1.2.1.4: aldehyde dehydrogenase (NADP+)
This is an abbreviated version!
For detailed information about aldehyde dehydrogenase (NADP+), go to the full flat file.
Word Map on EC 1.2.1.4
-
1.2.1.4
-
voltage-gated
-
kvbeta1
-
voltage-dependent
-
pore-forming
-
juxtaparanodal
-
paranodal
-
caspr
-
medicine
-
retinaldehyde
-
synthesis
- 1.2.1.4
-
voltage-gated
-
kvbeta1
-
voltage-dependent
-
pore-forming
-
juxtaparanodal
-
paranodal
-
caspr
- medicine
- retinaldehyde
- synthesis
Reaction
Synonyms
AKR1A4, ALD6, aldehyde dehydrogenase (NADP+), aldehyde dehydrogenase 3A1, aldehyde dehydrogenase 6, aldehyde reductase, ALDH, ALDH1, ALDH1F1, ALDH3A1, ALDH6, AlDHPyr1147, dehydrogenase, aldehyde (nicotinamide adenine dinucleotide phosphate), Kvbeta2, NADP dependent aldehyde dehydrogenase, NADP+-dependent Ald6, NADP-acetaldehyde dehydrogenase, NADP-dependent aldehyde dehydrogenase, Seegmiller enzyme, Ta0439, TaAlDH
ECTree
Advanced search results
Engineering
Engineering on EC 1.2.1.4 - aldehyde dehydrogenase (NADP+)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
A200E
-
the mutant shows strongly reduced activity (50fold) with NADP+ compared to the wild type enzyme
A200E/V210Q
-
the mutant shows strongly reduced activity (250fold) with NADP+ and about 3fold increased activity with NAD+ compared to the wild type enzyme
D176S
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
D176S/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
D176S/S206K
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
D176S/S206K/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
D176S/S206K/M262I/W271Y/W275V
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
F34M/Y399C/S405N
site-directed mutagenesis, crystal structure analysis
M262I
site-directed mutagenesis, the mutation results in 30% higher activity with NAD+ compared to wild-type enzyme, the surface mutation M262I has influence on the solubility
S175E
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/D176S
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/D176S/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/D176S/S206K
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/D176S/S206K/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/S206K
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S175E/S206K/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S206K
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
S206K/M262I
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
D176S
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
F34M/Y399C/S405N
-
site-directed mutagenesis, crystal structure analysis
-
S175E
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
S206K
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
D176S
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
F34M/Y399C/S405N
-
site-directed mutagenesis, crystal structure analysis
-
S175E
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
S206K
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
D176S
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
F34M/Y399C/S405N
-
site-directed mutagenesis, crystal structure analysis
-
S175E
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
S206K
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
D176S
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
F34M/Y399C/S405N
-
site-directed mutagenesis, crystal structure analysis
-
S175E
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
S206K
-
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme
-
additional information
construction of an enzyme mutant with deletion of the catalytic residues
additional information
-
construction of an enzyme mutant with deletion of the catalytic residues
-
additional information
random mutagenesis approach for the aldehyde dehydrogenase of Thermoplasma acidophilum (TaALDH) to increase volumetric activity and slightly improve NAD+ acceptance. Roughly 450 mutants do not show any activity, and around 400 mutants have an activity below the template (M33) threshold. Saturation mutagenesis of the residues at the entrance of the substrate pocket can eliminate substrate inhibition. Molecular dynamics simulations show a significant gain of flexibility at the cofactor binding site for the final variant
additional information
-
random mutagenesis approach for the aldehyde dehydrogenase of Thermoplasma acidophilum (TaALDH) to increase volumetric activity and slightly improve NAD+ acceptance. Roughly 450 mutants do not show any activity, and around 400 mutants have an activity below the template (M33) threshold. Saturation mutagenesis of the residues at the entrance of the substrate pocket can eliminate substrate inhibition. Molecular dynamics simulations show a significant gain of flexibility at the cofactor binding site for the final variant
-
additional information
-
random mutagenesis approach for the aldehyde dehydrogenase of Thermoplasma acidophilum (TaALDH) to increase volumetric activity and slightly improve NAD+ acceptance. Roughly 450 mutants do not show any activity, and around 400 mutants have an activity below the template (M33) threshold. Saturation mutagenesis of the residues at the entrance of the substrate pocket can eliminate substrate inhibition. Molecular dynamics simulations show a significant gain of flexibility at the cofactor binding site for the final variant
-
additional information
-
random mutagenesis approach for the aldehyde dehydrogenase of Thermoplasma acidophilum (TaALDH) to increase volumetric activity and slightly improve NAD+ acceptance. Roughly 450 mutants do not show any activity, and around 400 mutants have an activity below the template (M33) threshold. Saturation mutagenesis of the residues at the entrance of the substrate pocket can eliminate substrate inhibition. Molecular dynamics simulations show a significant gain of flexibility at the cofactor binding site for the final variant
-
additional information
-
random mutagenesis approach for the aldehyde dehydrogenase of Thermoplasma acidophilum (TaALDH) to increase volumetric activity and slightly improve NAD+ acceptance. Roughly 450 mutants do not show any activity, and around 400 mutants have an activity below the template (M33) threshold. Saturation mutagenesis of the residues at the entrance of the substrate pocket can eliminate substrate inhibition. Molecular dynamics simulations show a significant gain of flexibility at the cofactor binding site for the final variant
-