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EC 1.14.15.25 Details
show Brenda entryEC number
1.14.15.25
Accepted name
p-cymene methyl-monooxygenase
Reaction
p-cymene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = 4-isopropylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Other name(s)
cymAa (gene name),
cymA (gene name),
p-cymene methyl hydroxylase
Systematic name
p-cymene,ferredoxin:oxygen oxidoreductase (methyl-hydroxylating)
Comment
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.
History
created 2018
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1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.6.7.1 created 1972, deleted 1978 1.6.7.2 created 1972, deleted 1978 1.6.7.3 created 1978, deleted 1978 1.14.99.5 created 1972, modified 1986, modified 2000, deleted 2000 1.14.99.6 created 1972, modified 2000, deleted 2000 1.14.99.8 created 1972, deleted 1984 1.14.99.13 created 1972, deleted 1984 1.14.99.16 created 1972, deleted 2002 1.14.99.17 created 1972, deleted 1976 1.14.99.18 created 1976, modified 1999, deleted 2003 1.14.99.25 created 1986, deleted 2000
