ENZYME entry: EC 188.8.131.52
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- Toluene + NADH + O(2) <=> 2-methylphenol + NAD(+) + H(2)O
- 2-methylphenol + NADH + O(2) <=> 3-methylcatechol + NAD(+) + H(2)O
- The enzyme, characterized from the bacterium Burkholderia cepacia,
belongs to a class of nonheme, oxygen-dependent diiron enzymes.
- It contains a hydroxylase component with two binuclear iron centers,
an NADH-oxidoreductase component containing FAD and a [2Fe-2S] iron-
sulfur cluster, and a third component involved in electron transfer
between the hydroxylase and the reductase.
- The enzyme dihydroxylates its substrate in two sequential
hydroxylations, initially forming 2-methylphenol, which is
hydroxylated to 3-methylcatechol.
|PRIAM enzyme-specific profiles||184.108.40.206|
|KEGG Ligand Database for Enzyme Nomenclature||220.127.116.11|
|IUBMB Enzyme Nomenclature||18.104.22.168|
|MEDLINE||Find literature relating to 22.214.171.124|
entries corresponding to 1.14.13.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-