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1.1.1.21: aldose reductase

This is an abbreviated version!
For detailed information about aldose reductase, go to the full flat file.

Word Map on EC 1.1.1.21

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 B1, 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, EC 1.1.1.139, Fibroblast growth factor regulated protein, FR-1 protein, GRE3, HAR, HRAR, isobutyraldehyde reductase, More, MVDP, NADPH dependent xylose reductase, 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 aldose reductase

Engineering

Engineering on EC 1.1.1.21 - aldose reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C298A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C298A/W219Y
C298S
C303D
introduction of residue from binding pocket of isoform ALR1 into ALR2, analysis of binding properties of inhibitors
C303S
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