Information on EC 1.14.12.25 - p-cumate 2,3-dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.12.25
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RECOMMENDED NAME
GeneOntology No.
p-cumate 2,3-dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
p-cumate + NADH + H+ + O2 = (2R,3S)-2,3-dihydroxy-2,3-dihydro-p-cumate + NAD+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
p-cumate degradation to 2-oxopent-4-enoate
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Xylene degradation
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
4-isopropylbenzoate:oxygen 2,3-oxidoreductase
The enzyme, characterized from several Pseudomonas strains, is involved in the degradation of p-cymene and p-cumate. It comprises four components: a ferredoxin, a ferredoxin reductase, and two subunits of a catalytic component. The enzyme can also act on indole, transforming it to the water-insoluble blue dye indigo.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q51973 i,e, subunit CmtAa, Q51974 i.e. subunit CmtAb, Q51975 i.e. subunit CmtAc, Q51978 i.e. subunit CmtAd
Q51973 and Q51974 and Q51975 and Q51978
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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a mutant of Pseudomonas putida, which is unable to grow with p-cumate, accumulates 2,3-dihydroxy-4-isoproplycyclohexa-4,6-dienoate. Both hydroxyl atoms of the dihydrodiol are derived from the same molecule of 02
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
indole-2-carboxylate + NADH + H+ + O2
2,3-dihydroxy-2,3-dihydro-1H-indole-2-carboxylic acid + NAD+
show the reaction diagram
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product rearranges spontaneously forming indigo, indirubin, and isatin
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?
indole-3-carboxylate + NADH + H+ + O2
2,3-dihydroxy-2,3-dihydro-1H-indole-3-carboxylic acid + NAD+
show the reaction diagram
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?
m-toluate + NADH + H+ + O2
1,6-dihydroxy-5-methylcyclohexa-2,4-diene-1-carboxylic acid + NAD+
show the reaction diagram
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?
p-cumate + NADH + H+ + O2
(2R,3S)-2,3-dihydroxy-2,3-dihydro-p-cumate + NAD+
show the reaction diagram
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?
p-cumate + NADH + H+ + O2
2,3-dihydroxy-2,3-dihydro-p-cumate + NAD+
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
p-cumate + NADH + H+ + O2
(2R,3S)-2,3-dihydroxy-2,3-dihydro-p-cumate + NAD+
show the reaction diagram
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?
p-cumate + NADH + H+ + O2
2,3-dihydroxy-2,3-dihydro-p-cumate + NAD+
show the reaction diagram
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the substrate for the ring cleavage of 2,3-dihydroxy-p-cumate is formed from p-cumate in two reactions via a dihydrodiol intermediate (2,3-dihydroxy-4-isopropylcyclohexa-4,6-dienoate). Both hydroxyl atoms of the dihydrodiol are derived from the same molecule of 02
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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enrichment of mutants defective in the utilization of p-cymene as sole carbon source by incubation of cells in minimal growth media containing p-cymene, p-chlorotoluene, p-bromotoluene, alpha-chloro-p-xylene, or p-iodobenzoate. Several classes of mutants can be isolated, p-cymene hydroxylase and p-cumate 2,3-dioxygenase are likely to be multicomponent enzymes