BRENDA - Enzyme Database show
show all sequences of 1.14.12.25

p-Cymene pathway in Pseudomonas putida: initial reactions

DeFrank, J.; Ribbons, D.; J. Bacteriol. 129, 1356-1364 (1977)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
p-cumate + NADH + H+ + O2
Pseudomonas putida
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2,3-dihydroxy-2,3-dihydro-p-cumate + NAD+
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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Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
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Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
p-cumate + NADH + H+ + O2
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738485
Pseudomonas putida
2,3-dihydroxy-2,3-dihydro-p-cumate + NAD+
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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?
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
p-cumate + NADH + H+ + O2
Pseudomonas putida
-
2,3-dihydroxy-2,3-dihydro-p-cumate + NAD+
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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?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
p-cumate + NADH + H+ + O2
-
738485
Pseudomonas putida
2,3-dihydroxy-2,3-dihydro-p-cumate + NAD+
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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?
General Information
General Information
Commentary
Organism
physiological function
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
Pseudomonas putida
General Information (protein specific)
General Information
Commentary
Organism
physiological function
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
Pseudomonas putida
Other publictions for EC 1.14.12.25
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743615
Agullo
p-Cymene promotes its catabol ...
Paraburkholderia xenovorans
PLoS ONE
12
e0169544
2017
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738506
Eaton
p-Cumate catabolic pathway in ...
Pseudomonas putida, Pseudomonas putida DSM 6899
J. Bacteriol.
178
1351-1362
1996
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738505
Eaton
Formation of indigo and relate ...
Pseudomonas putida
J. Bacteriol.
177
6983-6988
1995
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738486
Wigmore
p-Cymene pathway in Pseudomona ...
Pseudomonas putida
J. Bacteriol.
143
816-824
1980
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738485
DeFrank
p-Cymene pathway in Pseudomona ...
Pseudomonas putida
J. Bacteriol.
129
1356-1364
1977
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