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Information on EC 1.3.3.3 - coproporphyrinogen oxidase and Organism(s) Escherichia coli and UniProt Accession P36553

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EC Tree
     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.3 With oxygen as acceptor
                1.3.3.3 coproporphyrinogen oxidase
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This record set is specific for:
Escherichia coli
UNIPROT: P36553 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
coproporphyrinogen oxidase, coproporphyrinogen iii oxidase, hem13, cpox4, copro'gen oxidase, klhem13, coprogen oxidase, oxygen-dependent coproporphyrinogen iii oxidase, sll1185, hemn1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
coproporphyrinogen-III oxidase
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Coprogen oxidase
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coproporphyrinogen III oxidase
coproporphyrinogenase
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-
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COX
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oxygen-dependent coproporphyrinogen III oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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oxidation
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reduction
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oxidative decarboxylation
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SYSTEMATIC NAME
IUBMB Comments
coproporphyrinogen:oxygen oxidoreductase (decarboxylating)
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CAS REGISTRY NUMBER
COMMENTARY hide
9076-84-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
show the reaction diagram
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-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
show the reaction diagram
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
protoporphyrinogen-IX + O2
protoporphyrin IX + CO2
show the reaction diagram
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capacity to oxidize not only coproporphyrinogen-III but also protoporphyrinogen-IX
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?
protoporphyrinogen-IX + O2
protoporphyrin-IX + CO2
show the reaction diagram
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capacity to oxidize not only coproporphyrinogen-III but also protoporphyrinogen-IX
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?
additional information
?
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no activity of HemF with protoporphyrinogen-IX and coporphyrinogen-III
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
show the reaction diagram
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step in heme biosynthesis
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-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
show the reaction diagram
protoporphyrinogen-IX + O2
protoporphyrin-IX + CO2
show the reaction diagram
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capacity to oxidize not only coproporphyrinogen-III but also protoporphyrinogen-IX
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
about 0.03 mol per mol of polypeptide for both enzyme forms
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
Mn2+
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required, bound to the enzyme, stimulates, restores the enzyme inactivated by metal chelators, coordinated by residues His96, His106, His145, and His175
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
protoporphyrin-IX
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inhibition of HemF
additional information
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mutation of the nucleotide binding motif GGGXXTP does not affect the enzyme activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0031
Coproporphyrinogen-III
recombinant wild-type enzyme, pH 7.0, 37°C
0.0016 - 0.0043
Coproporphyrinogen-III
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
Coproporphyrinogen-III
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recombinant O2-dependent enzyme form
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37.5
purified recombinant wild-type and selenomethinonine enzymes
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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recombinant O2-dependent enzyme form
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
oxygen-dependent enzyme form HemF
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
2 * 35000, recombinant enzyme, SDS-PAGE, 2 * 35390, recombinant enzyme, mass spectrometry, 2 * 35718, recombinant selenomethionine-labeled enzyme, mass spectrometry
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
50000
recombinant enzyme, gel filtration
70000
recombinant enzyme, native PAGE
52800
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x * 52800, SDS-PAGE, oxygen-independent enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 35000, recombinant enzyme, SDS-PAGE, 2 * 35390, recombinant enzyme, mass spectrometry, 2 * 35718, recombinant selenomethionine-labeled enzyme, mass spectrometry
?
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x * 52800, SDS-PAGE, oxygen-independent enzyme
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C167S
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site-directed mutagenesis, activity and kinetics similar to the wild-type
G127V
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site-directed mutagenesis, activity and kinetics similar to the wild-type
H106L
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site-directed mutagenesis, inactive mutant
H145L
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site-directed mutagenesis, inactive mutant
H175L
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site-directed mutagenesis, inactive mutant
H96L
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site-directed mutagenesis, inactive mutant
P133A
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site-directed mutagenesis, activity and kinetics similar to the wild-type
T132A
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site-directed mutagenesis, activity and kinetics similar to the wild-type
W123L
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site-directed mutagenesis, activity and kinetics similar to the wild-type
W124R
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site-directed mutagenesis, activity and kinetics similar to the wild-type
W166L
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site-directed mutagenesis, activity and kinetics similar to the wild-type
W274L
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site-directed mutagenesis, inactive mutant
W298L
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site-directed mutagenesis, activity and kinetics similar to the wild-type
W36L
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site-directed mutagenesis, activity and kinetics similar to the wild-type
Y135F
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site-directed mutagenesis, activity similar to the wild-type
Y160F
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site-directed mutagenesis, activity and kinetics similar to the wild-type
Y170F
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site-directed mutagenesis, activity and kinetics similar to the wild-type
Y213F
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site-directed mutagenesis, activity and kinetics similar to the wild-type
Y240F
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site-directed mutagenesis, activity and kinetics similar to the wild-type
Y276F
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site-directed mutagenesis, activity and kinetics similar to the wild-type
additional information
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mutation of the nucleotide binding motif GGGXXTP does not affect the enzyme activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
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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)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Narita, S.; Taketani, S.; Inokuchi, H.
Oxidation of protoporphyrinogen IX in Escherichia coli is mediated by the aerobic coproporphyrinogen oxidase
Mol. Gen. Genet.
261
1012-1020
1999
Escherichia coli
Manually annotated by BRENDA team
Troup, B.; Hungerer, C.; Jahn, D.
Cloning and characterization of the Escherichia coli hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase
J. Bacteriol.
177
3326-3331
1995
Escherichia coli
Manually annotated by BRENDA team
Macieira, S.; Martins, B.M.; Huber, R.
Oxygen-dependent coproporphyrinogen-III oxidase from Escherichia coli: one-step purification and biochemical characterisation
FEMS Microbiol. Lett.
226
31-37
2003
Escherichia coli (P36553), Escherichia coli
Manually annotated by BRENDA team
Breckau, D.; Mahlitz, E.; Sauerwald, A.; Layer, G.; Jahn, D.
Oxygen-dependent coproporphyrinogen III oxidase (HemF) from Escherichia coli is stimulated by manganese
J. Biol. Chem.
278
46625-46631
2003
Escherichia coli
Manually annotated by BRENDA team
Layer, G.; Kervio, E.; Morlock, G.; Heinz, D.W.; Jahn, D.; Retey, J.; Schubert, W.D.
Structural and functional comparison of HemN to other radical SAM enzymes
Biol. Chem.
386
971-980
2005
Escherichia coli
Manually annotated by BRENDA team