1.2.1.30: carboxylate reductase (NADP+)
This is an abbreviated version!
For detailed information about carboxylate reductase (NADP+), go to the full flat file.
Word Map on EC 1.2.1.30
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1.2.1.30
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synthesis
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bio-based
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fragrance
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autoinduction
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phosphopantetheinylation
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over-reduction
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benzaldehyde
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industry
- 1.2.1.30
- synthesis
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bio-based
-
fragrance
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autoinduction
-
phosphopantetheinylation
-
over-reduction
- benzaldehyde
- industry
Reaction
Synonyms
aromatic acid reductase, aryl aldehyde:NADP+ oxidoreductase, aryl-aldehyde dehydrogenase (NADP+), aryl-aldehyde oxidoreductase, ATP/NADPH-dependent carboxylic acid reductase, CAR, carboxylate reductase, carboxylate reductases, Carboxylic acid reductase, kaCAR, mab3CAR, maCAR, mmCAR, mpCAR, msCAR, naCAR, NcCAR, niCAR, noCAR, tpCAR, type I CAR, type III CAR
ECTree
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Engineering
Engineering on EC 1.2.1.30 - carboxylate reductase (NADP+)
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E697Q
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site-directed mutagenesis, the mutant enzyme retains 48.8% of wild-type activity with benzoate substrate
Q637E
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site-directed mutagenesis, the mutant enzyme retains 47.1% of wild-type activity with benzoate substrate
A922G
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
E337A
E433A
E441A
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
F787A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
G432A
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site-directed mutagenesis, the mutant shows activity similar to wild-type
G457A
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
G592A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
G691A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
G694A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
G697A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
G755A
site-directed mutagenesis, the mutant has activity similar to wild-type
G843A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
G882A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
H237A
K190A
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site-directed mutagenesis, the mutant shows increased activity compared to wild-type
K848A
N885A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
P189A
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site-directed mutagenesis, the mutant shows activity similar to wild-type
P198A
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
P234A
P285A
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
P904A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
T186A
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site-directed mutagenesis, the mutant shows activity similar to wild-type
Y542A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
Y844A
P285A
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site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
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P285A
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site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
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P285A
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site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
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P285A
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site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
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P285A
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site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
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additional information
E337A
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site-directed mutagenesis, mutant shows decreased activity compared to wild-type
E433A
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site-directed mutagenesis, mutant shows decreased activity compared to wild-type
H237A
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site-directed mutagenesis, mutant shows decreased activity compared to wild-type
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site-directed mutagenesis, the mutant shows increased activity compared to wild-type
P234A
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
-
additional information
-
hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Kutzneria albida (Ka) resulting in hybrid enzymes: Mav(A)-Ka(PR), Mav(AP)-Ka(R), Ka(A)-Mav(PR), and Ka(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes
additional information
-
hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Mycobacterium marinum (Mm), Kutzneria albida (Ka), and Nocardia iowensis (Ni), and one fungal strain, Neurospora crassa (Nc), resulting in hybrid enzymes: Mav(A)-Mm(PR), Mav(AP)-Mm(R), Mm(A)-Mav(PR), Mm(AP)-Mav(R), Mav(A)-Ka(PR), Mav(AP)-Ka(R), Ka(A)-Mav(PR), Ka(AP)-Mav(R), Mav(A)-Ni(PR), Mav(AP)-Ni(R), Ni(A)-Mav(PR), and Ni(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs, overview. When mutations Q637E and E697Q are introduced into hybrid CAR, Mm(A)-Mav(PR), reduction in activities is also observed, albeit to a less extent. Analysis of substrate specificity of recombinant hybrid mutant enzymes
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
additional information
hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Mycobacterium marinum (Mm) resulting in hybrid enzymes: Mav(A)-Mm(PR), Mav(AP)-Mm(R), Mm(A)-Mav(PR), and Mm(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
-
additional information
-
hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Mycobacterium marinum (Mm) resulting in hybrid enzymes: Mav(A)-Mm(PR), Mav(AP)-Mm(R), Mm(A)-Mav(PR), and Mm(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
additional information
-
hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from fungus Neurospora crassa (Nc), resulting in hybrid enzymes: Mav(A)-Nc(PR), Mav(AP)-Nc(R), Nc(A)-Mav(PR), and Nc(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes
additional information
the replacement of Gly184, Arg870, and Trp978 by alanine does not result in soluble expression. Pro904 is located close to Trp978, and its substitution by Ala yields significantly less soluble protein. Replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity. Substitutions with alanine (P189A, P234A, P285A, E441A, and G457A) enhanced the specific activity toward hexanoic acid compared to the wild-type
additional information
-
the replacement of Gly184, Arg870, and Trp978 by alanine does not result in soluble expression. Pro904 is located close to Trp978, and its substitution by Ala yields significantly less soluble protein. Replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity. Substitutions with alanine (P189A, P234A, P285A, E441A, and G457A) enhanced the specific activity toward hexanoic acid compared to the wild-type
-
additional information
-
the replacement of Gly184, Arg870, and Trp978 by alanine does not result in soluble expression. Pro904 is located close to Trp978, and its substitution by Ala yields significantly less soluble protein. Replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity. Substitutions with alanine (P189A, P234A, P285A, E441A, and G457A) enhanced the specific activity toward hexanoic acid compared to the wild-type
-
additional information
-
the replacement of Gly184, Arg870, and Trp978 by alanine does not result in soluble expression. Pro904 is located close to Trp978, and its substitution by Ala yields significantly less soluble protein. Replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity. Substitutions with alanine (P189A, P234A, P285A, E441A, and G457A) enhanced the specific activity toward hexanoic acid compared to the wild-type
-
additional information
-
the replacement of Gly184, Arg870, and Trp978 by alanine does not result in soluble expression. Pro904 is located close to Trp978, and its substitution by Ala yields significantly less soluble protein. Replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity. Substitutions with alanine (P189A, P234A, P285A, E441A, and G457A) enhanced the specific activity toward hexanoic acid compared to the wild-type
-
additional information
-
the replacement of Gly184, Arg870, and Trp978 by alanine does not result in soluble expression. Pro904 is located close to Trp978, and its substitution by Ala yields significantly less soluble protein. Replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity. Substitutions with alanine (P189A, P234A, P285A, E441A, and G457A) enhanced the specific activity toward hexanoic acid compared to the wild-type
-
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
additional information
-
hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Nocardia iowensis (Ni) resulting in hybrid enzymes: Mav(A)-Ni(PR), Mav(AP)-Ni(R), Ni(A)-Mav(PR), and Ni(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
-