Information on EC 1.2.1.39 - phenylacetaldehyde dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.39
-
RECOMMENDED NAME
GeneOntology No.
phenylacetaldehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phenylacetaldehyde + NAD+ + H2O = phenylacetate + NADH + 2 H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
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reduction
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-phenylalanine degradation II (anaerobic)
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L-phenylalanine degradation IV (mammalian, via side chain)
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phenylethylamine degradation I
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phenylethylamine degradation II
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styrene degradation
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phenylalanine metabolism
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Phenylalanine metabolism
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Styrene degradation
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
phenylacetaldehyde:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
58943-37-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Achromobacter eurydice
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Bacteria S5
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-naphthaldehyde + NAD+ + H2O
1-naphthoate + NADH + H+
show the reaction diagram
-
24% activity relative to phenylacetaldehyde
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
show the reaction diagram
-
-
-
-
?
3-phenylpropionaldehyde + NAD+ + H2O
3-phenylpropionate + NADH + H+
show the reaction diagram
-
34% activity relative to phenylacetaldehyde
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-
?
4-hydroxyphenylacetaldehyde + NAD+ + H2O
4-hydroxyphenylacetate + NADH + H+
show the reaction diagram
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
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-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
decanal + NAD+ + H2O
decanoate + NADH + H+
show the reaction diagram
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17% activity relative to phenylacetaldehyde
-
-
?
heptanal + NAD+ + H2O
heptanoate + NADH
show the reaction diagram
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
show the reaction diagram
indoleacetaldehyde + NAD+ + H2O
indoleacetate + NADH
show the reaction diagram
Achromobacter eurydice
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slow reaction
-
-
?
n-butyraldehyde + NAD+ + H2O
n-butyrate + NADH
show the reaction diagram
Achromobacter eurydice
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slow reaction
-
-
?
octanal + NAD+ + H2O
octanoate + NADH + H+
show the reaction diagram
phenylacetaldehyde + NAD+ + H2O
?
show the reaction diagram
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + 2 H+
show the reaction diagram
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
show the reaction diagram
phenylacetaldehyde + NAD+ + H2O
phenylacetic acid + NADH + H+
show the reaction diagram
-
-
-
?
phenylacetaldehyde + NADP+ + H2O
phenylacetate + NADPH + 2 H+
show the reaction diagram
phenylacetaldehyde + NADP+ + H2O
phenylacetate + NADPH + H+
show the reaction diagram
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-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
show the reaction diagram
additional information
?
-
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
4-hydroxyphenylacetaldehyde + NAD+ + H2O
4-hydroxyphenylacetate + NADH + H+
show the reaction diagram
phenylacetaldehyde + NAD+ + H2O
?
show the reaction diagram
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + 2 H+
show the reaction diagram
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
show the reaction diagram
phenylacetaldehyde + NAD+ + H2O
phenylacetic acid + NADH + H+
show the reaction diagram
B1N7H3
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
additional information
enzyme PDH accepts both NAD+ and NADP+ as electron acceptors, but exhibits 86% of its maximal activity with NAD+ but only 5% of its maximal activity with NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
1 mM stimulates by 53%
Cs+
Achromobacter eurydice
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monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
K+
Achromobacter eurydice
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monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
Li+
Achromobacter eurydice
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monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
Na+
Achromobacter eurydice
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monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
NH4+
Achromobacter eurydice
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monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
Rb+
Achromobacter eurydice
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monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dihydroxyphenylacetaldehyde
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above 0.01 mM
4-hydroxyphenylacetaldehyde
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above 0.01 mM
8-Quinolinol
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34% inhibition in the presence of 1 mM
Ba2+
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19% inhibition in the presence of 1 mM
Cu2+
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44% inhibition in the presence of 1 mM
EDTA
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18% inhibition in the presence of 1 mM
Hg2+
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77% inhibition in the presence of 1 mM
hydrozine
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51% inhibition in the presence of 1 mM
iodoacetamide
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completely inhibits in the presence of 1 mM
iodoacetate
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18% inhibition in the presence of 1 mM
K+
Achromobacter eurydice
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above 1 M
Mn2+
inhibits and activates
N-ethylmaleimide
Achromobacter eurydice
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N-ethylmaleinimide
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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
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25% inhibition in the presence of 1 mM
Ni2+
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12% inhibition in the presence of 1 mM
p-chloromercuribenzoate
phenylacetaldehyde
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
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Zn2+
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41% inhibition in the presence of 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
3,4-dihydroxyphenylacetaldehyde
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0.004
4-hydroxyphenylacetaldehyde
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2.15
acetaldehyde
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pH 7.5
0.008
benzaldehyde
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pH 7.5
0.0066
Heptanal
-
pH 7.5
0.0056
Hexanal
-
pH 7.5
0.018 - 0.116
NAD+
0.025 - 0.22
NADP+
0.00124 - 0.0116
phenylacetaldehyde
0.07
propionaldehyde
-
pH 7.5
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14.5
acetaldehyde
-
pH 7.5
0.16
benzaldehyde
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pH 7.5
26.7
Heptanal
-
pH 7.5
21.8
Hexanal
-
pH 7.5
3.5 - 53
NAD+
9 - 63
NADP+
96.8
phenylacetaldehyde
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pH 7.5
20.8
propionaldehyde
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pH 7.5
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
NAD+
pH 8.5, 28°C
0.0025
NADP+
pH 8.5, 28°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.069
NAD+
pH 8.5, 28°C, cooperative substrate inhibition
0.067
NADP+
pH 8.5, 28°C, cooperative substrate inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.102
purified native enzyme, with cofactor NADP+, pH 8.5, 28°C
0.21
purified recombinant Strep-tagged enzyme, pH 8.5, 28°C
0.261
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cell-free extract
4.16
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15.9fold purified enzyme
19
Achromobacter eurydice
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-
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6.5
assay at, reverse reaction
8.5
assay at, forward reaction
8.9
Achromobacter eurydice
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-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53290
; calculated
53700
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2 * 53700, calculation from nucleotide sequence
54000
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x * 54000, SDS-PAGE
55000
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2 * 55000, SDS-PAGE
61000
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4 * 61000, SDS-PAGE
210700
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gel filtration
219000
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gel filtration
227000
recombinant His-tagged enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 54000, SDS-PAGE
dimer
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2 * 53700, calculation from nucleotide sequence; 2 * 55000, SDS-PAGE
homotetramer
tetramer
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-
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, sitting drop vapor diffusion method, mixing of 5-7 mg/ml protein in 10 mM Tris, pH 7.5, and 1 mM 2-mercaptoethanol, with 100-200 mM trisodium citrate, pH 8.5, and 12-16% PEG 3350, at 4°C, X-ray diffraction structure determination and analysis at 2.83 A resolution, molecular replacement using ALDH1, PDB ID 1BXS, as a starting model, model building
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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at pH 8.0, PADH retains 60% of the initial activity
690567
additional information
Achromobacter eurydice
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unstable after dilution, especially in alkaline medium
390292
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable after dilution
Achromobacter eurydice
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM Tris-HCl buffer
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by gel filtration, 15.9fold with a 0.21% yield
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native enzyme 126fold by cross-flow filtration, ultracentrifugation, and anion exchange chromatography, recombinant Strep-tagged enzyme 137fold from Escherichia coli strain DHalpha by affinity chromatography on a Strep-Tactin column
recombinant N-terminally His-tagged enzyme, NPADH, from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration to over 90% purity
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Expression in Escherichia coli, production of knock out-mutants is carried out by mutagenesis.
gene ebA4954, recombinant expression of N-terminally Strep-tagged enzyme in Escherichia coli strain DHalpha
gene styD, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His-tagged enzyme, NPADH, in Escherichia coli strain BL21(DE3)
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