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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Cofactor
Cofactor on EC 1.3.98.3 - coproporphyrinogen dehydrogenase
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4Fe-4S-center
HemN binds a 4Fe-4S cluster through three cysteine residues: Cys-62, Cys-66 and Cys-69, a juxtaposed S-adenosyl-L-methionine coordinates the fourth Fe ion through its amide nitrogen and carboxylate oxygen, detailed binding mode, cofactor geometry required for Radical SAM catalysis
4Fe-4S-center
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requirement, oxygen-sensitive Fe-S cluster, Cys-62, Cys-66 and Cys-69 are part of the conserved CXXXCXXC motif and essential for Fe-S cluster formation and enzyme function, Tyr-56 and His-58 are important for the Fe-S cluster integrity, His-58 may provide the fourth ligand besides the three cysteine residues
4Fe-4S-center
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structure, location and coordination of the cofactor, HemN requires the juxtaposition of the [4Fe-4S] cluster and the cosubstrate S-adenosyl-L-methionine
heme
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in vivo, HemW occurs as a heme-free cytosolic form, as well as a heme-containing membrane-associated form
S-adenosyl-L-methionine
HemN contains two S-adenosyl-L-methionine molecules as cofactors, detailed binding mode
S-adenosyl-L-methionine
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HemN contains a catalytically essential [4Fe-4S] cluster that transfers an electron to bound S-adenosyl-L-methionine, thereby producing methionine and a 5'-deoxyadenosyl radical
S-adenosyl-L-methionine
HemN is a radical S-adenosyl-L-methionine and [4Fe-4S] containing enzyme