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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

Reaction

an aldehyde
+
NADP+
+
H2O
=
a carboxylate
+
NADPH
+
H+

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

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.4 aldehyde dehydrogenase (NADP+)

Engineering

Engineering on EC 1.2.1.4 - aldehyde dehydrogenase (NADP+)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R197E
-
very low activity
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