BRENDA - Enzyme Database show
show all sequences of 1.2.1.39

Genetic analyses and molecular characterization of the pathways involved in the conversion of 2-phenylethylamine and 2-phenylethanol into phenylacetic acid in Pseudomonas putida U

Arias, S.; Olivera, E.R.; Arcos, M.; Naharro, G.; Luengo, J.M.; Environ. Microbiol. 10, 413-432 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
Expression in Escherichia coli, production of knock out-mutants is carried out by mutagenesis.
Pseudomonas putida
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53290
-
; calculated
Pseudomonas putida
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phenylacetaldehyde + NAD+ + H2O
Pseudomonas putida
-
phenylacetate + NADH + H+
-
-
?
phenylacetaldehyde + NAD+ + H2O
Pseudomonas putida
-
phenylacetic acid + NADH + H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
B1N7H3
U strain, although enzymatic activity decreases in knock-out mutants good phenylacetaldehyde dehydrogenase acivity is present in the bacterium, PeaF and PeaG are suggested to replace PeaE
-
Pseudomonas putida
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell culture
-
Pseudomonas putida
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
Analysis of phenylacetaldehyde dehydrogenase activity in cell-free extracts reveals that although enzymatic activity decreases in the peaE knocked-out mutant (20% with respect to the control), good phenylacetaldehyde dehydrogenase activity is present. Another aldehyde dehydrogenase(s) exist(s) that could replace the role played by PeaE
Pseudomonas putida
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phenylacetaldehyde + NAD+ + H2O
-
686425
Pseudomonas putida
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
-
686425
Pseudomonas putida
phenylacetic acid + NADH + H+
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
;
Pseudomonas putida
Cloned(Commentary) (protein specific)
Commentary
Organism
Expression in Escherichia coli, production of knock out-mutants is carried out by mutagenesis.
Pseudomonas putida
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Pseudomonas putida
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53290
-
-
Pseudomonas putida
53290
-
calculated
Pseudomonas putida
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phenylacetaldehyde + NAD+ + H2O
Pseudomonas putida
-
phenylacetate + NADH + H+
-
-
?
phenylacetaldehyde + NAD+ + H2O
Pseudomonas putida
-
phenylacetic acid + NADH + H+
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell culture
-
Pseudomonas putida
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
Analysis of phenylacetaldehyde dehydrogenase activity in cell-free extracts reveals that although enzymatic activity decreases in the peaE knocked-out mutant (20% with respect to the control), good phenylacetaldehyde dehydrogenase activity is present. Another aldehyde dehydrogenase(s) exist(s) that could replace the role played by PeaE
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phenylacetaldehyde + NAD+ + H2O
-
686425
Pseudomonas putida
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
-
686425
Pseudomonas putida
phenylacetic acid + NADH + H+
-
-
-
?
Other publictions for EC 1.2.1.39
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)
741787
Crabo
Structure and biochemistry of ...
Pseudomonas putida, Pseudomonas putida S12
Arch. Biochem. Biophys.
616
47-58
2017
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-
1
1
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6
2
-
2
1
2
-
6
-
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1
1
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2
2
1
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1
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1
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1
1
1
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6
-
2
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2
1
2
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-
1
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-
2
2
1
-
-
-
1
-
-
-
-
3
3
-
-
-
742786
Debnar-Daumler
Simultaneous involvement of a ...
Aromatoleum aromaticum, Aromatoleum aromaticum EbN1
J. Bacteriol.
196
483-492
2014
-
-
1
-
-
-
4
3
-
-
-
2
-
4
-
-
1
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-
-
2
-
6
1
1
-
-
2
2
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-
5
2
-
-
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-
1
5
-
-
-
-
4
2
3
-
-
-
2
-
-
-
1
-
-
2
-
6
1
1
-
-
2
2
-
-
-
-
1
1
-
2
2
724020
Koma
Production of aromatic compoun ...
Escherichia coli
Appl. Environ. Microbiol.
78
6203-6216
2012
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2
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5
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2
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-
2
-
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-
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-
-
-
-
-
-
1
1
-
-
-
725180
Satoh
Engineering of a tyrosol-produ ...
Escherichia coli
J. Agric. Food Chem.
60
979-984
2012
-
-
-
-
-
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1
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2
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1
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1
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1
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1
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-
1
-
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-
-
-
-
-
-
-
-
2
2
-
-
-
686425
Arias
Genetic analyses and molecular ...
Pseudomonas putida
Environ. Microbiol.
10
413-432
2008
-
-
1
-
-
-
-
-
-
-
1
2
-
5
-
-
-
-
-
1
1
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2
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-
1
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1
2
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-
2
2
-
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-
-
1
1
-
2
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
690567
Hirano
Purification and characterizat ...
Brevibacterium sp., Brevibacterium sp. KU1309
Appl. Microbiol. Biotechnol.
76
357-363
2007
-
-
-
-
-
-
14
2
1
4
2
2
-
5
-
-
1
-
-
-
2
1
13
1
1
-
-
-
1
1
1
1
-
-
-
-
-
-
1
-
-
-
-
14
-
2
1
4
2
2
-
-
-
1
-
-
2
1
13
1
1
-
-
-
1
1
1
-
-
-
-
-
-
-
670833
Rodriguez-Zavala
Characterization of E. coli te ...
Escherichia coli
Protein Sci.
15
1387-1396
2006
-
-
-
-
-
-
-
8
-
-
1
1
-
1
-
-
-
-
-
-
-
-
8
1
-
-
-
9
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
8
-
-
1
1
-
-
-
-
-
-
-
-
8
1
-
-
-
9
-
-
-
-
-
-
-
-
-
-
718
Schneider
Anaerobic metabolism of L-phen ...
Thauera aromatica
Arch. Microbiol.
168
310-320
1997
-
-
-
-
-
-
-
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-
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-
1
-
4
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2
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-
1
-
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1
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-
1
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-
2
-
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-
-
-
-
-
-
-
-
-
-
-
-
390298
Long
Enzymology of oxidation of tro ...
Pseudomonas sp., Pseudomonas sp. AT3
J. Bacteriol.
179
1044-1050
1997
-
-
-
-
-
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2
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6
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4
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1
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1
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2
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-
4
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390299
Ferrandez
Molecular characterization of ...
Escherichia coli
FEBS Lett.
406
23-27
1997
-
-
1
-
-
-
-
-
1
-
3
1
-
2
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2
1
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1
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1
1
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1
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3
1
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-
2
1
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-
390300
Hanlon
2-Phenylethylamine catabolism ...
Escherichia coli
Microbiology
143
513-518
1997
-
-
-
-
-
-
3
3
-
-
1
2
-
3
-
-
1
-
-
-
1
-
5
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
3
-
3
-
-
1
2
-
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-
1
-
-
1
-
5
1
-
-
-
-
-
-
-
-
-
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-
-
-
390301
O'Connor
The effect of nutrient limitat ...
Pseudomonas putida, Pseudomonas putida CA-3
Appl. Environ. Microbiol.
62
3594-3599
1996
-
-
-
-
-
-
-
-
-
-
-
2
-
9
-
-
-
-
-
-
-
-
4
-
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-
-
-
-
-
1
-
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-
1
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-
2
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-
4
-
-
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-
-
-
-
-
-
-
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-
-
-
-
390293
Hartmans
Bacterial degradation of styre ...
Bacteria, Bacteria S5
Appl. Environ. Microbiol.
56
1347-1351
1990
-
-
-
-
-
-
-
-
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-
2
-
5
-
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4
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1
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1
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2
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-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390294
Hartmans
Metabolism of styrene oxide an ...
Xanthobacter sp. 124X, Xanthobacter sp.
Appl. Environ. Microbiol.
55
2850-2855
1989
-
-
-
-
-
-
-
-
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2
-
2
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4
-
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-
1
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1
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2
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4
-
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-
7426
Van den Tweel
-
Catabolism of DL-alpha-phenylh ...
Flavobacterium sp.
Arch. Microbiol.
149
207-213
1988
-
-
-
-
-
-
-
-
-
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-
1
-
1
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2
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1
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1
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1
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2
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390296
Parrott
2-Phenylethylamine catabolism ...
Escherichia coli
J. Gen. Microbiol.
133
347-351
1987
-
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2
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1
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1
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1
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2
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-
390292
Fujioka
-
Metabolism of phenylalanine (A ...
Achromobacter eurydice
Methods Enzymol.
17A
585-596
1970
-
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1
3
1
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7
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1
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1
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1
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1
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5
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1
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1
1
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1
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1
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7
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1
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5
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1
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1
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