Information on EC 1.2.1.30 - aryl-aldehyde dehydrogenase (NADP+)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.2.1.30
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RECOMMENDED NAME
GeneOntology No.
aryl-aldehyde dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an aromatic aldehyde + NADP+ + AMP + diphosphate + H2O = an aromatic acid + NADPH + H+ + ATP
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
aryl-aldehyde:NADP+ oxidoreductase (ATP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9074-94-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
F328
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Manually annotated by BRENDA team
Nocadia sp.
strain NRRL 5646
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Manually annotated by BRENDA team
Nocadia sp. NRRL 5646
strain NRRL 5646
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Manually annotated by BRENDA team
JCM 3016
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Manually annotated by BRENDA team
JCM 3016
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Manually annotated by BRENDA team
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Swissprot
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-ibuprofen + NADPH + ATP
(2R)-2-(4-(2-methylpropyl)phenyl)propanal + NADP+ + AMP + H2O
show the reaction diagram
alpha-ketoglutaric acid + NADPH + ATP
? + NADP+ + AMP + phosphate
show the reaction diagram
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
show the reaction diagram
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
show the reaction diagram
benzoate + NADPH + ATP
benzaldehyde + NADP+ + AMP + phosphate
show the reaction diagram
benzoic acid + ATP + NADPH + H+
benzaldehyde + AMP + diphosphate + NADP+
show the reaction diagram
highest turnover number
-
-
?
benzoic acid + NADPH + ATP
benzaldehyde + benzyl alcohol + NADP+ + AMP + phosphate
show the reaction diagram
-
-
-
?
benzoic acid + NADPH + ATP
benzaldehyde + NADP+ + AMP + H2O
show the reaction diagram
butyric acid + ATP + NADPH + H+
butyraldehyde + AMP + diphosphate + NADP+
show the reaction diagram
-
highest Km value
-
?
caffeic acid + NADPH + ATP
3-(3,4-dihydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
show the reaction diagram
-
-
-
?
capric acid + ATP + NADPH + H+
capraldehyde + AMP + diphosphate + NADP+
show the reaction diagram
-
-
-
?
caproic acid + ATP + NADPH + H+
caproaldehyde + AMP + diphosphate + NADP+
show the reaction diagram
-
-
-
?
caprylic acid + ATP + NADPH + H+
caprylaldehyde + AMP + diphosphate + NADP+
show the reaction diagram
-
-
-
?
cinnamic acid + NADPH + ATP
3-phenyl-2-propen-1-al + NADP+ + AMP + H2O
show the reaction diagram
cis-aconitic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
show the reaction diagram
-
-
-
?
citric acid + NADPH + ATP
? + NADP+ + AMP + phosphate
show the reaction diagram
-
-
-
?
coniferic acid + NADPH + ATP
coniferyl aldehyde + NADP+ + AMP + phosphate
show the reaction diagram
-
-
-
?
D-malic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
show the reaction diagram
-
-
-
?
DL-malic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
show the reaction diagram
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-
-
?
fatty acid + ATP + NADPH + H+
fatty aldehyde + AMP + diphosphate + NADP+
show the reaction diagram
-
-
-
?
ferulic acid + NADPH + ATP
3-(4-hydroxy-3-methoxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
show the reaction diagram
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-
-
?
ferulic acid + NADPH + ATP
ferulic acid + coniferyl aldehyde + coniferyl alcohol + NADP+ + AMP + phosphate
show the reaction diagram
not completely reduced
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-
?
ibuprofen + NADPH + ATP
2-(4-isobutylphenyl)propanal + NADP+ + AMP + H2O
show the reaction diagram
L-malic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
show the reaction diagram
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-
-
?
lauric acid + ATP + NADPH + H+
lauraldehyde + AMP + diphosphate + NADP+
show the reaction diagram
highest catalytic efficiency
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-
?
m-coumaric acid + NADPH + ATP
3-(3-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
show the reaction diagram
m-hydroxybenzoic acid + NADPH + ATP
m-hydroxybenzaldehyde + NADP+ + AMP + H2O
show the reaction diagram
o-coumaric acid + NADPH + ATP
3-(2-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
show the reaction diagram
p-anisic acid + NADPH + ATP
p-methoxybenzaldehyde + NADP+ + AMP + H2O
show the reaction diagram
p-coumaric acid + NADPH + ATP
3-(4-hydroxphenyl)-2-propen-1-al + NADP+ + AMP + H2O
show the reaction diagram
p-hydroxybenzoic acid + NADPH + ATP
p-hydroxybenzaldehyde + NADP+ + AMP + H2O
show the reaction diagram
salicylic acid + NADPH + ATP
salicyl aldehyde + NADP+ + AMP + H2O
show the reaction diagram
sinapic acid + NADPH + ATP
3-(4-hydroxy-3,5-dimethoxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
show the reaction diagram
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-
-
?
trans-aconitic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
show the reaction diagram
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-
-
?
vanillic acid + NADPH + ATP
4-hydroxy-3-methoxybenzaldehyde + NADP+ + AMP + H2O
show the reaction diagram
vanillic acid + NADPH + ATP
vanillin + NADP+ + AMP + phosphate
show the reaction diagram
vanillic acid + NADPH + ATP
vanillin + vanillyl alcohol + NADP+ + AMP + phosphate
show the reaction diagram
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with Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.83, in which recombinant Npt is expressed along with recombinant car, vanillic acid is reduced to vanillin and vanillyl alcohol, with vanillin (80%) as the major product. Escherichia coli BL21-CodonPlus(DE3)-RP/pHAT305 (expressing only recombinant Car) reduce only 50% of the vanillic acid starting material, with vanillyl alcohol being the major metabolite. With Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.83, in which recombinant car is presumed to be in the fully active, phosphopantetheinylated holo form, the rate of reduction of vanillic acid is much faster than that of vanillin to vanillyl alcohol by endogenous Escherichia coli aldehyde dehydrogenase
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?
additional information
?
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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
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
show the reaction diagram
fatty acid + ATP + NADPH + H+
fatty aldehyde + AMP + diphosphate + NADP+
show the reaction diagram
B2HN69
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
no cofactor: NADH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
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inhibition of the exchange reaction of diphosphate and ATP
anthranilic acid
Nocadia sp.
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competitive inhibitor with benzoic acid as a substrate
hydroxylamine
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inhibition of the exchange reaction of diphosphate and ATP
iodoacetamide
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inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
iodoacetate
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inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
N-ethylmaleimide
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inhibition of the reduction of benzoyladenosine 5'-monophosphate
NADPH
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inhibition of the exchange reaction of diphosphate and ATP, inhibitory effect increases when dithiothreitol is added
o-Iodosobenzoate
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inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
p-chloromercuribenzoate
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inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
p-diazobenzenesulfonate
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inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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stimulation of the reduction of the intermediate benzoyladenosine 5'-monophosphate to benzaldehyde
phosphopantetheine transferase
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required for activating the enzyme. Recombinant car is an apoenzyme that requires phosphopantetheinylation for conversion to a fully active holoenzyme
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additional information
levels of recombinant Car and Gdh are slightly higher when cultures are grown without chloramphenicol
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0345
(R)-ibuprofen
Nocadia sp.
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0.0573 - 0.152
ATP
0.063 - 0.645
Benzoate
0.362
Benzoic acid
pH and temperature not specified in the publication
0.2
benzoyladenosine 5'-monophosphate
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0.155
Ibuprofen
Nocadia sp.
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0.0293 - 0.13
NADPH
0.167
salicylate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.261
anthranilic acid
Nocadia sp.
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.008
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induced cells
0.035
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induced cells
0.11
pH 7.5, 25C, recombinant enzyme with His-tag
0.3
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recombinant car incubated with CoA
0.36
recombinant Car expressed in Escherichia coli BL21-CodonPlus(DE3)-RP cells cultured in LB medium with ampicillin, at 16 h
0.5
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Nocardia cell free extract incubated with recombinant car
1.5
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recombinant car incubated with CoA and Escherichia coli MV1190/pUC8-sfp cell free extract
1.6
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Nocardia cell free extract incubated with recombinant car and CoA. Recombinant car incubated with CoA and Npt
2.1
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car purified from BL21-CodonPlus(DE3)-RP/pPV1.184 (car and sfp)
5.89
Nocadia sp.
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
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for the reduction of benzoyladenosine 5'-monophosphate
7.7 - 8.1
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salicylate + ATP + NADPH
8.4 - 9.2
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for the exchange reaction of diphosphate and ATP
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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not active below, benzoate + ATP
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 36
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salicylate + ATP + NADPH
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26 - 37
in vitro half-lives of 73, 70, and 48 h at 26, 30, and 37C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
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gel filtration
128300
x * 128300, deduced from gene sequence, x * 132400, SDS-PAGE, recombinant enzyme carrying His-tag
132400
x * 128300, deduced from gene sequence, x * 132400, SDS-PAGE, recombinant enzyme carrying His-tag
140000
Nocadia sp.
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1 * 140000, SDS-PAGE
163000
Nocadia sp.
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 128300, deduced from gene sequence, x * 132400, SDS-PAGE, recombinant enzyme carrying His-tag
monomer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol in chromatographic buffers stabilizes
Nocadia sp.
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, 2 weeks
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0C, in the presence of dithiothreitol, 2 months
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0C, plus reagents with SH-groups, 3 weeks
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4C, 50 mM Tris-HCl buffer, pH 7.5, 10% glycerol, 8 hours
Nocadia sp.
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pH 7.6, 50% glycerol, 1 mM EDTA, 2.5 mM mercaptoethanol, 6 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by a combination of Mono-Q, Reactive Green 19 agarose affinity chromatography, and hydroxyapatite chromatography
Nocadia sp.
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by gel filtration
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by precipitation of nucleic acids with protamine sulfate, ammonium sulphate fractionation, adsorption on calcium-phosphate gel and chromatography on TEAE-cellulose and on hydroxylapatite
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nickel affinity column chromatography
recombinant enzyme with his-tag
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
plasmids pHAT305(Placcar), pPV2.83(Placcar Placnpt), pPV2.84(Placcar Placgdh) or pPV2.85(Placcar Plac npt gdh) expressed in Escherichia coli BL21-CodonPlus(DE3)-RP cells
recombinant car expressed in Escherichia coli BL21-CodonPlus(DE3)-RP/pHAT305 and in Escherichia coli BL21-CodonPlus(DE3)-RP/pPV1.184 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S689A
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completely inactive
S691A
-
has 39% of the activity of recombinant car
S694A
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has 50% of the activity of recombinant car
S696A
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has 76% of the activity of recombinant car
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
vanillic acid reduction in Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.85 cells containing car, npt and gdh is complete in 6 h, and is faster than in cells containing only car and/or npt. The availability of Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.85 expressing holo-Car and Gdh provides a means of generating a range of value-added aldehydes or alcohols of importance in pharmaceutical, food and agricultural industries. Uses of directed evolution and related mutant generating processes, may enable a Car-system with broader substrate specificities and one that is capable of achieving much higher product yields
synthesis
by combining the carboxylic acid reductase-dependent pathway with an exogenous fatty acid-generating lipase, natural oils (coconut oil, palm oil, and algal oil bodies) can be enzymatically converted into fatty alcohols across a broad chain length range (C8-C18)