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4.1.1.83
The ferredoxin-like domain of the activating enzyme is required for generating a lasting glycyl radical in 4-hydroxyphenylacetate decarboxylase
Clostridioides difficile
4.1.1.83
4-Hydroxyphenylacetate decarboxylase activating enzyme catalyses a classical S-adenosylmethionine reductive cleavage reaction
Clostridium scatologenes
4.1.1.83
4-hydroxyphenylacetate decarboxylases: Properties of a novel subclass of glycyl radical enzyme systems
Clostridioides difficile
4.1.1.83
4-hydroxyphenylacetate decarboxylases: Properties of a novel subclass of glycyl radical enzyme systems
Clostridium scatologenes
4.1.1.83
4-hydroxyphenylacetate decarboxylases: Properties of a novel subclass of glycyl radical enzyme systems
Clostridium scatologenes 957
4.1.1.83
Catalytic mechanism of the glycyl radical enzyme 4-hydroxyphenylacetate decarboxylase from continuum electrostatic and QC/MM calculations
Clostridium scatologenes
4.1.1.83
p-Cresol formation by cell-free extracts of Clostridium difficile
Clostridioides difficile
4.1.1.83
p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p-cresol
Clostridioides difficile
4.1.1.83
Structural basis for a Kolbe-type decarboxylation catalyzed by a glycyl radical enzyme
Clostridium scatologenes
4.1.1.83
Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is essential for catalytic activity
Clostridioides difficile
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