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

Reaction

Coproporphyrinogen III
+ 2 S-adenosyl-L-methionine =
protoporphyrinogen IX
+ 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine

Synonyms

anaerobic coproporphyrinogen III oxidase, At5g63290, AtHEMN1, BtrN, Coprogen oxidase, coproporphyrinogen III oxidase, coproporphyrinogen oxidase, coproporphyrinogenase, CPO, 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

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.98 With other, known, physiological acceptors
                1.3.98.3 coproporphyrinogen dehydrogenase

Engineering

Engineering on EC 1.3.98.3 - coproporphyrinogen dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C62S
-
inactive mutant, no Fe-S cluster formation
C66S
-
inactive mutant, no Fe-S cluster formation
C69S
-
inactive mutant, no Fe-S cluster formation
C71S
-
inactive mutant, same Fe-S cluster formation as in wild-type HemN
E145A
-
appears colorless, the [4Fe-4S] cluster content is slightly reduced, no detectable S-adenosylmethionine cleavage, no detectable CPO activity
E145I
-
appears colorless, the [4Fe-4S] cluster content is slightly reduced, no detectable S-adenosylmethionine cleavage, no detectable CPO activity
F310A
-
is slightly yellow, the [4Fe-4S] cluster content is slightly reduced, cleaves only one S-adenosylmethionine molecule per molecule protein, residual CPO activity
F310L
-
is slightly yellow, the [4Fe-4S] cluster content is slightly reduced, cleaves only one S-adenosylmethionine molecule per molecule protein, no detectable CPO activity
F68L
-
mutant with 89% of wild-type activity
G111V/G113V
-
double mutation of Gly-111 and Gly-113, which are part of the potential GGGTP S-adenosyl-L-methionine binding motif, completely abolishes enzyme activity, reduced Fe-S cluster formation
H58L
-
inactive mutant, no Fe-S cluster formation
I329A
-
contains the same amount of iron-sulfur cluster as the wild-type HemN, but cleaves only one S-adenosylmethionine molecule per molecule protein, no detectable CPO activity; exhibits the same yellow-brown color as wild-type HemN, but the [4Fe-4S] cluster content is slightly reduced and cleaves only one S-adenosylmethionine molecule per molecule protein, no detectable CPO activity
Q311A
-
contains the same amount of iron-sulfur cluster as the wild-type HemN, but cleaves only one S-adenosylmethionine molecule per molecule protein, no detectable CPO activity; exhibits the same yellow-brown color as wild-type HemN, but the [4Fe-4S] cluster content is slightly reduced and cleaves only one S-adenosylmethionine molecule per molecule protein, no detectable CPO activity
Y56A
-
appears colorless, the [4Fe-4S] cluster content is slightly reduced, no detectable S-adenosylmethionine cleavage, no detectable CPO activity
Y56F
-
mutant with 45% of wild-type activity and reduced Fe-S cluster formation
Y56L
-
appears colorless, the [4Fe-4S] cluster content is slightly reduced, no detectable S-adenosylmethionine cleavage, no detectable CPO activity
additional information