EC Number   |
Substrates |
Organism  |
Products |
Reversibility |
|---|
    1.3.98.3 | coproporphyrinogen-III + S-adenosyl-L-methionine |
- |
Cereibacter sphaeroides |
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine |
- |
? |
| 1.3.98.3 | coproporphyrinogen III + 2 S-adenosyl-L-methionine |
- |
Escherichia coli |
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine |
- |
? |
| 1.3.98.3 | coproporphyrinogen III + 2 S-adenosyl-L-methionine |
via reaction intermediate harderoporphyrinogen, not isoharderoporphyrinogen |
Escherichia coli |
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine |
- |
? |
| 1.3.98.3 | coproporphyrinogen III + 2 S-adenosyl-L-methionine |
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 |
Escherichia coli |
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine |
- |
? |
| 1.3.98.3 | coproporphyrinogen III + 2 S-adenosyl-L-methionine |
conversion of coproporphyrinogen III to protoporphyrinogen IX via the reaction intermediate harderoporphyrinogen |
Escherichia coli |
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine |
- |
? |
| 1.3.98.3 | coproporphyrinogen-III + S-adenosyl-L-methionine |
- |
Escherichia coli |
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine |
- |
? |
| 1.3.98.3 | coproporphyrinogen-III + S-adenosyl-L-methionine |
HemN catalyzes the essential conversion of coproporphyrinogen-III to protoporphyrinogen IX during heme biosynthesis |
Escherichia coli |
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine |
- |
? |
| 1.3.98.3 | coproporphyrinogen-III + S-adenosyl-L-methionine |
HemN catalyzes the prepenultimate step in anaerobic heme biosynthesis |
Escherichia coli |
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine |
- |
? |
| 1.3.98.3 | coproporphyrinogen-III + S-adenosyl-L-methionine |
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 |
Escherichia coli |
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine |
- |
? |
| 1.3.98.3 | coproporphyrinogen-III + S-adenosyl-L-methionine |
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 |
Escherichia coli |
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine |
- |
? |
