4-hydroxyphenylacetate decarboxylase;
p-hydroxyphenylacetate decarboxylase;
p-Hpd;
4-Hpd;
4-hydroxyphenylacetate carboxy-lyase

Lyases;
Carbon-carbon lyases;
Carboxy-lyases

4-(hydroxyphenyl)acetate carboxy-lyase (4-methylphenol-forming)

(4-hydroxyphenyl)acetate + H+ = 4-methylphenol + CO2 [RN:R07312]

R07312

4-hydroxyphenylacetate [CPD:C00642];
H+ [CPD:C00080]

The enzyme, from the strict anaerobe Clostridium difficile, can also use (3,4-dihydroxyphenyl)acetate as a substrate, yielding 4-methylcatechol as a product. The enzyme is a glycyl radical enzyme.

1  [PMID:3938267]

D'Ari L, Barker HA.

p-Cresol formation by cell-free extracts of Clostridium difficile.

Arch. Microbiol. 143 (1985) 311-2.

Clostridium difficile [GN:cdf]

2  [PMID:11231288]

Selmer T, Andrei PI.

p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p-cresol.

Eur. J. Biochem. 268 (2001) 1363-72.

Clostridium difficile [GN:cdf]

3  [PMID:15153112]

Andrei PI, Pierik AJ, Zauner S, Andrei-Selmer LC, 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 (2004) 2225-30.

Clostridium difficile [GN:cdf]