1.1.1.21: aldehyde reductase

This is an abbreviated version, for detailed information about aldehyde reductase, go to the full flat file.

Reaction

alditol
+
NAD(P)+
=
aldose
+
NAD(P)H
+
H+

Synonyms

17betaHSD5, 20-alpha-HSD, 20-alpha-hydroxysteroid dehydrogenase, AdhA, AKR1B, AKR1B1, AKR1B10, AKR1B13, AKR1B14, AKR1B3, AKR1C3, AKR4C7, aldehyde reductase, alditol/NADP+ oxidoreductase, alditol: NADP+ 1-oxidoreductase, alditol:NAD(P)+1oxidoreductase, alditol:NADP 1-oxidoreductase, alditol:NADP oxidoreductase, aldo-keto reductase, aldo-keto reductase family 1 member B7, aldoketo reductase 1C3, aldose reductase, aldose reductase 2, aldose reductase-like, aldose reductase-like protein, aldose xylose reductase, ALDRXV4, ALR, ALR1, ALR2, AR, ARI, BAR, Fibroblast growth factor regulated protein, FR-1 protein, GRE3, HAR, HRAR, isobutyraldehyde reductase, More, MVDP, NADPH-aldopentose reductase, NADPH-aldose reductase, polyol dehydrogenase (NADP2), RLAR, small intestine reductase, TPN-polyol dehydrogenase, VAS deferens androgen-dependent protein, YqhD

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.21 aldehyde reductase

Engineering

Engineering on EC 1.1.1.21 - aldehyde reductase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C298A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C298A/W219Y
C303D
-
introduction of residue from binding pocket of isoform ALR1 into ALR2, analysis of binding properties of inhibitors
F115Y
-
stable and active
F121P
-
introduction of residue from binding pocket of isoform ALR1 into ALR2, analysis of binding properties of inhibitors
G213P
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G213S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H110A
-
mutant enzyme
H110Q
-
mutant enzyme
K77M
-
mutant enzyme
L300A
-
introduction of residue from binding pocket of isoform ALR1 into ALR2, analysis of binding properties of inhibitors
L301M
-
introduction of residue from binding pocket of isoform ALR1 into ALR2, analysis of binding properties of inhibitors
R268A
-
site-directed mutagenesis, the mutant shows similar kinetics for the aldehyde substrate, but highly reduced affinity for the nucleotide cofactor, and reduced activity compared to the wild-type enzyme
R293A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S210A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S214A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S226A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S302R
-
introduction of residue from binding pocket of isoform ALR1 into ALR2, analysis of binding properties of inhibitors
T113A
-
stable and active
T113A/F115Y
-
10fold decrease in kcat value, does not bind to inhibitor (5-chloro-2-[(4-cyanobenzyl)carbamoyl]phenoxy)acetic acid
T113V
-
inhibition constants and vibrational frequencies of inhibitor (5-chloro-2-[(4-cyanobenzyl)carbamoyl]phenoxy)acetic acid in the active site
V301L
-
site-directed mutagenesis
V47I
-
introduction of residue from binding pocket of isoform ALR1 into ALR2, analysis of binding properties of inhibitors
W219A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W219E
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y48F
-
mutant enzyme
Y48S
-
mutant enzyme
C298S
-
similar sensitivity against Cu2+ as wild-type
additional information