1.14.15.25: p-cymene methyl-monooxygenase

This is an abbreviated version!
For detailed information about p-cymene methyl-monooxygenase, go to the full flat file.

Reaction

+ 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ =

+ 2 oxidized ferredoxin [iron-sulfur] cluster +

Synonyms

cymA, cymAa, CymB, CymM, p-cymene methyl hydroxylase

ECTree

1 Oxidoreductases

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor

1.14.15.25 p-cymene methyl-monooxygenase

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Results	in table
1	AA Sequence
3	Cloned(Commentary)
3	Cofactor
1	Expression
1	General Information
1	Molecular Weight [Da]
5	Organism
4	Pathway
1	pH Optimum
1	Reaction
5	Reference
1	Storage Stability
8	Substrates and Products (Substrate)
3	Subunits
7	Synonyms
1	Systematic Name
2	Temperature Stability [°C]

Systematic Name

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Systematic Name on EC 1.14.15.25 - p-cymene methyl-monooxygenase

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p-cymene,ferredoxin:oxygen oxidoreductase (methyl-hydroxylating)

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, ferredoxin---NAD+ reductase) 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, toluene methyl-monooxygenase.