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Enzyme Nomenclature
Information on EC 1.2.1.39 - phenylacetaldehyde dehydrogenase
for references in articles please use BRENDA:EC1.2.1.39
Word Map on EC 1.2.1.39
- 1.2.1.39
-
phenylacetic
- phenylpyruvate
-
nad+-dependent
- 2-phenylethylamine
- 2-phenylethanol
-
denitrifying
- aromaticum
-
dinucleotide-dependent
- 4-hydroxyphenylacetaldehyde
-
homotetrameric
-
tungsten-dependent
- tungstate
- 4-hydroxyphenylacetate
- phenylacetyl-coa
- tyrosol
-
betaproteobacterium
-
aromatoleum
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.2.1.39
-
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RECOMMENDED NAME
GeneOntology No.
phenylacetaldehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phenylacetaldehyde + NAD+ + H2O = phenylacetate + NADH + 2 H+
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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-
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reduction
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-
-
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oxidation
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
phenylacetaldehyde:NAD+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
58943-37-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
FeaB plays a major role in the formation of 4-hydroxyphenylacetate
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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-naphthaldehyde + NAD+ + H2O
1-naphthoate + NADH + H+
-
24% activity relative to phenylacetaldehyde
-
-
?
3-phenylpropionaldehyde + NAD+ + H2O
3-phenylpropionate + NADH + H+
-
34% activity relative to phenylacetaldehyde
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + H+
-
17% activity relative to phenylacetaldehyde
-
-
?
indoleacetaldehyde + NAD+ + H2O
indoleacetate + NADH
Achromobacter eurydice
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slow reaction
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetic acid + NADH + H+
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
-
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
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-
-
-
?
4-hydroxyphenylacetaldehyde + NAD+ + H2O
4-hydroxyphenylacetate + NADH + H+
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-
-
-
?
4-hydroxyphenylacetaldehyde + NAD+ + H2O
4-hydroxyphenylacetate + NADH + H+
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-
-
?
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+
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54% activity relative to phenylacetaldehyde
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
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21% activity relative to phenylacetaldehyde
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
21% activity relative to phenylacetaldehyde
-
-
?
octanal + NAD+ + H2O
octanoate + NADH + H+
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31% activity relative to phenylacetaldehyde
-
-
?
octanal + NAD+ + H2O
octanoate + NADH + H+
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31% activity relative to phenylacetaldehyde
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
Achromobacter eurydice
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inducible enzyme appears when cells are grown on L-phenylalanine or on L-tryptophan as sole source of carbon
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-
?
phenylacetaldehyde + NAD+ + H2O
?
-
inducible enzyme of 2-phenylethylamine catabolism
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-
?
phenylacetaldehyde + NAD+ + H2O
?
-
a positive regulatory protein required for expression of phenylacetaldehyde dehydrogenase is located next to the PAD gene
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-
?
phenylacetaldehyde + NAD+ + H2O
?
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enzyme is involved in the catabolism of 2-phenylethylamine
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-
?
phenylacetaldehyde + NAD+ + H2O
?
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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
?
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involved in DL-phenylacrylic acid and phenylacetic acid catabolism
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-
?
phenylacetaldehyde + NAD+ + H2O
?
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enzyme is involved in degradation of styrene. Low constitutive levels of NAD+-dependent phenylacetaldehyde dehydrogenase
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-
?
phenylacetaldehyde + NAD+ + H2O
?
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enzyme is involved in degradation of styrene. Low constitutive levels of NAD+-dependent phenylacetaldehyde dehydrogenase
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-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in metabolism of atropine
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-
?
phenylacetaldehyde + NAD+ + H2O
?
-
enzyme is involved in metabolism of atropine
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-
?
phenylacetaldehyde + NAD+ + H2O
?
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enzyme is involved in the anaerobic metabolism of L-phenylalanine
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-
?
phenylacetaldehyde + NAD+ + H2O
?
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inolved in degradation of styrene oxide and 2-phenylethanol
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-
?
phenylacetaldehyde + NAD+ + H2O
?
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inolved in degradation of styrene oxide and 2-phenylethanol
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-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
Achromobacter eurydice
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highly specific for phenylacetaldehyde, NADP+ is about 1% as active as NAD+
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ir
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
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best substrate
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-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
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-
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-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
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best substrate
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
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the enzyme participates in metabolism of phenylalanine
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
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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+
-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phenylacetaldehyde + NAD+ + H2O
phenylacetic acid + NADH + H+
B1N7H3
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-
-
?
4-hydroxyphenylacetaldehyde + NAD+ + H2O
4-hydroxyphenylacetate + NADH + H+
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-
-
-
?
4-hydroxyphenylacetaldehyde + NAD+ + H2O
4-hydroxyphenylacetate + NADH + H+
P80668
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
?
Achromobacter eurydice
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inducible enzyme appears when cells are grown on L-phenylalanine or on L-tryptophan as sole source of carbon
-
-
?
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
?
-
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 + H+
-
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
the enzyme participates in metabolism of phenylalanine
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
-
active with NAD+ and NADP+, preference for NAD+. kcat/Km for NADP+ with propionaldehyde is 2460
NAD+
-
active with NAD+ and NADP+, preference for NAD+. kcat/Km for NAD+ with propionaldehyde as cosubstrate is 34700
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
B4EH14
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 53700, calculation from nucleotide sequence; 2 * 55000, SDS-PAGE
homotetramer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Achromobacter eurydice
-
unstable after dilution, especially in alkaline medium
390292
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.39)
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