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Literature summary for 1.1.1.430 extracted from

  • Cui, Z.; Mao, Y.; Zhao, Y.; Chen, C.; Tang, Y.; Chen, T.; Ma, H.; Wang, Z.
    Concomitant cell-free biosynthesis of optically pure D-(-)-acetoin and xylitol via a novel NAD+ regeneration in two-enzyme cascade (2018), J. Chem. Technol. Biotechnol., 93, 3444-3451 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Yamadazyma tenuis

Protein Variants

Protein Variants Comment Organism
additional information a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH) Yamadazyma tenuis

Inhibitors

Inhibitors Comment Organism Structure
additional information no substrate inhibition by D-xylose Yamadazyma tenuis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
NADH pH 6.5, 42°C, recombinant His-tagged enzyme Yamadazyma tenuis
29.8
-
D-xylose pH 6.5, 42°C, recombinant His-tagged enzyme Yamadazyma tenuis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-xylose + NADH + H+ Yamadazyma tenuis
-
xylitol + NAD+
-
r
D-xylose + NADPH + H+ Yamadazyma tenuis
-
xylitol + NADP+
-
r

Organism

Organism UniProt Comment Textmining
Yamadazyma tenuis O74237
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration Yamadazyma tenuis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.12
-
purified recombinant His-tagged enzyme, pH 6.5, 42°C Yamadazyma tenuis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-xylose + NADH + H+
-
Yamadazyma tenuis xylitol + NAD+
-
r
D-xylose + NADPH + H+
-
Yamadazyma tenuis xylitol + NADP+
-
r

Subunits

Subunits Comment Organism
? x * 39000, about, recombinant His-tagged enzyme, SDS-PAGE, x * 36000, about, sequence calculation Yamadazyma tenuis

Synonyms

Synonyms Comment Organism
CT-XR
-
Yamadazyma tenuis
NAD(P)H-dependent D-xylose reductase UniProt Yamadazyma tenuis
NADH-dependent XR
-
Yamadazyma tenuis
XYL1
-
Yamadazyma tenuis
xylose reductase
-
Yamadazyma tenuis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
42
-
-
Yamadazyma tenuis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
27 57 activity range Yamadazyma tenuis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37 42 purified recombinant His-tagged enzyme CT-XR, unstable at 42°C, complete inactivation after 6 h, CT-XR is more stable at 37°C maintaining 37.4% of initial activity after 6 h Yamadazyma tenuis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
11.42
-
NADH pH 6.5, 42°C, recombinant His-tagged enzyme Yamadazyma tenuis
11.42
-
D-xylose pH 6.5, 42°C, recombinant His-tagged enzyme Yamadazyma tenuis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
Yamadazyma tenuis

pH Range

pH Minimum pH Maximum Comment Organism
5.5 9 activity range Yamadazyma tenuis

Cofactor

Cofactor Comment Organism Structure
additional information most XRs are NADPH-dependent rather than NADH-dependent. CT-XR from Candida tenuis shows a similar preference for both NADH and NADPH Yamadazyma tenuis
NAD+
-
Yamadazyma tenuis
NADH
-
Yamadazyma tenuis
NADP+
-
Yamadazyma tenuis
NADPH
-
Yamadazyma tenuis

General Information

General Information Comment Organism
physiological function most XRs are NADPH-dependent rather than NADH-dependent. CT-XR from Candida tenuis shows a similar preference for both NADH and NADPH, and has been reported to efficiently produce xylitol in vitro Yamadazyma tenuis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.383
-
D-xylose pH 6.5, 42°C, recombinant His-tagged enzyme Yamadazyma tenuis
285.5
-
NADH pH 6.5, 42°C, recombinant His-tagged enzyme Yamadazyma tenuis