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
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1.3.98.5
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propionate
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raman
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listeria
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monocytogenes
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propionyl
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decarboxylases
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monoderm
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uv-vis
- 1.3.98.5
- propionate
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raman
-
listeria
- monocytogenes
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propionyl
- decarboxylases
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monoderm
-
uv-vis
Reaction
Synonyms
ChdC, coproheme decarboxylase, coproheme III oxidative decarboxylase, HemQ, Imo2113, lmo2113
ECTree
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Engineering
Engineering on EC 1.3.98.5 - hydrogen peroxide-dependent heme synthase
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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
Y113A/K151A
disruption of the H-bond interactions with p2 and p4, impairs the structural rearrangement upon binding of coproheme
Y147A/R220A/S225A
mutations affect the extended H-bond network spanning from p2 to p4
K151A
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disruption of the H-bond interactions with p2 and p4, impairs the structural rearrangement upon binding of coproheme. Decarboxylation activity is highly impaired
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M149A
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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
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M149A/Q187A
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binding of coproheme is significantly decreased. In the absence of the Q187, only the A0 conformer is found
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Q187A
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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
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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