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Literature summary for 1.3.98.5 extracted from

  • Milazzo, L.; Gabler, T.; Pfanzagl, V.; Michlits, H.; Furtmueller, P.G.; Obinger, C.; Hofbauer, S.; Smulevich, G.
    The hydrogen bonding network of coproheme in coproheme decarboxylase from Listeria monocytogenes Effect on structure and catalysis (2019), J. Inorg. Biochem., 195, 61-70 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
K151A disruption of the H-bond interactions with p2 and p4, impairs the structural rearrangement upon binding of coproheme. Decarboxylation activity is highly impaired Listeria monocytogenes serotype 1/2a
Q187A catalytic activity similar to wild-type Listeria monocytogenes serotype 1/2a
R133A catalytic activity similar to wild-type Listeria monocytogenes serotype 1/2a
R179A catalytic activity similar to wild-type Listeria monocytogenes serotype 1/2a
Y113A catalytic activity similar to wild-type Listeria monocytogenes serotype 1/2a
Y113A/K151A disruption of the H-bond interactions with p2 and p4, impairs the structural rearrangement upon binding of coproheme Listeria monocytogenes serotype 1/2a
Y147A mutant is completely inactive Listeria monocytogenes serotype 1/2a
Y147A/R220A/S225A mutations affect the extended H-bond network spanning from p2 to p4 Listeria monocytogenes serotype 1/2a

Organism

Organism UniProt Comment Textmining
Listeria monocytogenes serotype 1/2a Q8Y5F1
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-
Listeria monocytogenes serotype 1/2a ATCC BAA-679 Q8Y5F1
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Fe-coproporphyrin III + 2 H2O2
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 Listeria monocytogenes serotype 1/2a heme b + 2 CO2 + 4 H2O
-
 ?
Fe-coproporphyrin III + 2 H2O2
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 Listeria monocytogenes serotype 1/2a ATCC BAA-679 heme b + 2 CO2 + 4 H2O
-
 ?

Synonyms

Synonyms Comment Organism
ChdC
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 Listeria monocytogenes serotype 1/2a