| EC |
2.7.1.238 |
| Accepted name: |
phenol phosphorylase |
| Reaction: |
ATP + phenol + H2O = AMP + phenyl phosphate + phosphate |
| Other name(s): |
phenylphosphate synthase |
| Systematic name: |
ATP:phenol phosphotransferase (AMP-forming) |
| Comments: |
The enzyme, characterized from the bacterium Thauera aromatica, catalyses the first step in an anaerobic phenol degradation pathway. The enzyme, composed of three subunits, transfers the β-phosphoryl from ATP to phenol, forming phenyl phosphate, AMP, and phosphate [1]. During catalysis a diphosphoryl group is transferred from ATP to a histidine residue in one of the enzyme's subunits, from which phosphate is cleaved to render the reaction unidirectional. The remaining histidine phosphate subsequently serves as the actual phosphorylation agent [2]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Schmeling, S., Narmandakh, A., Schmitt, O., Gad'on, N., Schuhle, K. and Fuchs, G. Phenylphosphate synthase: a new phosphotransferase catalyzing the first step in anaerobic phenol metabolism in Thauera aromatica. J. Bacteriol. 186 (2004) 8044–8057. [DOI] [PMID: 15547277] |
| 2. |
Narmandakh, A., Gad'on, N., Drepper, F., Knapp, B., Haehnel, W. and Fuchs, G. Phosphorylation of phenol by phenylphosphate synthase: role of histidine phosphate in catalysis. J. Bacteriol. 188 (2006) 7815–7822. [DOI] [PMID: 16980461] |
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| [EC 2.7.1.238 created 2022] |
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