_EC 1.14.15.25 p-cymene methyl-monooxygenase.

0 PDB entries

EC 1.-.-.- Oxidoreductases. [21,484 PDB entries] EC 1.14.-.- Acting on paired donors, with incorporation or reduction of molecu [4,719 PDB entries] EC 1.14.15.- With reduced iron-sulfur protein as one donor, and incorporation [293 PDB entries] EC 1.14.15.25 p-cymene methyl-monooxygenase. [-]

Reaction:		p-cymene + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H(+) = 4-isopropylbenzyl alcohol + 2 oxidized [2Fe-2S]-[ferredoxin] + H2O.
		p-cymene + 2 × reduced [2Fe-2S]-[ferredoxin] + O2 + 2 × H(+) = 4-isopropylbenzyl alcohol + 2 × oxidized [2Fe-2S]-[ferredoxin] + H2O Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Other name(s):		p-cymene methyl hydroxylase.
Comments:		The enzyme, characterized from several Pseudomonas strains, initiates p-cymene catabolism through hydroxylation of the methyl group. The enzyme has a distinct preference for substrates containing at least an alkyl or heteroatom substituent at the para-position of toluene. The electrons are provided by a reductase (EC 1.18.1.3) that transfers electrons from Nadh via fad and an [2Fe-2S] cluster. In Pseudomonas chlororaphis the presence of a third component of unknown function greatly increases the activity. cf. Ec 1.14.15.26.
Links:		[IntEnz]   [ExPASy]   [KEGG]

There are no PDB entries in enzyme class E.C.1.14.15.25