Information on EC 1.14.15.25 - p-cymene methyl-monooxygenase

for references in articles please use BRENDA:EC1.14.15.25
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Pseudomonas

EC NUMBER
COMMENTARY hide
1.14.15.25
-
RECOMMENDED NAME
GeneOntology No.
p-cymene methyl-monooxygenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
p-cymene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = 4-isopropylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
p-cymene degradation to p-cumate
-
-
Xylene degradation
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
p-cymene,ferredoxin:oxygen oxidoreductase (methyl-hydroxylating)
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
P95461 and O84920 and O84919
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-(methylthio)toluene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
4-(methylthio)benzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
O33456 and O33457
-
-
-
?
4-chlorostyrene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
4-chlorostyrene oxide + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
O33456 and O33457
-
-
-
?
4-ethyltoluene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
4-ethylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
O33456 and O33457
-
-
-
?
4-fluorotoluene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
4-fluorobenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
O33456 and O33457
-
-
-
?
p-cymene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
4-isopropylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
O33456 and O33457
-
-
-
?
styrene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
styrene oxide + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
O33456 and O33457
-
-
-
?
additional information
?
-
O33456 and O33457
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
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
-
[2Fe-2S]-center
O33456 and O33457
reductase subunit CymAb
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.4
P95461 and O84920 and O84919
NADH-cytochrome c reductase activity of subunit CymA
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
P95461 and O84920 and O84919
gel fitlration, reductase component CymA
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
P95461 and O84920 and O84919
10 min, 42% loss of activity, NADH-cytochrome c reductase activity of subunit CymA
50
P95461 and O84920 and O84919
10 min, 98% loss of activity, NADH-cytochrome c reductase activity of subunit CymA
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
70°C, 50 mM potassium phosphate buffer (pH 7.0), 60% glycerol (v/v), subunit CymA is stable for 1 month
P95461 and O84920 and O84919
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
P95461 and O84920 and O84919
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of subunits CymABM is induced by growth on p-cymene
P95461 and O84920 and O84919