EC |
4.1.1.83 |
Accepted name: |
4-hydroxyphenylacetate decarboxylase |
Reaction: |
(4-hydroxyphenyl)acetate + H+ = 4-methylphenol + CO2 |
Other name(s): |
p-hydroxyphenylacetate decarboxylase; p-Hpd; 4-Hpd; 4-hydroxyphenylacetate carboxy-lyase |
Systematic name: |
(4-hydroxyphenyl)acetate carboxy-lyase (4-methylphenol-forming) |
Comments: |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 340137-18-0 |
References: |
1. |
D'Ari, L. and Barker, H.A. p-Cresol formation by cell-free extracts of Clostridium difficile. Arch. Microbiol. 143 (1985) 311–312. [PMID: 3938267] |
2. |
Selmer, T. and Andrei, P.I. p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p-cresol. Eur. J. Biochem. 268 (2001) 1363–1372. [DOI] [PMID: 11231288] |
3. |
Andrei, P.I., Pierik, A.J., Zauner, S., Andrei-Selmer, L.C. and 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) 2225–2230. [DOI] [PMID: 15153112] |
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[EC 4.1.1.83 created 2005] |
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