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1-naphthaldehyde + NAD+ + H2O
1-naphthoate + NADH + H+
-
24% activity relative to phenylacetaldehyde
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
-
-
-
?
3-phenylpropionaldehyde + NAD+ + H2O
3-phenylpropionate + NADH + H+
-
34% activity relative to phenylacetaldehyde
-
?
4-hydroxyphenylacetaldehyde + NAD+ + H2O
4-hydroxyphenylacetate + NADH + H+
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
decanal + NAD+ + H2O
decanoate + NADH + H+
-
17% activity relative to phenylacetaldehyde
-
?
heptanal + NAD+ + H2O
heptanoate + NADH
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
indoleacetaldehyde + NAD+ + H2O
indoleacetate + NADH
Achromobacter eurydice
-
slow reaction
-
?
n-butyraldehyde + NAD+ + H2O
n-butyrate + NADH
Achromobacter eurydice
-
slow reaction
-
?
octanal + NAD+ + H2O
octanoate + NADH + H+
phenylacetaldehyde + NAD+ + H2O
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + 2 H+
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
phenylacetaldehyde + NAD+ + H2O
phenylacetic acid + NADH + H+
-
-
?
phenylacetaldehyde + NADP+ + H2O
phenylacetate + NADPH + 2 H+
phenylacetaldehyde + NADP+ + H2O
phenylacetate + NADPH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
additional information
?
-
4-hydroxyphenylacetaldehyde + NAD+ + H2O

4-hydroxyphenylacetate + NADH + H+
-
-
-
?
4-hydroxyphenylacetaldehyde + NAD+ + H2O
4-hydroxyphenylacetate + NADH + H+
-
-
?
benzaldehyde + NAD+ + H2O

benzoate + NADH + H+
-
54% activity relative to phenylacetaldehyde
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
54% activity relative to phenylacetaldehyde
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
?
hexanal + NAD+ + H2O

hexanoate + NADH + H+
-
21% activity relative to phenylacetaldehyde
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
21% activity relative to phenylacetaldehyde
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
?
octanal + NAD+ + H2O

octanoate + NADH + H+
-
31% activity relative to phenylacetaldehyde
-
?
octanal + NAD+ + H2O
octanoate + NADH + H+
-
31% activity relative to phenylacetaldehyde
-
?
phenylacetaldehyde + NAD+ + H2O

?
Achromobacter eurydice
-
inducible enzyme appears when cells are grown on L-phenylalanine or on L-tryptophan as sole source of carbon
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
involved in degradation of styrene
-
?
phenylacetaldehyde + NAD+ + H2O
?
Bacteria S5
-
involved in degradation of styrene
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
inducible enzyme of 2-phenylethylamine catabolism
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
a positive regulatory protein required for expression of phenylacetaldehyde dehydrogenase is located next to the PAD gene
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in the catabolism of 2-phenylethylamine
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
involved in DL-phenylacrylic acid and phenylacetic acid catabolism
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in degradation of styrene. Low constitutive levels of NAD+-dependent phenylacetaldehyde dehydrogenase
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in degradation of styrene. Low constitutive levels of NAD+-dependent phenylacetaldehyde dehydrogenase
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in metabolism of atropine
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in metabolism of atropine
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in the anaerobic metabolism of L-phenylalanine
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
inolved in degradation of styrene oxide and 2-phenylethanol
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
inolved in degradation of styrene oxide and 2-phenylethanol
-
?
phenylacetaldehyde + NAD+ + H2O

phenylacetate + NADH + 2 H+
-
-
r
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + 2 H+
-
-
r
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + 2 H+
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + 2 H+
-
-
?
phenylacetaldehyde + NAD+ + H2O

phenylacetate + NADH + H+
Achromobacter eurydice
-
highly specific for phenylacetaldehyde, NADP+ is about 1% as active as NAD+
-
ir
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
Bacteria S5
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
best substrate
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
best substrate
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
the enzyme participates in metabolism of phenylalanine
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
rate-limiting step is the hydride transfer
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NADP+ + H2O

phenylacetate + NADPH + 2 H+
-
-
r
phenylacetaldehyde + NADP+ + H2O
phenylacetate + NADPH + 2 H+
-
-
r
propionaldehyde + NAD+ + H2O

propionate + NADH
Achromobacter eurydice
-
slow reaction
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
-
-
-
?
additional information

?
-
enzyme is highly specific for phenylacetaldehyde, has cooperative kinetics toward the substrate, and shows considerable substrate inhibition. No activity with benzaldehyde and indole-3-carbaldehyde, substrate specificity, overview
-
?
additional information
?
-
-
enzyme is highly specific for phenylacetaldehyde, has cooperative kinetics toward the substrate, and shows considerable substrate inhibition. No activity with benzaldehyde and indole-3-carbaldehyde, substrate specificity, overview
-
?
additional information
?
-
enzyme is highly specific for phenylacetaldehyde, has cooperative kinetics toward the substrate, and shows considerable substrate inhibition. No activity with benzaldehyde and indole-3-carbaldehyde, substrate specificity, overview
-
?
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4-hydroxyphenylacetaldehyde + NAD+ + H2O
4-hydroxyphenylacetate + NADH + H+
phenylacetaldehyde + NAD+ + H2O
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + 2 H+
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
phenylacetaldehyde + NAD+ + H2O
phenylacetic acid + NADH + H+
-
-
-
?
4-hydroxyphenylacetaldehyde + NAD+ + H2O

4-hydroxyphenylacetate + NADH + H+
-
-
-
-
?
4-hydroxyphenylacetaldehyde + NAD+ + H2O
4-hydroxyphenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O

?
Achromobacter eurydice
-
inducible enzyme appears when cells are grown on L-phenylalanine or on L-tryptophan as sole source of carbon
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
involved in degradation of styrene
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
Bacteria S5
-
involved in degradation of styrene
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
inducible enzyme of 2-phenylethylamine catabolism
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
a positive regulatory protein required for expression of phenylacetaldehyde dehydrogenase is located next to the PAD gene
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in the catabolism of 2-phenylethylamine
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
involved in DL-phenylacrylic acid and phenylacetic acid catabolism
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in degradation of styrene. Low constitutive levels of NAD+-dependent phenylacetaldehyde dehydrogenase
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in degradation of styrene. Low constitutive levels of NAD+-dependent phenylacetaldehyde dehydrogenase
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in metabolism of atropine
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in metabolism of atropine
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in the anaerobic metabolism of L-phenylalanine
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
inolved in degradation of styrene oxide and 2-phenylethanol
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
-
inolved in degradation of styrene oxide and 2-phenylethanol
-
-
?
phenylacetaldehyde + NAD+ + H2O

phenylacetate + NADH + 2 H+
-
-
-
r
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + 2 H+
-
-
-
r
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + 2 H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + 2 H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O

phenylacetate + NADH + H+
-
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
the enzyme participates in metabolism of phenylalanine
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
?
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Ca2+
-
1 mM stimulates by 53%
Cs+
Achromobacter eurydice
-
monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
K+
Achromobacter eurydice
-
monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
Li+
Achromobacter eurydice
-
monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
Na+
Achromobacter eurydice
-
monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
NH4+
Achromobacter eurydice
-
monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
Rb+
Achromobacter eurydice
-
monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
Mg2+

-
1 mM stimulates by 42%
Mg2+
the enzyme includes both an activating and inhibitory metal binding site in the catalytic mechanism of NPADH. The activating divalent metal binding site may be best described as the direct interaction of the metal ion with the pyrophosphate linkage joining the nicotinamide mononucleotide and adenosine mononucleotide components of the pyridine nucleotide structure. A second mononuclear metal binding site, occupied by Mg2+ is detected in this structure. The Mg2+ in this site assumes a roughly octahedral geometry and is coordinated by the backbone carbonyl oxygens of Val40, Asp109, Glu196, and Val345, as well as a monodentate interaction with a carboxylate oxygen of Asp109. The sixth ligand is a crystallographically resolved water molecule
Mn2+

-
1 mM stimulates by 17%
Mn2+
inhibits and activates
additional information

Achromobacter eurydice
-
divalent cations (Mg2+, Ca2+) are inactive
additional information
-
is not stimulated by 10 mM KCl
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3,4-dihydroxyphenylacetaldehyde
-
above 0.01 mM
4-hydroxyphenylacetaldehyde
-
above 0.01 mM
8-Quinolinol
-
34% inhibition in the presence of 1 mM
Ba2+
-
19% inhibition in the presence of 1 mM
Cu2+
-
44% inhibition in the presence of 1 mM
EDTA
-
18% inhibition in the presence of 1 mM
Hg2+
-
77% inhibition in the presence of 1 mM
hydrozine
-
51% inhibition in the presence of 1 mM
iodoacetamide
-
completely inhibits in the presence of 1 mM
iodoacetate
-
18% inhibition in the presence of 1 mM
K+
Achromobacter eurydice
-
above 1 M
Mn2+
inhibits and activates
N-ethylmaleimide
Achromobacter eurydice
-
-
N-ethylmaleinimide
-
completely inhibits in the presence of 1 mM
NADH
product inhibition, competitive binding of NAD+. For many aldehyde dehydrogenases, NADH binds competitively with NAD+ and forms a nonproductive dead-end complex during catalysis. In the absence of styrene monooxygenase reductase, which regenerates NAD+ from NADH in the first step of styrene catabolism, NPADH is inhibited by a ternary complex involving NADH, product, and phenylacetaldehyde, substrate
NADP+
cooperative substrate inhibition
NaN3
-
25% inhibition in the presence of 1 mM
Ni2+
-
12% inhibition in the presence of 1 mM
PMSF
inactivates NPADH, presumably by modifying the active site cysteine
Pyridine nucleotides
titrations of NPADH with NADþ and NADH are evaluated to estimate the binding affinities of the oxidized and reduced pyridine nucleotides under equilibrium conditions. Mg2+ is included in these studies
-
Zn2+
-
41% inhibition in the presence of 1 mM
Mg2+

at high concentrations
Mg2+
inhibits and activates
NAD+

cooperative substrate inhibition
NAD+
substrate inhibition, competitive binding of NADH
p-chloromercuribenzoate

Achromobacter eurydice
-
-
p-chloromercuribenzoate
-
completely inhibits in the presence of 1 mM
phenylacetaldehyde

the enzyme is highly specific for phenylacetaldehyde, has cooperative kinetics toward the substrate, and shows considerable substrate inhibition
phenylacetaldehyde
-
high concentration (0.1 mM) inhibits
phenylacetaldehyde
-
above 0.01 mM
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malfunction

deletion of feaB gene results in increased desired aromatic compounds with decreased by-products. 2-Phenylethanol is not degraded by a feaB-deficient strain
malfunction
-
disruption of the endogenous phenylacetaldehyde dehydrogenase gene shuts off 4-hydroxyphenylacetate production and improves the production of tyrosol as a sole product
metabolism

-
FeaB plays a major role in the formation of 4-hydroxyphenylacetate
metabolism
the enzyme catalyzes a step in the styrene catabolic pathway of Pseudomonas putida
metabolism
two distinct enzymes are involved in the oxidation of phenylacetaldehyde to phenylacetate, an aldehyde:ferredoxin oxidoreductase (AOR) and a phenylacetaldehyde dehydrogenase (PDH). PDH is the primary enzyme during anaerobic phenylalanine degradation, whereas AOR is not essential for the metabolic pathway and exhibits probably a function as a detoxifying enzyme if high aldehyde concentrations accumulate in the cytoplasm, which would lead to substrate inhibition of PDH
metabolism
-
the enzyme catalyzes a step in the styrene catabolic pathway of Pseudomonas putida
metabolism
-
two distinct enzymes are involved in the oxidation of phenylacetaldehyde to phenylacetate, an aldehyde:ferredoxin oxidoreductase (AOR) and a phenylacetaldehyde dehydrogenase (PDH). PDH is the primary enzyme during anaerobic phenylalanine degradation, whereas AOR is not essential for the metabolic pathway and exhibits probably a function as a detoxifying enzyme if high aldehyde concentrations accumulate in the cytoplasm, which would lead to substrate inhibition of PDH
physiological function

phenylacetaldehyde dehydrogenase catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid in the styrene catabolic and detoxification pathway of Pseudomonas putida strain S12
physiological function
-
phenylacetaldehyde dehydrogenase catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid in the styrene catabolic and detoxification pathway of Pseudomonas putida strain S12
additional information

substrate channel and active site structure, overview. A majority of conserved residues in NPADH localize to the active site and NAD+-binding pocket. At the interface between the two pockets are the catalytic Cys 301 and Glu 267 residues, which serve as the general nucleophile and general base for the reaction, respectively
additional information
-
substrate channel and active site structure, overview. A majority of conserved residues in NPADH localize to the active site and NAD+-binding pocket. At the interface between the two pockets are the catalytic Cys 301 and Glu 267 residues, which serve as the general nucleophile and general base for the reaction, respectively
additional information
-
substrate channel and active site structure, overview. A majority of conserved residues in NPADH localize to the active site and NAD+-binding pocket. At the interface between the two pockets are the catalytic Cys 301 and Glu 267 residues, which serve as the general nucleophile and general base for the reaction, respectively
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dimer

-
2 * 55000, SDS-PAGE
dimer
-
2 * 53700, calculation from nucleotide sequence
homotetramer

4 * 53500, recombinant Strep-tagged enzyme, SDS-PAGE
homotetramer
-
4 * 53500, recombinant Strep-tagged enzyme, SDS-PAGE
homotetramer
-
4 * 61000, SDS-PAGE
homotetramer
-
4 * 61000, SDS-PAGE
homotetramer
4 * 55000, recombinant His-tagged enzyme, SDS-PAGE
homotetramer
-
4 * 55000, recombinant His-tagged enzyme, SDS-PAGE
additional information

the oligomerization domains of all four subunits form the core of PADH and are responsible not only for the effective dimerization observed within the homotetramer, but also for the association of these dimers to form the tetramer. Each 496 amino acid PADH subunit consists of three domains: an N-terminal NADþ-binding domain (residues 1-130 and 159-269), a catalytic domain (residues 270-471), and an oligomerization domain (131-158 and 472-496). The enzyme has a unique set of intersubunit interactions and active site tunnel for substrate entrance. Each oligomerization domain of NPADH contains a six-residue insertion that extends this loop over the substrate entrance tunnel of a neighboring subunit, thereby obstructing the active site of the adjacent subunit. This feature might be an important factor in the homotropic activation and product inhibition mechanisms. The substrate channel of NPADH is narrower and lined with more aromatic residues, which include Phe170, Phe295, Phe466, and Trp177, suggesting a means for enhancing substrate specificity
additional information
-
the oligomerization domains of all four subunits form the core of PADH and are responsible not only for the effective dimerization observed within the homotetramer, but also for the association of these dimers to form the tetramer. Each 496 amino acid PADH subunit consists of three domains: an N-terminal NADþ-binding domain (residues 1-130 and 159-269), a catalytic domain (residues 270-471), and an oligomerization domain (131-158 and 472-496). The enzyme has a unique set of intersubunit interactions and active site tunnel for substrate entrance. Each oligomerization domain of NPADH contains a six-residue insertion that extends this loop over the substrate entrance tunnel of a neighboring subunit, thereby obstructing the active site of the adjacent subunit. This feature might be an important factor in the homotropic activation and product inhibition mechanisms. The substrate channel of NPADH is narrower and lined with more aromatic residues, which include Phe170, Phe295, Phe466, and Trp177, suggesting a means for enhancing substrate specificity
additional information
-
the oligomerization domains of all four subunits form the core of PADH and are responsible not only for the effective dimerization observed within the homotetramer, but also for the association of these dimers to form the tetramer. Each 496 amino acid PADH subunit consists of three domains: an N-terminal NADþ-binding domain (residues 1-130 and 159-269), a catalytic domain (residues 270-471), and an oligomerization domain (131-158 and 472-496). The enzyme has a unique set of intersubunit interactions and active site tunnel for substrate entrance. Each oligomerization domain of NPADH contains a six-residue insertion that extends this loop over the substrate entrance tunnel of a neighboring subunit, thereby obstructing the active site of the adjacent subunit. This feature might be an important factor in the homotropic activation and product inhibition mechanisms. The substrate channel of NPADH is narrower and lined with more aromatic residues, which include Phe170, Phe295, Phe466, and Trp177, suggesting a means for enhancing substrate specificity
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Schneider, S.; Mohamed, M.E.S.; Fuchs, G.
Anaerobic metabolism of L-phenylalanine via benzoyl-CoA in the denitrifying bacterium Thauera aromatica
Arch. Microbiol.
168
310-320
1997
Thauera aromatica
brenda
Van den Tweel, W.J.J.; Smits, J.P.; de Bont, J.A.M.
Catabolism of DL-alpha-phenylhydracrylic, phenylacetic and 3- and 4-hydroxyphenylacetic acid via homogentisic acid in a Flavobacterium sp.
Arch. Microbiol.
149
207-213
1988
Flavobacterium sp.
-
brenda
Fujioka, M.; Morino, Y.; Wada, H.
Metabolism of phenylalanine (Achromobacter eurydice)
Methods Enzymol.
17A
585-596
1970
Achromobacter eurydice
-
brenda
Hartmans, S.; van der Werf, M.J.; de Bont, J.A.M.
Bacterial degradation of styrene involving a novel flavin adenine dinucleotide-dependent styrene monooxygenase
Appl. Environ. Microbiol.
56
1347-1351
1990
Bacteria, Bacteria S5
brenda
Hartmans, S.; Smits, J.P.; van der Werf, M.J.; Volkering, F.; de Bont, J.A.M.
Metabolism of styrene oxide and 2-phenylethanol in the styrene-degrading Xanthobacter strain 124X
Appl. Environ. Microbiol.
55
2850-2855
1989
Xanthobacter sp., Xanthobacter sp. 124X
brenda
Parrott, S.; Jones, S.; Cooper, R.A.
2-Phenylethylamine catabolism by Escherichia coli K12
J. Gen. Microbiol.
133
347-351
1987
Escherichia coli
brenda
Long, M.T.; Bartholomew, B.A.; Smith, M.J.; Trudgill, P.W.; Hopper, D.J.
Enzymology of oxidation of tropic acid to phenylacetic acid in metabolism of atropine by Pseudomonas sp. strain AT3
J. Bacteriol.
179
1044-1050
1997
Pseudomonas sp., Pseudomonas sp. AT3
brenda
Ferrandez, A.; Prieto, M.A.; Garcia, J.L.; Diaz, E.
Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli
FEBS Lett.
406
23-27
1997
Escherichia coli
brenda
Hanlon, S.P.; Hill, T.K.; Flavell, M.A.; Stringfellow, J.M.; Cooper, R.A.
2-Phenylethylamine catabolism by Escherichia coli K-12: gene organization and expression
Microbiology
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Escherichia coli
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O'Connor, K.; Duetz, W.; Wind, B.; Dobson, A.D.W.
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Appl. Environ. Microbiol.
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Pseudomonas putida, Pseudomonas putida CA-3
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Rodriguez-Zavala, J.S.; Allali-Hassani, A.; Weiner, H.
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Escherichia coli
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Arias, S.; Olivera, E.R.; Arcos, M.; Naharro, G.; Luengo, J.M.
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
Environ. Microbiol.
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Pseudomonas putida, Pseudomonas putida (B1N7H3)
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Hirano, J.; Miyamoto, K.; Ohta, H.
Purification and characterization of aldehyde dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU1309
Appl. Microbiol. Biotechnol.
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Brevibacterium sp., Brevibacterium sp. KU1309
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Koma, D.; Yamanaka, H.; Moriyoshi, K.; Ohmoto, T.; Sakai, K.
Production of aromatic compounds by metabolically engineered Escherichia coli with an expanded shikimate pathway
Appl. Environ. Microbiol.
78
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Escherichia coli (P80668), Escherichia coli
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Satoh, Y.; Tajima, K.; Munekata, M.; Keasling, J.D.; Lee, T.S.
Engineering of a tyrosol-producing pathway, utilizing simple sugar and the central metabolic tyrosine, in Escherichia coli
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Escherichia coli
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Crabo, A.G.; Singh, B.; Nguyen, T.; Emami, S.; Gassner, G.T.; Sazinsky, M.H.
Structure and biochemistry of phenylacetaldehyde dehydrogenase from the Pseudomonas putida S12 styrene catabolic pathway
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Pseudomonas putida (V4GH04), Pseudomonas putida, Pseudomonas putida S12 (V4GH04), Pseudomonas putida S12
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Debnar-Daumler, C.; Seubert, A.; Schmitt, G.; Heider, J.
Simultaneous involvement of a tungsten-containing aldehyde ferredoxin oxidoreductase and a phenylacetaldehyde dehydrogenase in anaerobic phenylalanine metabolism
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Aromatoleum aromaticum (Q5P171), Aromatoleum aromaticum, Aromatoleum aromaticum EbN1 (Q5P171)
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