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IUBMB 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 , ferredoxin—NAD+ Pseudomonas chlororaphis the presence of a third component of unknown function greatly increases the activity. cf . EC 1.14.15.26 , toluene methyl-monooxygenase.
Reaction Schemes
+
+
2
reduced ferredoxin [iron-sulfur] cluster
+
2
=
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
Synonyms
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p-cymene methyl hydroxylase
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-
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cymA
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-
-
-
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p-cymene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = 4-isopropylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
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-
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-
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MetaCyc
p-cymene degradation to p-cumate
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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.
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4-(methylthio)toluene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
4-(methylthio)benzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
O33456; O33457
Substrates: -
?
4-chlorostyrene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
4-chlorostyrene oxide + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
O33456; O33457
Substrates: -
?
4-ethyltoluene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
4-ethylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
O33456; O33457
Substrates: -
?
4-fluorotoluene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
4-fluorobenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
O33456; O33457
Substrates: -
?
p-cymene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
4-isopropylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
O33456; O33457
Substrates: -
?
styrene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
styrene oxide + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
O33456; O33457
Substrates: -
?
additional information
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O33456; O33457
Substrates: enzyme can attack benzylic and toluic alcohols as well as toluene and xylenes, probably with the formation of gem-diol intermediates which spontaneously dehydrate to yield the corresponding aldehydes
?
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[2Fe-2S]-center
O33456; O33457
reductase subunit CymAb
Ferredoxin
O33456; O33457
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Ferredoxin
O33456; O33457
reductase subunit CymAb
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8.4
NADH-cytochrome c reductase activity of subunit CymA
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UniProt
brenda
P95461 i.e. reductase subunit CymA, cf. EC 1.8.1.3, O84920 i.e. subunit CymB, O84919 i.e. subunit CymM
UniProt
brenda
P95461 i.e. subunit CymA, O84920 i.e. subunit CymB, O84919 i.e. subunit CymM
UniProt
brenda
O33456 i.e. hydroxylase subunit CymAa, O33457 i.e. reductase subunit CymAb, cf. EC 1.8.1.3
O33456; O33457
UniProt
brenda
O33456 i.e. subunit CymAa, O33457 i.e. subunit CymAb
O33456; O33457
UniProt
brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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physiological function
expression of all three components (cymMBA) in Escherichia coli leads to p-cymene methyl group hydroxylation, while expression of cymM and cymA along with the partially truncated cymB gene shows an 85% decrease in the hydroxylation capacity. The CymM gene product shows similarity to integral-membrane di-iron enzymes, while that CymB shows no significant similarity to other known proteins
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P95461_9PSED
349
0
38433
TrEMBL
-
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39000
gel fitlration, reductase component CymA
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?
x * 38400, calculated
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x * 38433, calculated, x * 38000, SDS-PAGE of reductase component CymA
?
O33456; O33457
x * 43117, hydrolase subunit CymAa, x * 38295, reductase subunit CymAb, calculated
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30
10 min, 42% loss of activity, NADH-cytochrome c reductase activity of subunit CymA
50
10 min, 98% loss of activity, NADH-cytochrome c reductase activity of subunit CymA
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70°C, 50 mM potassium phosphate buffer (pH 7.0), 60% glycerol (v/v), subunit CymA is stable for 1 month
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expression in Escherichia coli
O33456; O33457
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expression of subunits CymABM is induced by growth on p-cymene
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Nishio, T.; Patel, A.; Wang, Y.; Lau, P.C.
Biotransformations catalyzed by cloned p-cymene monooxygenase from Pseudomonas putida F1
Appl. Microbiol. Biotechnol.
55
321-325
2001
Pseudomonas putida (O33456 and O33457)
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Dutta, T.K.; Gunsalus, I.C.
Reductase gene sequences and protein structures p-cymene methyl hydroxylase
Biochem. Biophys. Res. Commun.
233
502-506
1997
Pseudomonas chlororaphis subsp. aureofaciens (P95461), Pseudomonas chlororaphis subsp. aureofaciens
brenda
Eaton, R.W.
p-Cymene catabolic pathway in Pseudomonas putida F1 cloning and characterization of DNA encoding conversion of p-cymene to p-cumate
J. Bacteriol.
179
3171-3180
1997
Pseudomonas putida (O33456 and O33457)
brenda
Dutta, T.; Dutta, A.; Chakraborty, J.; Sarkar, J.; Pal Chowdhury, P.; Gunsalus, I.
Purification and properties of reductase of the three-component p-cymene methyl hydroxylase from Pseudomonas chlororaphis subsp. aureofaciens
Process Biochem.
47
1263-1267
2012
Pseudomonas chlororaphis subsp. aureofaciens (P95461 and O84920 and O84919)
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brenda
Dutta, T.; Chakraborty, J.; Roy, M.; Ghosal, D.; Khara, P.; Gunsalus, I.
Cloning and characterization of a p-cymene monooxygenase from Pseudomonas chlororaphis subsp. aureofaciens
Res. Microbiol.
161
876-882
2010
Pseudomonas chlororaphis subsp. aureofaciens (P95461 and O84920 and O84919)
brenda
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