Reference on EC 4.1.1.83 - 4-hydroxyphenylacetate decarboxylase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
D'Ari, L.; Barker, H.A.
p-Cresol formation by cell-free extracts of Clostridium difficile
Arch. Microbiol.
143
311-312
1985
Clostridioides difficile
Selmer, T.; Andrei, P.I.
p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p-cresol
Eur. J. Biochem.
268
1363-1372
2001
Clostridioides difficile
Andrei, P.I.; Pierik, A.J.; Zauner, S.; Andrei-Selmer, L.C.; Selmer, T.
Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is essential for catalytic activity
Eur. J. Biochem.
271
2225-2230
2004
Clostridioides difficile (Q84F14), Clostridioides difficile (Q84F15), Clostridioides difficile (Q84F16), Clostridioides difficile
Yu, L.; Blaser, M.; Andrei, P.I.; Pierik, A.J.; Selmer, T.
4-hydroxyphenylacetate decarboxylases: Properties of a novel subclass of glycyl radical enzyme systems
Biochemistry
45
9584-9592
2006
Clostridioides difficile, Clostridium scatologenes, Clostridium scatologenes 957
Martins, B.M.; Blaser, M.; Feliks, M.; Ullmann, G.M.; Buckel, W.; Selmer, T.
Structural basis for a Kolbe-type decarboxylation catalyzed by a glycyl radical enzyme
J. Am. Chem. Soc.
133
14666-14674
2011
Clostridium scatologenes (Q38HX4), Clostridium scatologenes
Feliks, M.; Martins, B.M.; Ullmann, G.M.
Catalytic mechanism of the glycyl radical enzyme 4-hydroxyphenylacetate decarboxylase from continuum electrostatic and QC/MM calculations
J. Am. Chem. Soc.
135
14574-14585
2013
Clostridium scatologenes
Selvaraj, B.; Pierik, A.J.; Bill, E.; Martins, B.M.
4-Hydroxyphenylacetate decarboxylase activating enzyme catalyses a classical S-adenosylmethionine reductive cleavage reaction
J. Biol. Inorg. Chem.
18
633-643
2013
Clostridium scatologenes
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