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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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Word Map
- 1.2.1.30
- synthesis
-
bio-based
-
fragrance
-
autoinduction
-
phosphopantetheinylation
-
over-reduction
- benzaldehyde
- industry
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
carboxylate reductases, macar, nicar, mmcar, nocar, nccar, aryl-aldehyde oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aromatic acid reductase
-
-
-
-
aryl-aldehyde dehydrogenase (NADP+)
-
-
-
-
aryl-aldehyde oxidoreductase
ATP/NADPH-dependent carboxylic acid reductase
CAR
carboxylate reductase
carboxylate reductases
Carboxylic acid reductase
maCAR
mmCAR
mpCAR
NcCAR
niCAR
type I CAR
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
-
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Aspergillus niger
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Neurospora crassa
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Moorella thermoacetica
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Nocardia asteroides
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Trametes versicolor
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Nocardia iowensis
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Mycobacteroides abscessus
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Mycobacterium marinum
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Mycolicibacterium smegmatis
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Syncephalastrum racemosum
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Nocardia otitidiscaviarum
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Tsukamurella paurometabola
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Nocardia brasiliensis
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Mycolicibacterium phlei
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Segniliparus rotundus
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Aspergillus terreus
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Aspergillus terreus NIH 2624
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Mycobacterium marinum ATCC BAA-535
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Segniliparus rotundus CIP 108378
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Segniliparus rotundus ATCC BAA-972
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Segniliparus rotundus JCM 13578
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Nocardia asteroides JCM 3016
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Aspergillus terreus FGSC A1156
-
-
-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Segniliparus rotundus DSM 44985
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-
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
Segniliparus rotundus CDC 1076
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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oxidation
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reduction
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-
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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
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop-2-enal + NADP+ + AMP + diphosphate
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop2-enal + NADP+ + AMP + diphosphate
2-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-hydroxypropionate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
-
-
-
-
ir
3-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-nitrobenzoate + NADPH + H+ + ATP
4-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
4-hydroxybutyrate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
-
-
-
-
ir
4-methoxybenzoate + NADPH + H+ + ATP
2-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
5-hydroxypentanoate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
-
-
-
-
ir
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 + H+ + ATP
benzaldehyde + benzyl alcohol + NADP+ + AMP + diphosphate
-
-
-
?
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 + H+ + ATP
3-(4-hydroxy-3-methoxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O + diphosphate
-
-
-
?
ferulic acid + NADPH + H+ + ATP
ferulic acid + coniferyl aldehyde + coniferyl alcohol + NADP+ + AMP + diphosphate
not completely reduced
-
-
?
glutarate + NADPH + H+ + ATP
5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
lauric acid + ATP + NADPH + H+
lauraldehyde + AMP + diphosphate + NADP+
highest catalytic efficiency
-
-
?
pyridine-2-carboxylate + NADPH + H+ + ATP
pyridine-2-carbaldehyde + NADP+ + AMP + diphosphate
sinapic acid + NADPH + ATP
3-(4-hydroxy-3,5-dimethoxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
trans-aconitic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
-
-
-
?
vanillic acid + NADPH + H+ + ATP
4-hydroxy-3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
vanillic acid + NADPH + H+ + ATP
vanillin + vanillyl alcohol + NADP+ + AMP + diphosphate
-
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
-
-
?
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop-2-enal + NADP+ + AMP + diphosphate
-
-
-
?
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop-2-enal + NADP+ + AMP + diphosphate
-
-
-
-
?
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop2-enal + NADP+ + AMP + diphosphate
-
-
-
-
?
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop2-enal + NADP+ + AMP + diphosphate
-
-
-
-
?
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop2-enal + NADP+ + AMP + diphosphate
-
-
-
-
?
(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
-
-
-
?
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
-
-
-
ir
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
-
-
-
ir
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
-
-
-
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
-
-
-
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
-
-
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
-
-
-
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
-
-
-
?
3-phenylprop-2-ynoate + NADPH + H+ + ATP
3-phenylprop-2-ynal + NADP+ + AMP + diphosphate
-
-
-
?
3-phenylprop-2-ynoate + NADPH + H+ + ATP
3-phenylprop-2-ynal + NADP+ + AMP + diphosphate
-
-
-
-
?
3-phenylprop-2-ynoate + NADPH + H+ + ATP
3-phenylprop-2-ynal + NADP+ + AMP + diphosphate
-
-
-
-
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
-
-
-
ir
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
-
-
-
ir
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
5-hydroxypentanoate + NADPH + H+ + ATP
5-hydroxypentanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
5-hydroxypentanoate + NADPH + H+ + ATP
5-hydroxypentanal + NADP+ + AMP + diphosphate
-
-
-
ir
5-hydroxypentanoate + NADPH + H+ + ATP
5-hydroxypentanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Nocardia asteroides JCM 3016
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
Amorphotheca resinae F328
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
ir
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
ir
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
r
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
r
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
Nocadia sp.
-
-
-
ir
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
Nocadia sp. NRRL 5646
-
-
-
ir
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
Nocardia asteroides JCM 3016
-
-
-
?
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Aspergillus terreus NIH 2624
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + ATP
benzaldehyde + NADP+ + AMP + phosphate
best substrate
-
-
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
via an adenylated intermediate
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
via an adenylated intermediate
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
via an adenylated intermediate
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + H2O + diphosphate
-
-
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + H2O + diphosphate
Amorphotheca resinae F328
-
-
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + H2O + diphosphate
-
rate relative to salycilate 286%
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + H2O + diphosphate
-
the reaction proceeds via benzoyladenosine 5'-monophosphate which is further reduced by NADPH to benzaldehyde
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + H2O + diphosphate
Nocadia sp.
-
the reaction proceeds via benzoyladenosine 5'-monophosphate which is further reduced by NADPH to benzaldehyde
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + H2O + diphosphate
Nocadia sp. NRRL 5646
-
the reaction proceeds via benzoyladenosine 5'-monophosphate which is further reduced by NADPH to benzaldehyde
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + H2O + diphosphate
-
-
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + H2O + diphosphate
Nocardia asteroides JCM 3016
-
-
-
?
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
-
-
-
?
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
Neurospora crassa 74-OR23-1A
-
-
-
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
Neurospora crassa ATCC 24698
-
-
-
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
Neurospora crassa CBS 708.71
-
-
-
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
Neurospora crassa DSM 1257
-
-
-
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
Neurospora crassa FGSC 987
-
-
-
?
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
-
-
-
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
-
-
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
furan-2-carboxylate + NADPH + H+ + ATP
furan-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
furan-2-carboxylate + NADPH + H+ + ATP
furan-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
glutarate + NADPH + H+ + ATP
5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
-
-
-
-
ir
glutarate + NADPH + H+ + ATP
5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
-
-
-
ir
glutarate + NADPH + H+ + ATP
5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
-
-
-
-
ir
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
-
-
-
?
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
Neurospora crassa 74-OR23-1A
-
-
-
?
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
Neurospora crassa ATCC 24698
-
-
-
?
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
Neurospora crassa CBS 708.71
-
-
-
?
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
-
-
-
?
malonate + NADPH + H+ + ATP
3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
-
low activity
-
-
ir
malonate + NADPH + H+ + ATP
3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
low activity
-
-
ir
malonate + NADPH + H+ + ATP
3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
-
low activity
-
-
ir
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
-
-
-
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
-
-
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
-
-
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
-
-
-
?
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
-
-
-
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
Neurospora crassa 74-OR23-1A
-
-
-
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
Neurospora crassa ATCC 24698
-
-
-
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
Neurospora crassa CBS 708.71
-
-
-
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
Neurospora crassa DSM 1257
-
-
-
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
Neurospora crassa FGSC 987
-
-
-
?
pyridine-2-carboxylate + NADPH + H+ + ATP
pyridine-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
pyridine-2-carboxylate + NADPH + H+ + ATP
pyridine-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
salicylic acid + NADPH + ATP
salicyl aldehyde + NADP+ + AMP + H2O
-
-
-
?
salicylic acid + NADPH + ATP
salicyl aldehyde + NADP+ + AMP + H2O
-
rate relative to benzoate 9%
-
?
succinate + NADPH + H+ + ATP
4-oxobutanoate + 1,4-butanedial + NADP+ + AMP + diphosphate
-
-
-
ir
succinate + NADPH + H+ + ATP
4-oxobutanoate + 1,4-butanedial + NADP+ + AMP + diphosphate
-
-
-
-
ir
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
-
ir
vanillic acid + NADPH + H+ + ATP
4-hydroxy-3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
vanillic acid + NADPH + H+ + ATP
4-hydroxy-3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
vanillic acid + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
?
vanillic acid + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
?
additional information
?
-
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
Aspergillus terreus NIH 2624
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
-
no activity of the wild-type enzyme with succinate. Substrate specificity of recombinant hybrid mutant enzymes, overview
-
-
-
additional information
?
-
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
-
substrate specificity of recombinant hybrid mutant enzymes, overview
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
substrate specificity of recombinant hybrid mutant enzymes, overview
-
-
-
additional information
?
-
the enzyme is active against C2-C18 fatty acids. Enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity
-
-
-
additional information
?
-
the enzyme is active against C2-C18 fatty acids. Enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
substrate specificity of recombinant hybrid mutant enzymes, overview
-
-
-
additional information
?
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
-
no activity with 2-methoxybenzoate, 4-nitrobenzoate, 2-nitrobenzoate, phenylpropynoate, butanoate, pyridine-2-carboxylate, 1H-pyrrole-2-carboxylate, and furan-2-carboxylate
-
-
-
additional information
?
-
-
enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity. No activity with 2-methoxybenzoate, 4-nitrobenzoate, 2-nitrobenzoate, phenylpropynoate, pyridine-2-carboxylate, and 1H-pyrrole-2-carboxylate
-
-
-
additional information
?
-
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
NcCAR wild-type and mutants efficiently reduce aliphatic acids
-
-
-
additional information
?
-
-
substrate specificity of recombinant hybrid mutant enzymes, overview
-
-
-
additional information
?
-
Neurospora crassa 74-OR23-1A
NcCAR wild-type and mutants efficiently reduce aliphatic acids
-
-
-
additional information
?
-
Neurospora crassa ATCC 24698
NcCAR wild-type and mutants efficiently reduce aliphatic acids
-
-
-
additional information
?
-
Neurospora crassa CBS 708.71
NcCAR wild-type and mutants efficiently reduce aliphatic acids
-
-
-
additional information
?
-
Neurospora crassa DSM 1257
NcCAR wild-type and mutants efficiently reduce aliphatic acids
-
-
-
additional information
?
-
Neurospora crassa FGSC 987
NcCAR wild-type and mutants efficiently reduce aliphatic acids
-
-
-
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
?
-
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
-
the enzyme prefers benzoates and aliphatic acids that are substituted with a phenyl group in the 3-position. No reaction of this CAR with simple aliphatic acids
-
-
-
additional information
?
-
Nocardia asteroides JCM 3016
-
the enzyme prefers benzoates and aliphatic acids that are substituted with a phenyl group in the 3-position. No reaction of this CAR with simple aliphatic acids
-
-
-
additional information
?
-
-
enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity
-
-
-
additional information
?
-
pyruvic, isocitric acid, fumaric acid and maleic acid are not substrates for the enzyme
-
-
?
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
no activity with 2-methoxybenzoate, 4-nitrobenzoate, 2-nitrobenzoate, pyridine-2-carboxylate, 1H-pyrrole-2-carboxylate, and furan-2-carboxylate
-
-
-
additional information
?
-
-
substrate specificity of recombinant hybrid mutant enzymes, overview
-
-
-
additional information
?
-
-
no activity with 2-methoxybenzoate, 4-nitrobenzoate, 2-nitrobenzoate, 1H-pyrrole-2-carboxylate and furan-2-carboxylate
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
-
the enzyme is active against C2-C18 fatty acids
-
-
-
additional information
?
-
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
-
the enzyme is active against C2-C18 fatty acids
-
-
-
additional information
?
-
-
no activity with 2-nitrobenzoate and 1H-pyrrole-2-carboxylate
-
-
-
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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 + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
Amorphotheca resinae F328
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
Nocardia asteroides JCM 3016
-
-
-
?
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
Aspergillus terreus NIH 2624
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
via an adenylated intermediate
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
via an adenylated intermediate
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
-
ir
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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
diphosphate
-
product inhibition, mixed inhibition with ATP, competitive versus 4-methylbenzoic acid
NADP+
-
product inhibition, NADP+ shows competitive inhibition with NADPH
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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
-
for activation, CARs require PPTase-mediated post-translational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
-
additional information
-
for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
-
additional information
for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
-
additional information
-
for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
-
additional information
-
for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
-
additional information
-
for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
-
additional information
levels of recombinant Car and Gdh are slightly higher when cultures are grown without chloramphenicol
-
additional information
for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
-
additional information
-
for activation, CARs require PPTase-mediated post-translational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cardiovascular Diseases
Feasibility of cardiovascular disease risk assessments in rheumatology outpatient clinics: experiences from the nationwide NOCAR project.
Hypotension
ANAPHYLACTIC SHOCK DECREASES CEREBRAL BLOOD FLOW MORE THAN WHAT WOULD BE EXPECTED FROM SEVERE ARTERIAL HYPOTENSION.
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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
additional information
additional information
-
kinetic analysis
-
additional information
additional information
-
kinetic analysis
-
additional information
additional information
-
stopped-flow measurements, steady-state (kcat) and single-turnover (kobs) kinetics of wild-type and hybrid mutant enzymes, comparisons, overview
-
additional information
additional information
-
stopped-flow measurements, steady-state (kcat) and single-turnover (kobs) kinetics of wild-type and hybrid mutant enzymes, comparisons, overview
-
additional information
additional information
-
stopped-flow measurements, steady-state (kcat) and single-turnover (kobs) kinetics of wild-type and hybrid mutant enzymes, comparisons, overview
-
additional information
additional information
-
stopped-flow measurements, steady-state (kcat) and single-turnover (kobs) kinetics of wild-type and hybrid mutant enzymes, comparisons, overview
-
additional information
additional information
stopped-flow measurements, steady-state (kcat) and single-turnover (kobs) kinetics of wild-type and hybrid mutant enzymes, comparisons, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.34
diphosphate
-
pH and temperature not specified in the publication, versus 4-methylbenzoic acid
0.22
diphosphate
-
pH and temperature not specified in the publication, versus ATP
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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
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28
30
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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
Nocardia asteroides JCM 3016
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
evolution
additional information
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids. Enzyme CAR from Mycobacterium marinum (mmCAR) reduces a number of aliphatic acids ranging from C3 to C18
physiological function
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids. The purified enzyme from Nocardia iowensis reduces a broader range of substituted aromatic acids in addition to dicarboxylic acids of the citric acid cycle, resulting in a branding of the aryl-aldehyde oxidoreductase class more broadly as carboxylic acid reductases (CARs)
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids. Whole cell reduction of aromatic carboxylic acids in the white-rot fungi Trametes versicolor
physiological function
requirement for the presence of a phosphopantetheine transferase for the loading of a phosphopantetheine group onto the CAR enzyme is shown for niCAR. Enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
physiological function
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
physiological function
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
physiological function
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
physiological function
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
physiological function
Aspergillus terreus NIH 2624
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
-
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids. Enzyme CAR from Mycobacterium marinum (mmCAR) reduces a number of aliphatic acids ranging from C3 to C18
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
malfunction
lack of posttranslational phosphopantetheinylation of a serine group in the recombinant CAR reduces the activity of recombinantly expressed enzyme
malfunction
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
malfunction
-
the purified CAR with a mutation to its conserved serine idue appears to degrade into separate A- and R-domains when incubated at room temperature
malfunction
Neurospora crassa CBS 708.71
-
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
-
malfunction
Neurospora crassa 74-OR23-1A
-
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
-
malfunction
Neurospora crassa DSM 1257
-
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
-
malfunction
Neurospora crassa ATCC 24698
-
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala