HOME
login
history
all enzymes
BRENDA home
History
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
- 2-phenylethanol
- phenylpyruvate
- 2-phenylethylamine
-
nad+-dependent
-
denitrifying
- 4-hydroxyphenylacetaldehyde
-
dinucleotide-dependent
-
homotetrameric
- 4-hydroxyphenylacetate
-
tungsten-dependent
-
aromatoleum
- tyrosol
- phenylacetyl-coa
- tungstate
-
betaproteobacterium
- aromaticum
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The enzyme appears in viruses and cellular organisms
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.2.1.39
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
phenylacetaldehyde dehydrogenase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phenylacetaldehyde + NAD+ + H2O = phenylacetate + NADH + 2 H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
phenylacetaldehyde:NAD+ oxidoreductase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
58943-37-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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+
-
-
-
-
?
4-hydroxyphenylacetaldehyde + NAD+ + H2O
4-hydroxyphenylacetate + NADH + H+
-
-
-
-
?
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
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
21% activity relative to phenylacetaldehyde
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
21% activity relative to phenylacetaldehyde
-
-
?
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
?
-
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+
Achromobacter eurydice
-
highly specific for phenylacetaldehyde, NADP+ is about 1% as active as NAD+
-
ir
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+
-
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+
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
?
4-hydroxyphenylacetaldehyde + NAD+ + H2O
4-hydroxyphenylacetate + NADH + H+
-
-
-
-
?
4-hydroxyphenylacetaldehyde + NAD+ + H2O
4-hydroxyphenylacetate + NADH + H+
P80668
-
-
-
?
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
?
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 53700, calculation from nucleotide sequence; 2 * 55000, SDS-PAGE
homotetramer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Achromobacter eurydice
-
unstable after dilution, especially in alkaline medium
390292
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Expression in Escherichia coli, production of knock out-mutants is carried out by mutagenesis.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.39)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
