Information on EC 1.1.1.9 - D-xylulose reductase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.9
-
RECOMMENDED NAME
GeneOntology No.
D-xylulose reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
xylitol + NAD+ = D-xylulose + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
degradation of sugar alcohols
-
-
Pentose and glucuronate interconversions
-
-
Metabolic pathways
-
-
xylitol degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
xylitol:NAD+ 2-oxidoreductase (D-xylulose-forming)
Also acts as an L-erythrulose reductase.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-16-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Y25
-
-
Manually annotated by BRENDA team
strain Y25
-
-
Manually annotated by BRENDA team
a DELTApyrG strain developed from strain KBN616
SwissProt
Manually annotated by BRENDA team
strain F-3
-
-
Manually annotated by BRENDA team
strain F-3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
CBS 4435
-
-
Manually annotated by BRENDA team
CBS 4435
-
-
Manually annotated by BRENDA team
strain Y-456
-
-
Manually annotated by BRENDA team
isolated from soil, China
-
-
Manually annotated by BRENDA team
strain Y-488
-
-
Manually annotated by BRENDA team
strain Y-488
-
-
Manually annotated by BRENDA team
strain Y-1017
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain CFN42
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain Y-1632
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
strictly NADPH-dependent XR with mutated strict NADP+-dependent XDH are more effective in increasing bioethanol production and decreasing xylitol accumulation than the NAD+-dependent wild-type XDH, overview
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-arabitol + NAD+
?
show the reaction diagram
-
-
-
-
?
D-arabitol + NAD+
? + NADH + H+
show the reaction diagram
D-fructose + NADH + H+
D-sorbitol + NAD+
show the reaction diagram
D-fructose + NADH + H+
sorbitol + NAD+
show the reaction diagram
D-iditol + NAD+
?
show the reaction diagram
D-mannitol + NAD+
?
show the reaction diagram
D-mannitol + NAD+
? + NADH + H+
show the reaction diagram
8% of the activity with xylitol
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
D-ribitol + NAD+
D-ribulose + NADH
show the reaction diagram
D-ribulose + NADH
D-ribitol + NAD+
show the reaction diagram
-
-
-
r
D-ribulose + NADH + H+
?
show the reaction diagram
-
-
-
?
D-sorbitol + NAD+
? + NADH + H+
show the reaction diagram
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
D-sorbitol + NAD+
L-sorbose + NADH + H+
show the reaction diagram
D-sorbitol + NAD+ |
D-fructose + NADH + H+
show the reaction diagram
D-threitol + NAD+
?
show the reaction diagram
D-xylitol + NAD+
D-xylulose + NADH
show the reaction diagram
D-xylulose + NAD+
xylitol + NADH + H+
show the reaction diagram
-
-
-
-
r
D-xylulose + NADH + H+
D-xylitol + NAD+
show the reaction diagram
D-xylulose + NADH + H+
xylitol + NAD+
show the reaction diagram
dihydroxyacetone + NADH
glycerol + NAD+
show the reaction diagram
-
-
-
-
-
erythritol + NAD+
? + NADH + H+
show the reaction diagram
0.77% of the activity with xylitol
-
-
?
erythritol + NAD+
L-erythrulose + NADH
show the reaction diagram
-
-
-
r
galactitol + NAD+
? + NADH + H+
show the reaction diagram
0.98% of the activity with xylitol
-
-
?
glycerol + NAD+
?
show the reaction diagram
L-arabinitol + NAD+
? + NADH + H+
show the reaction diagram
21% of the activity with xylitol
-
-
?
L-arabitol + NAD+
?
show the reaction diagram
L-arabitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
L-erythrulose + NADH
erythritol + NAD+
show the reaction diagram
L-iditol + NAD+
?
show the reaction diagram
-
-
-
-
?
L-sorbose + NADH + H+
?
show the reaction diagram
-
-
-
?
L-threitol + NAD+
? + NADH + H+
show the reaction diagram
L-xylulose + NADH
L-xylitol + NAD+
show the reaction diagram
-
-
-
-
?
meso-erythritol + NAD+
? + NADH + H+
show the reaction diagram
ribitol + NAD+
?
show the reaction diagram
ribitol + NAD+
? + NADH + H+
show the reaction diagram
40% of the activity with xylitol
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
Xylitol + NAD+
?
show the reaction diagram
xylitol + NAD+
D-xylose + NADH + H+
show the reaction diagram
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
xylitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
xylitol + NADP+
D-xylulose + NADPH + H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-xylulose + NADH + H+
xylitol + NAD+
show the reaction diagram
Xylitol + NAD+
?
show the reaction diagram
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
1 mM, 18% of the activity with Mg2+
Co2+
1 mM, 38% of the activity with Mg2+
Cu2+
1 mM, 51% of the activity with Mg2+
KCl
-
slight activation
MnCl2
-
10 mM, increase of activity by 100%
NaCl
-
activation
NH4Cl
-
activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
9.2% residual activity at 1 mM
Ca2+
complete inhibition at 1 mM
CaCl2
Cd2+
complete inhibition at 1 mM
Co2+
6.8% residual activity at 1 mM
CuSO4
cysteine
-
at 294 mM
D-xylulose
Fe3+
18% residual activity at 1 mM
HgCl2
-
complete inhibition
iodoacetate
-
complete inhibition
Mg2+
complete inhibition at 1 mM
MgCl2
-
10 mM, 4% inhibition
MgSO4
complete inhibition at 1 mM
Mn2+
8.4% residual activity at 1 mM
Na+
complete inhibition at 1 mM
NaCl
-
at 160 mM
NH4Cl
-
at 310 mM
Ni2+
11.3% residual activity at 1 mM
NiCl2
-
1 mM, complete inhibition
Pb(CH3COO)2
-
-
Pb2+
complete inhibition at 1 mM
PCMB
-
complete inhibition
ZnSO4
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
D-glucose
-
induces activity
D-Lyxose
-
induces activity
D-xylose
glycerol
-
induces activity
glycine
-
slight activation
GSH
-
activation
L-arabinose
-
induces activity
Sodium acetate
-
1 g/l in reaction medium, about 15% increase of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19.8
D-fructose
at pH 7.0 and 30C
0.7
D-ribulose
35C, pH 7.5, native enzyme
4 - 31.5
D-sorbitol
12 - 94
D-xylitol
0.66 - 43.9
D-xylulose
31.1
L-arabitol
at pH 7.0 and 30C
0.9
L-sorbose
35C, pH 7.5, native enzyme
0.027 - 500
NAD+
0.037 - 36.4
NADH
0.0205 - 170
NADP+
15.8 - 496
ribitol
0.16 - 785
sorbitol
0.039 - 175.5
xylitol
13.8
xylulose
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
920
D-fructose
-
25C, pH 7.5, Tris-HCl
74
D-ribulose
35C, pH 7.5, native enzyme
8.28 - 528
D-sorbitol
302.9 - 1800
D-xylulose
3.35
L-arabitol
at pH 7.0 and 30C
216
L-sorbose
35C, pH 7.5, native enzyme
0.052 - 30.33
NAD+
0.017 - 210
NADP+
4.5
ribitol
at pH 7.0 and 30C
1.19 - 161
sorbitol
1.12 - 2644
xylitol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.39
D-sorbitol
at pH 7.0 and 30C
0.11
L-arabitol
at pH 7.0 and 30C
0.03 - 32.36
NAD+
0.018 - 0.56
NADP+
0.29
ribitol
at pH 7.0 and 30C
1.12
xylitol
at pH 7.0 and 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
D-xylulose
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005
ZnSO4
Candida sp. HA 167
-
value identical for wildtype and for mutant E154C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.08
crude enzyme, at pH 7.0 and 30C
0.15 - 0.18
-
depending on nitrogen source in culture medium
0.76
-
purified native enzyme, pH 11.0, 30C, substrate meso-erythritol
2.16
-
specific activity of recombinant Saccharomyces cerevisiae strain TMB3057
4.9
after purification, at pH 7.0 and 30C
6.74
-
purified native enzyme, pH 11.0, 30C, substrate D-arabitol
12.89
-
purified native enzyme, pH 11.0, 30C, substrate D-mannitol
102.5
-
purified native enzyme, pH 11.0, 30C, substrate xylitol
113
-
substrate D-xylitol, pH 10, 30C
156.1
-
purified native enzyme, pH 11.0, 30C, substrate D-sorbitol
180.4
-
purified native enzyme, pH 5.0, 30C, substrate D-fructose
220
-
substrate D-sorbitol, pH 10, 30C
250
-
pH 8.4, 30C
564
-
purified native enzyme, pH 5.0, 30C, substrate D-xylulose
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
reduction reaction
6.7
-
reduction of erythrulose
7.2
-
xylitol formation
9.1 - 10
-
substrate oxidation, plateau
10.5 - 11
-
oxidation reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 11
8.7 - 10.5
-
about 80% of maximal oxidation activity at pH 8.7 and 10.5
9 - 10
-
fully active
9 - 12
-
oxidation reaction, activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 55
activity range, inactive at 60C
20 - 50
-
20C: about 50% of maximal activity, 50C: about 50% of maximal activity
20 - 55
-
activity range, profile overview
25 - 40
-
the oxidation and reduction activities of the enzyme on the condition of temperatures ranging from 25C to 40C are over 80%
35 - 68
-
about half-maximal activity at 35C and 68C
45 - 55
the enzyme partially loses its activity at 45-55C and also completely loses activity at temperatures greater than 60C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
-
isoelectric focusing
6
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
the organism grows on rice straw hemicellulosic hydrolysate, as the only source of nutrient, optimization of culture conditions for production of xylitol from D-xylose, xylitol dehydrogenase remains constant, whereas the level of xylose reductase decreases when the initial xylose concentration is increased from 30 to 70 g/l, development of enzyme activities, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
x * 27800, deduced from genen sequence, x * 27000, SDS-PAGE
27800
-
x * 27800, deduced from genen sequence, x * 27000, SDS-PAGE
28000
-
x * 28000, SDS-PAGE
34000
4 * 35858, calculated, 4 * 34000, SDS-PAGE
35858
4 * 35858, calculated, 4 * 34000, SDS-PAGE
36500
x * 38197, deduced from gene sequence, x * 36500, SDS-PAGE
38000
-
4 * 38000, SDS-PAGE
38197
x * 38197, deduced from gene sequence, x * 36500, SDS-PAGE
40300
2 * 40300, calculated from sequence
40400
-
2 * 40400 + 2 * 41800, SDS-PAGE
41800
-
2 * 40400 + 2 * 41800, SDS-PAGE
48000
-
2 * 48000, SDS-PAGE
72000
native enzyme, gel filtration, non-denaturing PAGE
80000
recombinant enzyme, gel filtration, non-denaturing PAGE
82000
-
gel filtration
87000
gel filtration
94000
-
PAGE
120000
-
gel filtration
130000
-
PAGE
135000
gel filtration
142000
-
PAGE
160000
172000
-
gel filtration
195000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homopentamer
homotetramer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of the holoenzyme to 1.9 A resolution
multi-template homology modeling. The structural model of XDH obtained consists of a classical alpha/beta Rossmann fold pattern commonly found in the MDR family, which is organized into two beta-barrel domains, the coenzyme-binding residues 163-300 and catalytic residues 1-162, 301-364
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
-
24 h, fully stable
655092
6.8 - 7.4
-
90% of maximal activity retained at pH 6.8 and 7.4 at 2C
246415
7
-
24 h stable at 2C
246415
7 - 9
-
stable
246421
7.2 - 7.9
stable
667227
8 - 10
-
4C, 60 min, stable
686433
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 40
-
10 min, 2.5 mM NAD+, stable
20
-
at room temperature, the enzyme is inactivated within 2 days
25
-
and below stable
30
-
1 h, completely stable
30 - 45
the enzyme exhibits activities of approximately 81% and 51% after being incubated at 30C and 35C, respectively, for 30 min. The enzyme completely loses its activity at temperatures greater than 45C
40
half-life 120 min
45 - 50
approximately 92% and 70% activities remain following incubations at 45 and 50C, respectively. The enzyme completely loses its activity above 60C
53.1
half denaturation temperature
additional information
-
wild-type: half denaturation temperature T1/2 (C): 35.2, thermal transition temperature Tcd (C): 43.0
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes during purification
-
30C, pH 6-7, 24 h, fully stable
-
crude water extract from liver acetone-powder unstable
-
EDTA stabilizes during purification
-
freezing/thawing inactivates, 8 cycles lead to 89% loss of activity and 11 cycles to complete inactivation
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
-
stable to precipitation with 50% v/v
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, acetone precipitate stable for weeks
-
-15C, 60% loss of activity after 1 month
-
-20C, stable with 50% v/v glycerol
-
-2C, purified stable for a month
-
0C, 34% loss of activity within a month
-
0C, partially purified stable for weeks
-
2C, 90% of maximal activity retained at pH 6.8 and 7.4 after 24 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, DEAE Toyopearl chromatography, phenyl Toyopearl chromatography, Mono Q chromatography, Superdex 200 gel filtration, and Reactive Red column chromatography
DEAEToyopearl 650 M column chromatography, butyl-Toyopearl 650 M column chromatography, MonoQ column chromatography, and Superdex 200 gel filtration; native enzyme by ammonium sulfate fractionation, anion exchange chromatography, hydrophobic interation chromatography, and another different step of anion exchange chromatography, followed by gel filtration. Recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
native enzyme 469fold from sstrain NH-10 by ammonium sulfate fractionation, two different steps of anion exchange chromatography, and gel filtration
-
Ni-NTA column chromatography and Sephacryl S-300 gel filtration
-
optimized extraction by cetyl trimethyl ammonium bromide reversed micelles
-
partial
recombinant enzmye
recombinant enzyme
using affinity chromatography and preparative gel filtration
-
using Ni-NTA chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a His-tagged fusion protein in Escherichia coli
-
expressed in Candida glycerinogenes
-
expressed in Candida glycerinogenes strain WL2002-5
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli JM 109
-
expressed in Saccharomyces cerevisiae strain DX23; recombinant overexpression in Saccharomyces cerevisiae strain D452-2, coexpression with Saccharomyces cerevisiae enzymes/genes xylulokinase XKS1, and xylose reductase XYL1 or XYL3, aldose reductase GRE3. Xylose fermentation efficiency of a strain overexpressing GRE3 is dramatically increased by high expression levels of XYL2
expressed in transketolase-deficient Saccharomyces cerevisiae strain (W303/tkl1 tkl2/2C)
-
expression in Escherichia coli
expression of the engineered D202A/L203R/V204S/E205P/S206R mutant enzyme fron Galactocandida mastotermitis with altered cofactor specificity, co-expression with a mutant NADPH-specific xylulose reductase from Candida tenuis in Saccharomyces cerevisiae, the transformed strain shows up to 50% decreased glycerol yield without increase in ethanol during xylose fermentation, overview
-
gene xdhA, coexpression of gene xdhA and cofactor regeneration enzyme, i.e. glucose dehydrogenase gene gdh from Bacillus subtilis, in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
-
gene xyl2, DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain JM109, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
genes XYL2 (D207A/I208R/F209S) and XYL2 (S96C/S99C/Y102C/D207A/I208R/F209S) are introduced into Saccharomyces cerevisiae, which already contain the Pichia stipitis XYL1 gene (encoding xylose reductase) and the endogenously overexpressed XKS1 gene (encoding xylulokinase)
-
overexpression in Saccharomyces cerevisiae
-
overexpression of the enzyme in Saccharomyces cerevisiae strain CEN.PK 113-7D under control of the constitutive TDH3 promoter, co-expression with xylose reductase from Candida tenuis
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression levels are increased with accumulation of xylitol
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 25C 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