1.1.1.9: D-xylulose reductase

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

Reaction

xylitol
+
NAD+
=
D-xylulose
+
NADH
+
H+

Synonyms

2,3-cis-polyol(DPN) dehydrogenase (C3-5), erythritol dehydrogenase, GmXDH, NAD-dependent xylitol dehydrogenase, pentitol-DPN dehydrogenase, PsXDH, reductase, D-xylulose, slSDH, XDH, XDH-Y25, xdhA, XL2, XYL2, xylitol dehydrogenase, xylitol-2-dehydrogenase

ECTree

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

Engineering

Engineering on EC 1.1.1.9 - D-xylulose reductase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D202A/L203R/V204S/E205P/S206R
-
site-directed mutagenesis, introduction of multiple site-directed mutations in the coenzyme-binding pocket of Galactocandida mastotermitis XDH to enable activity with NADP+, which is lacking in the wild-type enzyme, genetic metabolic engineering for improvement of xylose metabolism and fermentation in wild-type Saccharomyces cerevisiae strains, which are not able to naturally metabolize D-xylulose, overview
E154C
-
mutant bearing a disrupted Zn2+ binding site: purified preparations show a variable Zn2+ (0.10-0.40 atom/subunit), mutant exhibits a constant catalytic Zn2+ centre activity and does not require exogenous Zn2+ for activity or stability. E154C retains 0.019% and 0.74% of wild-type catalytic efficiency (kcat/Km (sorbitol): 7800/Msec and kcat:161/sec) for NAD+-dependent oxidation of sorbitol at 25°C respectively. The pH profile of kcat/Ksorbitol for E154C decreases below an apparent pK of 9.1, reflecting a shift in pK by about +1.7-1.9 pH units compared with the corresponding pH profiles for wild-type. IC50 (ZnSO4): 0.005 mM
synthesis
-
use of enzyme in a process for producing xylitol from D-glucose
D38S/M39R
the mutant enzyme is able to exclusively use NADP+, with no loss of activity
D205A/I206R
D207A
-
kcat/Km for NAD+ is 3.6fold lower than wild-type value, kcat/Km for NADP+ is 4.3fold higher than wild-type value
D207A/F209S
-
kcat/Km for NAD+ is 2.2fold lower than wild-type value, kcat/Km for NADP+ is 745fold higher than wild-type value
D207A/I208R
-
kcat/Km for NAD+ is 2.5fold lower than wild-type value, kcat/Km for NADP+ is 229fold higher than wild-type value
D207A/I208R/F209S
D207A/I208R/F209S/N211R
-
kcat/Km for NAD+ is 32.9fold lower than wild-type value, kcat/Km for NADP+ is 4292fold higher than wild-type value, increased thermostability
D207A/I208R/F209T
-
kcat/Km for NAD+ is 2.4fold lower than wild-type value, kcat/Km for NADP+ is 4754fold higher than wild-type value
D207A/I208R/F209Y
-
kcat/Km for NAD+ is 6.9fold lowerthan wild-type value, kcat/Km for NADP+ is 788fold higher than wild-type value
F209S
-
kcat/Km for NAD+ is 1.9fold lower than wild-type value, kcat/Km for NADP+ is 31.4fold higher than wild-type value
I208R
-
kcat/Km for NAD+ is nearly identical to wild-type value, kcat/Km for NADP+ is 44fold higher than wild-type value
I208R/F209S
-
kcat/Km for NAD+ is 30.7fold lower than wild-type value, kcat/Km for NADP+ is 1.5fold higher than wild-type value
N211R
-
kcat/Km for NAD+ is 1.1fold lower than wild-type value, kcat/Km for NADP+ is 7.6fold higher than wild-type value
S96C/S99C/Y102C
-
specific activity (U/min): 1440, half denaturation temperature T1/2 (°C): 46.1, thermal transition temperature Tcd (°C): 47.5
S96C/S99C/Y102C/D207A/I208R/F209S
S96C/S99C/Y102C/D207A/I208R/F209S/N211R
-
kcat/Km for NAD+ is 26.5fold lower than wild-type value, kcat/Km for NADP+ is 16154fold higher than wild-type value
S96C/S99C/Y102C/E101F
-
specific activity (U/min): 1550, half denaturation temperature T1/2 (°C): 50.9, thermal transition temperature Tcd (°C): 50.5
S96C/S99C/Y102C/F98R
-
specific activity (U/min): 1510, half denaturation temperature T1/2 (°C): 53.1, thermal transition temperature Tcd (°C): 51.7
S96C/S99C/Y102C/F98R/E101F
-
specific activity (U/min): 1620, half denaturation temperature T1/2 (°C): 56.0, thermal transition temperature Tcd (°C): 53.8
S96C/S99C/Y102C/H112D
-
specific activity (U/min): 1360, half denaturation temperature T1/2 (°C): 44.0, thermal transition temperature Tcd (°C): 47.0
S96C/S99C/Y102C/P95S
-
specific activity (U/min): 1220, half denaturation temperature T1/2 (°C): 37.4, thermal transition temperature Tcd (°C): 43.5
S96C/S99CY102C
-
kcat/Km for NAD+ is 1.1fold lower than wild-type value, kcat/Km for NADP+ is 8.8fold higher than wild-type value
additional information