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Information on EC 1.2.1.30 - carboxylate reductase (NADP+)
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1.2.1.30 carboxylate reductase (NADP+)IUBMB Comments
The enzyme contains an adenylation domain, a phosphopantetheinyl binding domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group. The enzyme activates its substrate to an adenylate form, followed by a transfer to the phosphopantetheinyl binding domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to an aldehyde and released.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
aromatic acid reductase, aryl-aldehyde dehydrogenase (NADP+), 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
aryl-aldehyde:NADP+ oxidoreductase (ATP-forming)
The enzyme contains an adenylation domain, a phosphopantetheinyl binding domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group. The enzyme activates its substrate to an adenylate form, followed by a transfer to the phosphopantetheinyl binding domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to an aldehyde and released.
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CAS REGISTRY NUMBER
COMMENTARY
9074-94-6
-
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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
alpha-ketoglutaric acid + NADPH + ATP
? + NADP+ + AMP + phosphate
-
-
-
?
benzaldehyde + NADP+ + benzoyladenosine 5'-monophosphate + phosphate
benzoate + NADPH + ATP
-
-
-
-
r
benzoic acid + ATP + NADPH + H+
benzaldehyde + AMP + diphosphate + NADP+
highest turnover number
-
-
?
benzoic acid + NADPH + ATP
benzaldehyde + benzyl alcohol + NADP+ + AMP + phosphate
-
-
-
?
butyric acid + ATP + NADPH + H+
butyraldehyde + AMP + diphosphate + NADP+
-
highest Km value
-
?
caffeic acid + NADPH + ATP
3-(3,4-dihydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
capric acid + ATP + NADPH + H+
capraldehyde + AMP + diphosphate + NADP+
-
-
-
?
caproic acid + ATP + NADPH + H+
caproaldehyde + AMP + diphosphate + NADP+
-
-
-
?
caprylic acid + ATP + NADPH + H+
caprylaldehyde + AMP + diphosphate + NADP+
-
-
-
?
coniferic acid + NADPH + ATP
coniferyl aldehyde + NADP+ + AMP + phosphate
-
-
-
?
fatty acid + ATP + NADPH + H+
fatty aldehyde + AMP + diphosphate + NADP+
-
-
-
?
ferulic acid + NADPH + ATP
3-(4-hydroxy-3-methoxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
ferulic acid + NADPH + ATP
ferulic acid + coniferyl aldehyde + coniferyl alcohol + NADP+ + AMP + phosphate
not completely reduced
-
-
?
lauric acid + ATP + NADPH + H+
lauraldehyde + AMP + diphosphate + NADP+
highest catalytic efficiency
-
-
?
sinapic acid + NADPH + ATP
3-(4-hydroxy-3,5-dimethoxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
trans-aconitic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
-
-
-
?
vanillic acid + NADPH + ATP
vanillin + vanillyl alcohol + NADP+ + AMP + phosphate
-
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
-
-
?
(R)-ibuprofen + NADPH + ATP
(2R)-2-(4-(2-methylpropyl)phenyl)propanal + NADP+ + AMP + H2O
Nocadia sp.
-
-
-
?
(R)-ibuprofen + NADPH + ATP
(2R)-2-(4-(2-methylpropyl)phenyl)propanal + NADP+ + AMP + H2O
Nocadia sp. NRRL 5646
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
ir
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
ir
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
r
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
r
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
Nocadia sp.
-
-
-
ir
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
Nocadia sp. NRRL 5646
-
-
-
ir
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
benzoate + NADPH + ATP
benzaldehyde + NADP+ + AMP + phosphate
best substrate
-
-
?
benzoic acid + NADPH + ATP
benzaldehyde + NADP+ + AMP + H2O
-
-
-
?
benzoic acid + NADPH + ATP
benzaldehyde + NADP+ + AMP + H2O
-
-
-
?
benzoic acid + NADPH + ATP
benzaldehyde + NADP+ + AMP + H2O
-
rate relative to salycilate 286%
-
?
benzoic acid + NADPH + ATP
benzaldehyde + NADP+ + AMP + H2O
-
the reaction proceeds via benzoyladenosine 5'-monophosphate which is further reduced by NADPH to benzaldehyde
-
?
benzoic acid + NADPH + ATP
benzaldehyde + NADP+ + AMP + H2O
Nocadia sp.
-
the reaction proceeds via benzoyladenosine 5'-monophosphate which is further reduced by NADPH to benzaldehyde
-
?
benzoic acid + NADPH + ATP
benzaldehyde + NADP+ + AMP + H2O
Nocadia sp. NRRL 5646
-
the reaction proceeds via benzoyladenosine 5'-monophosphate which is further reduced by NADPH to benzaldehyde
-
?
benzoic acid + NADPH + ATP
benzaldehyde + NADP+ + AMP + H2O
-
-
-
?
benzoic acid + NADPH + ATP
benzaldehyde + NADP+ + AMP + H2O
-
-
-
?
cinnamic acid + NADPH + ATP
3-phenyl-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
cinnamic acid + NADPH + ATP
3-phenyl-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
cinnamic acid + NADPH + ATP
3-phenyl-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
ibuprofen + NADPH + ATP
2-(4-isobutylphenyl)propanal + NADP+ + AMP + H2O
Nocadia sp.
-
-
-
?
ibuprofen + NADPH + ATP
2-(4-isobutylphenyl)propanal + NADP+ + AMP + H2O
Nocadia sp. NRRL 5646
-
-
-
?
m-coumaric acid + NADPH + ATP
3-(3-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
m-coumaric acid + NADPH + ATP
3-(3-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
m-hydroxybenzoic acid + NADPH + ATP
m-hydroxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
m-hydroxybenzoic acid + NADPH + ATP
m-hydroxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
o-coumaric acid + NADPH + ATP
3-(2-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
o-coumaric acid + NADPH + ATP
3-(2-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
p-anisic acid + NADPH + ATP
p-methoxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
p-anisic acid + NADPH + ATP
p-methoxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
p-coumaric acid + NADPH + ATP
3-(4-hydroxphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
p-coumaric acid + NADPH + ATP
3-(4-hydroxphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
p-coumaric acid + NADPH + ATP
3-(4-hydroxphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
p-hydroxybenzoic acid + NADPH + ATP
p-hydroxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
p-hydroxybenzoic acid + NADPH + ATP
p-hydroxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
salicylic acid + NADPH + ATP
salicyl aldehyde + NADP+ + AMP + H2O
-
-
-
?
salicylic acid + NADPH + ATP
salicyl aldehyde + NADP+ + AMP + H2O
-
rate relative to benzoate 9%
-
?
vanillic acid + NADPH + ATP
4-hydroxy-3-methoxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
vanillic acid + NADPH + ATP
4-hydroxy-3-methoxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
vanillic acid + NADPH + ATP
vanillin + NADP+ + AMP + phosphate
-
-
-
?
additional information
?
-
Nocadia sp.
-
other substrates are phenyl-substituted aliphatic acids, heterocyclic carboxylic acids, polyaromatic ring carboxylic acids, ibuprofen and its (R)-(-) isomer
-
-
?
additional information
?
-
Nocadia sp. NRRL 5646
-
other substrates are phenyl-substituted aliphatic acids, heterocyclic carboxylic acids, polyaromatic ring carboxylic acids, ibuprofen and its (R)-(-) isomer
-
-
?
additional information
?
-
pyruvic, isocitric acid, fumaric acid and maleic acid are not substrates for the enzyme
-
-
?
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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
fatty acid + ATP + NADPH + H+
fatty aldehyde + AMP + diphosphate + NADP+
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
aromatic acids + NADPH + ATP
aromatic aldehydes + NADP+ + AMP + H2O
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetamide
-
inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
iodoacetate
-
inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
N-ethylmaleimide
-
inhibition of the reduction of benzoyladenosine 5'-monophosphate
NADPH
-
inhibition of the exchange reaction of diphosphate and ATP, inhibitory effect increases when dithiothreitol is added
o-Iodosobenzoate
-
inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
p-chloromercuribenzoate
-
inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
p-diazobenzenesulfonate
-
inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
stimulation of the reduction of the intermediate benzoyladenosine 5'-monophosphate to benzaldehyde
phosphopantetheine transferase
-
required for activating the enzyme. Recombinant car is an apoenzyme that requires phosphopantetheinylation for conversion to a fully active holoenzyme
-
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
LITERATURE
IMAGE
0.362
benzoic acid
pH and temperature not specified in the publication
0.13
NADPH
-
reduction of the intermediate benzoyladenylate to benzaldehyde
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.36
recombinant Car expressed in Escherichia coli BL21-CodonPlus(DE3)-RP cells cultured in LB medium with ampicillin, at 16 h
1.5
-
recombinant car incubated with CoA and Escherichia coli MV1190/pUC8-sfp cell free extract
1.6
-
Nocardia cell free extract incubated with recombinant car and CoA. Recombinant car incubated with CoA and Npt
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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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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26 - 37
in vitro half-lives of 73, 70, and 48 h at 26, 30, and 37°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A1J5R952_9ZZZZ
614
0
65999
TrEMBL
other Location (Reliability: 5)
CAR_MYCMM
Mycobacterium marinum (strain ATCC BAA-535 / M)
1174
0
127797
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 128300, deduced from gene sequence, x * 132400, SDS-PAGE, recombinant enzyme carrying His-tag
monomer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
by a combination of Mono-Q, Reactive Green 19 agarose affinity chromatography, and hydroxyapatite chromatography
Nocadia sp.
-
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kato, N.; Konishi, H.; Masuda, M.; Joung, E.H.; Shimao, M.; Sakazawa, C.
Reductive transformation of benzoate by Nocardia asteroides and hormoconis resinae
J. Ferment. Bioeng.
69
220-223
1990
Amorphotheca resinae, Nocardia asteroides, Amorphotheca resinae F328, Nocardia asteroides JCM 3016
-
brenda
Gross, G.G.
Formation and reduction of intermediate acyladenylate by aryl-aldehyde. NADP oxidoreductase from Neurospora crassa
Eur. J. Biochem.
31
585-592
1972
Neurospora crassa
brenda
Gross, G.G.
Stoichiometric studies on aryl-aldehyde: NADP oxidoreductase from Neurospra crassa
FEBS Lett.
17
309-311
1971
Neurospora crassa
brenda
Gross, G.G.; Zenk, M.H.
Reduction of aromatic acids to aldehydes and alcohols in the cell-free system. 1. Purification and properties of aryl-aldehyde: NADP-oxidoreductase from Neurospora crassa
Eur. J. Biochem.
8
413-419
1969
Neurospora crassa
brenda
Gross, G.G.; Bolkart, K.H.; Zenk, M.H.
Reduction of cinnamic acid to cinnamaldehyde and alcohol
Biochem. Biophys. Res. Commun.
32
173-178
1968
Neurospora crassa
brenda
Li, T.; Rosazza, J.P.N.
Purification, characterization, and properties of an aryl aldehyde oxidoreductase from Nocardia sp. strain NRRL 5646
J. Bacteriol.
179
3482-3487
1997
Nocadia sp., Nocadia sp. NRRL 5646
brenda
He, A.; Li, T.; Daniels, L.; Fotheringham, I.; Rosazza, J.P.N.
Nocardia sp. carboxylic acid reductase: cloning, expression, and characterization of a new aldehyde oxidoreductase family
Appl. Environ. Microbiol.
70
1874-1881
2004
Nocardia sp. (Q6RKB1)
brenda
Venkitasubramanian, P.; Daniels, L.; Das, S.; Lamm, A.S.; Rosazza, J.P.
Aldehyde oxidoreductase as a biocatalyst: Reductions of vanillic acid
Enzyme Microb. Technol.
42
130-137
2008
Nocardia iowensis (Q6RKB1)
brenda
Venkitasubramanian, P.; Daniels, L.; Rosazza, J.P.
Reduction of carboxylic acids by Nocardia aldehyde oxidoreductase requires a phosphopantetheinylated enzyme
J. Biol. Chem.
282
478-485
2007
Nocardia iowensis
brenda
Akhtar, M.K.; Turner, N.J.; Jones, P.R.
Carboxylic acid reductase is a versatile enzyme for the conversion of fatty acids into fuels and chemical commodities
Proc. Natl. Acad. Sci. USA
110
87-92
2013
Mycobacterium marinum (B2HN69)
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