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1.3.98.5: hydrogen peroxide-dependent heme synthase

This is an abbreviated version!
For detailed information about hydrogen peroxide-dependent heme synthase, go to the full flat file.

Word Map on EC 1.3.98.5

Reaction

Fe-coproporphyrin III
+ 2 H2O2 =
protoheme
 + 2 CO2 + 4 H2O

Synonyms

ChdC, coproheme decarboxylase, coproheme III oxidative decarboxylase, HemQ, Imo2113, lmo2113

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.98 With other, known, physiological acceptors
                1.3.98.5 hydrogen peroxide-dependent heme synthase

Engineering

Engineering on EC 1.3.98.5 - hydrogen peroxide-dependent heme synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K151A
disruption of the H-bond interactions with p2 and p4, impairs the structural rearrangement upon binding of coproheme. Decarboxylation activity is highly impaired
M149A
mutation alters the heme coordination, which becomes a 6-coordinate low spin species with the amide nitrogen atom of the Q187 residue bound to the heme iron. In the mutant, two CO conformers are present corresponding to open (A0) and closed (A1) conformations. Residue M149 is involved in the formation of a covalent bond with a vinyl substituent of heme b at excess of hydrogen peroxide
M149A/Q187A
binding of coproheme is significantly decreased. In the absence of the Q187, only the A0 conformer is found
Q187A
R133A
catalytic activity similar to wild-type
R179A
catalytic activity similar to wild-type
Y113A
catalytic activity similar to wild-type
Y113A/K151A
disruption of the H-bond interactions with p2 and p4, impairs the structural rearrangement upon binding of coproheme
Y147A
mutant is completely inactive
Y147A/R220A/S225A
mutations affect the extended H-bond network spanning from p2 to p4
K151A
-
disruption of the H-bond interactions with p2 and p4, impairs the structural rearrangement upon binding of coproheme. Decarboxylation activity is highly impaired
-
M149A
-
mutation alters the heme coordination, which becomes a 6-coordinate low spin species with the amide nitrogen atom of the Q187 residue bound to the heme iron. In the mutant, two CO conformers are present corresponding to open (A0) and closed (A1) conformations. Residue M149 is involved in the formation of a covalent bond with a vinyl substituent of heme b at excess of hydrogen peroxide
-
M149A/Q187A
-
binding of coproheme is significantly decreased. In the absence of the Q187, only the A0 conformer is found
-
Q187A
-
in the absence of the Q187, only the A0 conformer is found compared to two CO conformers are present corresponding to open (A0) and closed (A1) conformations in mutant M149A
-
R133A
-
catalytic activity similar to wild-type
-
R179A
-
catalytic activity similar to wild-type
-
Y113A
-
catalytic activity similar to wild-type
-
Y147A
-
mutant is completely inactive
-
H156A
-
the mutant shows less than 10% of wild type activity
H156C
-
the mutant shows less than 10% of wild type activity