°C, 1% (w/v) NaN3 (100 mM Tris, pH 7.6), several years, no loss of activity
-20°C, 30-65% ammonium sulfate precipitate, 2 months
-
-30°C, 0.1 M potassium phosphate, pH 7.6, stable for months
-
25°C, 1% (w/v) NaN3 (100 mM Tris, pH 7.6), several months, no loss of activity
4°C, 0.1 M Tris-HCl, pH 7.4, 50% saturation ammonium sulfate, 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
69fold purificationcalcium phosphate gel
-
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and Ultrogel Ac44 gel filtration
by affinity chromatography; TALON metal affinity resin column chromatography
-
by Ni2+ affinity chromatography
by Ni2+ affinity chromatography; Ni2+ affinity column chromatography
-
by nickel affinity chromatography
-
Ni-NTA agarose metal affinity resin chromatography; Ni-NTA agarose metal affinity resin chromatography
-
Ni2+ affinity chromatography
-
nickel affinity column 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, chromatography techniques
-
to homogeneity, recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6x-his-tagged enzyme expressed in Escherichia coli
-
cpx1 cloned into LambdaZAP
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
DNA sequence determination and analysis of wild-type and mutant genes
-
expressed in Escherichia coli BL21(DE3) cells; expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3)RIL cells; expressed in Escherichia coli strain BL21(DE3)RIL; into vector pET21d
-
expressed in Escherichia coli strain BL21(DE3)RIL; into vector pET21d, expression in Escherichia coli BL21(DE3)RIL
-
expressed in Escherichia coli with the vector pET21d-CO
-
expression in Cos-1 cells
-
expression in Escherichia coli
expression in Escherichia coli BL21(DE3)RIL
-
expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
functional expression in Escherichia coli; recombinant expression of His-tagged enzyme in Escherichia coli
-
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