1.3.98.3: coproporphyrinogen dehydrogenase
This is an abbreviated version!
For detailed information about coproporphyrinogen dehydrogenase, go to the full flat file.
Word Map on EC 1.3.98.3
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1.3.98.3
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viruses
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interferon-inducible
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s-adenosylmethionine
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interferon-stimulated
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5\'-deoxyadenosyl
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ifn-stimulated
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isg15
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ifn-inducible
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radical-mediated
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polyi:c
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myxovirus
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ifitm3
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5'-deoxyadenosine
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maturase
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hydg
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protoporphyrinogen
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chuat
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siniperca
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medicine
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pharmacology
- 1.3.98.3
- viruses
-
interferon-inducible
- s-adenosylmethionine
-
interferon-stimulated
-
5\'-deoxyadenosyl
-
ifn-stimulated
- isg15
-
ifn-inducible
-
radical-mediated
-
polyi:c
-
myxovirus
-
ifitm3
- 5'-deoxyadenosine
-
maturase
- hydg
- protoporphyrinogen
-
chuat
-
siniperca
- medicine
- pharmacology
Reaction
+ 2 S-adenosyl-L-methionine = + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
Synonyms
anaerobic coproporphyrinogen III oxidase, At5g63290, AtHEMN1, BtrN, CgoX, Coprogen oxidase, coproporphyrinogen III oxidase, coproporphyrinogen oxidase, coproporphyrinogenase, CPO, EC 1.3.99.22, HemN, HEMN1, HemW, More, oxidase, coproporphyrinogen, oxygen-independent coproporphyrinogen III oxidase, oxygen-independent coproporphyrinogen-III oxidase, oxygen-independent CPO, radical S-adenosyl-L-methionine dehydrogenase, radical SAM enzyme, Sll1876, Sll1917, viperin
ECTree
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Substrates Products
Substrates Products on EC 1.3.98.3 - coproporphyrinogen dehydrogenase
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REACTION DIAGRAM
2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine
3-amino-2,3-dideoxy-scyllo-inosose + CO2 + L-methionine + 5'-deoxyadenosine
2-deoxystreptamine + S-adenosyl-L-methionine
? + CO2 + L-methionine + 5'-deoxyadenosine
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14.4% activity compared to 2-deoxy-scyllo-inosamine
-
-
?
coproporphyrinogen III + 2 S-adenosyl-L-methionine
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
coproporphyrinogen III + S-adenosyl-L-methionine
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
coproporphyrinogen-III + S-adenosyl-L-methionine
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
harderoporphyrinogen + 2 S-adenosyl-L-methionine
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
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HemN can utilize chemically synthesized harderoporphyrinogen as a substrate and converts it to protoporphyrinogen IX
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-
?
harderoporphyrinogen + S-adenosyl-L-methionine
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
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chemical substrate sythesis, overview
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-
?
myo-inositol + S-adenosyl-L-methionine
? + CO2 + L-methionine + 5'-deoxyadenosine
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0.9% activity compared to 2-deoxy-scyllo-inosamine
-
-
?
scyllo-inositol + S-adenosyl-L-methionine
? + CO2 + L-methionine + 5'-deoxyadenosine
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3.3% activity compared to 2-deoxy-scyllo-inosamine
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-
?
3-amino-2,3-dideoxy-scyllo-inosose + CO2 + L-methionine + 5'-deoxyadenosine
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-
-
-
r
2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine
3-amino-2,3-dideoxy-scyllo-inosose + CO2 + L-methionine + 5'-deoxyadenosine
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100% activity
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-
?
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
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-
-
-
?
coproporphyrinogen III + 2 S-adenosyl-L-methionine
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
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via reaction intermediate harderoporphyrinogen, not isoharderoporphyrinogen
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-
?
coproporphyrinogen III + 2 S-adenosyl-L-methionine
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
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via reaction intermediate harderoporphyrinogen, not isoharderoporphyrinogen. During this reaction the propionate side chains on pyrrole rings A and B of coproporphyrinogen III are oxidatively decarboxylated to the corresponding vinyl groups of protoporphyrinogen IX. Two molecules of CO2 are released during the reaction and a final electron acceptor is required to take up two electrons from each side chain
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-
?
coproporphyrinogen III + 2 S-adenosyl-L-methionine
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
conversion of coproporphyrinogen III to protoporphyrinogen IX via the reaction intermediate harderoporphyrinogen
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-
?
coproporphyrinogen III + 2 S-adenosyl-L-methionine
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
-
-
-
?
coproporphyrinogen III + 2 S-adenosyl-L-methionine
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
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reductive cleavage of S-adenosyl-L-methionine to produce methionine and a 5'-deoxyadenosyl radical intermediate, a reaction characteristic of the radical SAM superfamily, due to the presence of a CX3CX2C motif
detection of the cleavage and degradation products and analysis by mass spectrometry, overview
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?
coproporphyrinogen III + 2 S-adenosyl-L-methionine
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
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-
-
?
coproporphyrinogen III + 2 S-adenosyl-L-methionine
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
-
-
-
?
coproporphyrinogen III + 2 S-adenosyl-L-methionine
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
-
-
-
?
coproporphyrinogen III + 2 S-adenosyl-L-methionine
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
sll1876 encodes HemN operating under micro-oxic conditions
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-
?
coproporphyrinogen III + 2 S-adenosyl-L-methionine
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
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only Sll1876 shows CPO activity under anaerobic conditions, Sll1917 is inactive
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-
?
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
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-
-
-
?
coproporphyrinogen III + S-adenosyl-L-methionine
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
-
-
-
-
?
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
-
-
-
-
?
coproporphyrinogen-III + S-adenosyl-L-methionine
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
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-
-
-
?
coproporphyrinogen-III + S-adenosyl-L-methionine
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
HemN catalyzes the essential conversion of coproporphyrinogen-III to protoporphyrinogen IX during heme biosynthesis
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-
?
coproporphyrinogen-III + S-adenosyl-L-methionine
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
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HemN catalyzes the prepenultimate step in anaerobic heme biosynthesis
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-
?
coproporphyrinogen-III + S-adenosyl-L-methionine
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
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HemN catalyzes the oxygen-independent conversion of coproporphyrinogen-III to protoporphyrinogen IX, requires S-adenosyl-L-methionine, NAD(P)H and additional cytoplasmatic components for catalysis. Cys-62, Cys-66 and Cys-69 are part of the conserved CXXXCXXC motif and essential for iron-sulfur cluster formation and enzyme function. Gly-111 and Gly-113 are part of the potential GGGTP S-adenosyl-L-methionine binding motif and essential for enzymatic function, catalytic, radical mechanism
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-
?
coproporphyrinogen-III + S-adenosyl-L-methionine
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
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HemN requires the juxtaposition of the [4Fe-4S] cluster and the cosubstrate S-adenosyl-L-methionine. The reaction involves the stereospecific hydrogen abstraction of the pro-S hydrogen from the propionate side chain beta-C of coproporphyrinogen-III, involvement of a coproporphyrinogenyl III radical, which is then decarboxylated releasing CO2 and forming the vinyl group, enzyme structure, two-domain enzyme consisting of the catalytic N- and an alpha-helical C-terminal domain, substrate binding mode
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-
?
coproporphyrinogen-III + S-adenosyl-L-methionine
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
mechanism, the S-adenosyl-L-methionine sulfonium sulfur is near both the Fe and neighboring sulfur of the cluster allowing single electron transfer from the 4Fe-4S cluster to the S-adenosyl-L-methionine sulfonium. S-adenosyl-L-methionine is cleaved yielding a highly oxidizing 5-deoxyadenosyl radical, HemN binds a second S-adenosyl-L-methionine immediately adjacent to the first and may thus successively catalyze two propionate decarboxylations. Cofactor geometry required for Radical SAM catalysis, detailed enzyme structure, two distinct domains, domain structure, S-adenosyl-L-methionine binding mode
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-
?
coproporphyrinogen-III + S-adenosyl-L-methionine
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
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-
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?
?
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HemW shows no coproporphyrinogen III oxidase activity in vivo or in vitro
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-
?
additional information
?
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no activity with 1L-chiro-inositol, muco-inositol, allo-inositol, D-glucose, D-glucosamine, D-xylose, 1D-chiro-inositol, and 2,3-dideoxy-scyllo-inosose
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?