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
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
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-
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reduction
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-
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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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Metabolic pathways
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Microbial metabolism in diverse environments
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Phenylalanine metabolism
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phenylethylamine degradation I
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phenylethylamine degradation II
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styrene degradation
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Styrene degradation
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phenylalanine metabolism
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SYSTEMATIC NAME
IUBMB Comments
phenylacetaldehyde:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
58943-37-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Achromobacter eurydice
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-
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Manually annotated by BRENDA team
strain S5
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-
Manually annotated by BRENDA team
Bacteria S5
strain S5
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Manually annotated by BRENDA team
strain KU1309
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Manually annotated by BRENDA team
strain KU1309
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain CA-3
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Manually annotated by BRENDA team
strain AT3
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-
Manually annotated by BRENDA team
strain AT3
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain 124X
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Manually annotated by BRENDA team
strain 124X
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
FeaB plays a major role in the formation of 4-hydroxyphenylacetate
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
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-
?
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
-
17% activity relative to phenylacetaldehyde
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-
?
heptanal + NAD+ + H2O
heptanoate + NADH
show the reaction diagram
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-
-
-
?
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
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-
?
n-butyraldehyde + NAD+ + H2O
n-butyrate + NADH
show the reaction diagram
Achromobacter eurydice
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slow reaction
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-
?
octanal + NAD+ + H2O
octanoate + NADH + H+
show the reaction diagram
phenylacetaldehyde + NAD+ + H2O
?
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
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-
-
?
phenylacetaldehyde + NADP+ + H2O
phenylacetate + NADPH + H+
show the reaction diagram
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-
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?
propionaldehyde + NAD+ + H2O
propionate + NADH
show the reaction diagram
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 + 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+
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active with NAD+ and NADP+, preference for NAD+. kcat/Km for NADP+ with propionaldehyde is 2460
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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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
Mg2+
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1 mM stimulates by 42%
Mn2+
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1 mM stimulates by 17%
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
N-ethylmaleimide
Achromobacter eurydice
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N-ethylmaleinimide
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completely inhibits in the presence of 1 mM
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
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
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pH 7.5
0.0056
Hexanal
-
pH 7.5
0.035 - 0.116
NAD+
0.22
NADP+
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pH 7.5, cosubstrate: propionaldehyde
0.00124 - 0.0116
phenylacetaldehyde
0.07
propionaldehyde
-
pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14.5
acetaldehyde
Escherichia coli
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pH 7.5
0.16
benzaldehyde
Escherichia coli
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pH 7.5
26.7
Heptanal
Escherichia coli
-
pH 7.5
21.8
Hexanal
Escherichia coli
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pH 7.5
3.5 - 20.17
NAD+
9
NADP+
Escherichia coli
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pH 7.5, cosubstrate: propionaldehyde
96.8
phenylacetaldehyde
Escherichia coli
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pH 7.5
20.8
propionaldehyde
Escherichia coli
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pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 53700, calculation from nucleotide sequence; 2 * 55000, SDS-PAGE
homotetramer
tetramer
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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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Expression in Escherichia coli, production of knock out-mutants is carried out by mutagenesis.
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