HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.2.1.39 - phenylacetaldehyde dehydrogenase
for references in articles please use BRENDA:EC1.2.1.39Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.2.1.39 phenylacetaldehyde dehydrogenaseSpecify your search results
Word Map
- 1.2.1.39
-
phenylacetic
- monooxygenase
- phenylpyruvate
- 2-phenylethylamine
- 2-phenylethanol
-
nad+-dependent
-
denitrifying
-
betaproteobacterium
- aromaticum
-
tungsten-dependent
- tyrosol
- 4-hydroxyphenylacetaldehyde
- phenylethanols
-
aromatoleum
-
dinucleotide-dependent
-
agrochemical
- phenylacetyl-coa
- tungstate
The enzyme appears in viruses and cellular organisms
Synonyms
phenylacetaldehyde dehydrogenase, npadh, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ebA4954
feaB
NPADH
PAD
PADH
PDH
phenylacetaldehyde dehydrogenase
styD
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+
-
-
-
-
phenylacetaldehyde + NAD+ + H2O = phenylacetate + NADH + 2 H+
sequential reaction mechanism in which NAD+ serves as both the leading substrate and homotropic allosteric activator, catalytic mechanism involving E169, E267, and C301, overview. The catalytic Glu has two conformations: a passive conformer that tucks away to allow hydride transfer to the nicotinamide ring, and an active conformer that abstracts a proton from the thioester-deacylating water
phenylacetaldehyde + NAD+ + H2O = phenylacetate + NADH + 2 H+
sequential reaction mechanism in which NAD+ serves as both the leading substrate and homotropic allosteric activator, catalytic mechanism involving E169, E267, and C301, overview. The catalytic Glu has two conformations: a passive conformer that tucks away to allow hydride transfer to the nicotinamide ring, and an active conformer that abstracts a proton from the thioester-deacylating water
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
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.
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.
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
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
-
-
-
?
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+
-
-
?
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
?
-
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+
-
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 + NADP+ + H2O
phenylacetate + NADPH + 2 H+
-
-
r
phenylacetaldehyde + NADP+ + H2O
phenylacetate + NADPH + 2 H+
-
-
r
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
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
?
-
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+
-
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
NAD+
-
active with NAD+ and NADP+, preference for NAD+. kcat/Km for NAD+ with propionaldehyde as cosubstrate is 34700
NAD+
N-terminal NAD+-binding domain, comprising residues 1-130 and 159-269, structure analysis, overview
NADP+
-
active with NAD+ and NADP+, preference for NAD+. kcat/Km for NADP+ with propionaldehyde is 2460
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+
-
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+
-
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
Mg2+
Mn2+
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
-
phenylacetaldehyde
the enzyme is highly specific for phenylacetaldehyde, has cooperative kinetics toward the substrate, and shows considerable substrate inhibition
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
additional information
additional information
kinetic analysis, overview. The enzyme shows cooperative kinetics toward substrate phenylacetaldehyde and considerable substrate inhibition
-
additional information
additional information
-
kinetic analysis, overview. The enzyme shows cooperative kinetics toward substrate phenylacetaldehyde and considerable substrate inhibition
-
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.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
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
0.102
purified native enzyme, with cofactor NADP+, pH 8.5, 28°C
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.
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
brenda
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.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
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
Show AA Sequence and Transmembrane Helices (1004 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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
53290
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
additional information
homotetramer
4 * 53500, recombinant Strep-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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
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
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.
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)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
143
513-518
1997
Escherichia coli
brenda
O'Connor, K.; Duetz, W.; Wind, B.; Dobson, A.D.W.
The effect of nutrient limitation on styrene metabolism in Pseudomonas putida CA-3
Appl. Environ. Microbiol.
62
3594-3599
1996
Pseudomonas putida, Pseudomonas putida CA-3
brenda
Rodriguez-Zavala, J.S.; Allali-Hassani, A.; Weiner, H.
Characterization of E. coli tetrameric aldehyde dehydrogenases with atypical properties compared to other aldehyde dehydrogenases
Protein Sci.
15
1387-1396
2006
Escherichia coli
brenda
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.
10
413-432
2008
Pseudomonas putida, Pseudomonas putida (B1N7H3)
brenda
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.
76
357-363
2007
Brevibacterium sp., Brevibacterium sp. KU1309
brenda
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
6203-6216
2012
Escherichia coli (P80668), Escherichia coli
brenda
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
J. Agric. Food Chem.
60
979-984
2012
Escherichia coli
brenda
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
Arch. Biochem. Biophys.
616
47-58
2017
Pseudomonas putida (V4GH04), Pseudomonas putida, Pseudomonas putida S12 (V4GH04), Pseudomonas putida S12
brenda
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
J. Bacteriol.
196
483-492
2014
Aromatoleum aromaticum (Q5P171), Aromatoleum aromaticum, Aromatoleum aromaticum EbN1 (Q5P171)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.2.1.39)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
