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1.3.3.15: coproporphyrinogen III oxidase (coproporphyrin-forming)

This is an abbreviated version!
For detailed information about coproporphyrinogen III oxidase (coproporphyrin-forming), go to the full flat file.

Reaction

Coproporphyrinogen III
+ 3 O2 =
coproporphyrin III
+ 3 H2O2

Synonyms

CgoX, coproporphyrinogen III oxidase, coproporphyrinogen oxidase, hemY, PPO, proto'gen oxidase, protoporphyrinogen IX oxidase, protoporphyrinogen oxidase

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.3 With oxygen as acceptor
                1.3.3.15 coproporphyrinogen III oxidase (coproporphyrin-forming)

Engineering

Engineering on EC 1.3.3.15 - coproporphyrinogen III oxidase (coproporphyrin-forming)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F227R
the mutant exhibits slight decrease in catalysis compared to the wild type enzyme
I176A
the mutation leads to about 30fold decrease in catalytic efficiency compared to the wild type enzyme
K71A
the mutation leads to about 50fold decrease in catalytic efficiency compared to the wild type enzyme
P64A
the mutant exhibits a 14fold decrease in catalysis compared to the wild type enzyme
Y366N
the mutation leads to about 100fold decrease in catalytic efficiency compared to the wild type enzyme
K71A
-
the mutation leads to about 50fold decrease in catalytic efficiency compared to the wild type enzyme
-
F187W
-
the mutation inhibits the activation of the enzyme by VU0038882
M167F
-
the mutation inhibits the activation of the enzyme by VU0038882
N186F
-
the mutant exhibits increased baseline activity relative to the wild type enzyme
N186Y
-
the mutant exhibits increased baseline activity relative to the wild type enzyme
T183K
-
the mutation does not restrict enzyme function. The mutant does not respond to VU0038882 at concentrations up to 0.01 mM
F187W
-
the mutation inhibits the activation of the enzyme by VU0038882
-
M167F
-
the mutation inhibits the activation of the enzyme by VU0038882
-
N186F
-
the mutant exhibits increased baseline activity relative to the wild type enzyme
-
N186Y
-
the mutant exhibits increased baseline activity relative to the wild type enzyme
-
T183K
-
the mutation does not restrict enzyme function. The mutant does not respond to VU0038882 at concentrations up to 0.01 mM
-