1.1.1.10: L-xylulose reductase

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

Reaction

xylitol
+
NADP+
=
L-xylulose
+
NADPH
+
H+

Synonyms

DCXR, dicarbonyl/L-xylulose reductase, L-xylulose reductase, LXR3, More, NAD(P)H-dependent xylose reductase, NADP(+)-dependent xylitol dehydrogenase, P31h, P34H, reductase, L-xylulose, XDH, XR, xylitol dehydrogenase, xylose reductase

ECTree

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

Engineering

Engineering on EC 1.1.1.10 - L-xylulose reductase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N107D
-
site-directed mutagenesis, active site residue mutant, inactive
N107L
-
site-directed mutagenesis, active site residue mutant, inactive
D238E
-
site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation
D238E/L242W
-
site-directed mutagenesis, mutation leads to complete prevention of cold inactivation, mutant exists in tetrameric form at low temperature
D238E/L242W/T244C
-
site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
L242W
-
site-directed mutagenesis, mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
L242W/T244C
-
site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature
T244C
-
site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation
K153M
-
site-directed mutagenesis, active site mutant, complete loss of activity
N190V
-
site-directed mutagenesis, altered activity
N190V/W191S
-
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity
N190V/W191S/Q137M/L143F/H146L
-
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows high 3-ketosteroid reductase activity
Q137M
-
site-directed mutagenesis, altered activity, stable against cold inactivation
Q137M/F241L
-
site-directed mutagenesis, altered activity, sensitive to cold inactivation like the wild-type enzyme
Q137M/L143F
-
site-directed mutagenesis, increased Km for L-xylulose compared to the wild-type
Q137M/L143F/H146L
-
site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows 3-ketosteroid reductase activity
S136A
-
site-directed mutagenesis, active site mutant, complete loss of activity
Y149F
-
site-directed mutagenesis, active site mutant, complete loss of activity
D207/I208R/F209S
-
kcat/Km of mutant enzyme for NAD+ dropps 15fold compared with the native enzyme, kcat/Km for NADP+ increases up to 4100fold
S96C/S99C/Y102C/D207A/I208R/F209S
-
mutation produces a further 4fold improvement in the kcat/Km for NADP+ compared to mutant enzyme D207/I208R/F209S
additional information