BRENDA - Enzyme Database
show all sequences of 1.2.1.39

Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli

Ferrandez, A.; Prieto, M.A.; Garcia, J.L.; Diaz, E.; FEBS Lett. 406, 23-27 (1997)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Escherichia coli
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53700
-
2 * 53700, calculation from nucleotide sequence
Escherichia coli
55000
-
2 * 55000, SDS-PAGE
Escherichia coli
115000
-
-
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phenylacetaldehyde + NAD+ + H2O
Escherichia coli
enzyme is involved in the catabolism of 2-phenylethylamine
?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phenylacetaldehyde + NAD+ + H2O
-
390299
Escherichia coli
phenylacetate + NADH + H+
-
390299
Escherichia coli
?
phenylacetaldehyde + NAD+ + H2O
enzyme is involved in the catabolism of 2-phenylethylamine
390299
Escherichia coli
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 53700, calculation from nucleotide sequence; 2 * 55000, SDS-PAGE
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53700
-
2 * 53700, calculation from nucleotide sequence
Escherichia coli
55000
-
2 * 55000, SDS-PAGE
Escherichia coli
115000
-
-
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phenylacetaldehyde + NAD+ + H2O
Escherichia coli
enzyme is involved in the catabolism of 2-phenylethylamine
?
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phenylacetaldehyde + NAD+ + H2O
-
390299
Escherichia coli
phenylacetate + NADH + H+
-
390299
Escherichia coli
?
phenylacetaldehyde + NAD+ + H2O
enzyme is involved in the catabolism of 2-phenylethylamine
390299
Escherichia coli
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 53700, calculation from nucleotide sequence; 2 * 55000, SDS-PAGE
Escherichia coli
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)
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1
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2
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1
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2
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1
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2
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6
1
1
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2
2
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1
1
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2
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724020
Koma
Production of aromatic compoun ...
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Appl. Environ. Microbiol.
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2
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1
1
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725180
Satoh
Engineering of a tyrosol-produ ...
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J. Agric. Food Chem.
60
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2012
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1
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2
2
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686425
Arias
Genetic analyses and molecular ...
Pseudomonas putida
Environ. Microbiol.
10
413-432
2008
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-
1
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1
2
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5
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1
1
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1
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1
2
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2
2
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1
1
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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
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-
1
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-
2
1
13
1
1
-
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-
1
1
1
1
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-
1
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14
-
2
1
4
2
2
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1
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2
1
13
1
1
-
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1
1
1
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670833
Rodriguez-Zavala
Characterization of E. coli te ...
Escherichia coli
Protein Sci.
15
1387-1396
2006
-
-
-
-
-
-
-
8
-
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1
1
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1
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8
1
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9
-
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-
2
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-
2
-
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-
-
-
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8
-
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1
1
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-
-
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-
8
1
-
-
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9
-
-
-
-
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-
718
Schneider
Anaerobic metabolism of L-phen ...
Thauera aromatica
Arch. Microbiol.
168
310-320
1997
-
-
-
-
-
-
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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
-
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
-
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-
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-
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
-
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-
1
-
5
1
-
-
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1
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1
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3
-
3
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-
1
2
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1
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1
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390301
O'Connor
The effect of nutrient limitat ...
Pseudomonas putida, Pseudomonas putida CA-3
Appl. Environ. Microbiol.
62
3594-3599
1996
-
-
-
-
-
-
-
-
-
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-
2
-
9
-
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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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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
-
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-
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-
-
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-
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-
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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-
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1
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2
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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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3
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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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5
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1
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1
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