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Literature summary for 1.1.1.9 extracted from

  • Fan, E.S.; Lu, K.W.; Wen, R.C.; Shen, C.R.
    Photosynthetic reduction of xylose to xylitol using cyanobacteria (2020), Biotechnol. J., 15, e1900354 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene xyl2, recombinant expression of the enzyme in Synechococcus elongatus strain PCC7942, functional co-expression with a xylose transporter from Escherichia coli, Ec-XylE Scheffersomyces stipitis

Protein Variants

Protein Variants Comment Organism
additional information efficient uptake and reduction of xylose photoautotrophically in Synechococcus elongatus strain PCC7942 are demonstrated upon introduction of an effective xylose transporter from Escherichia coli (Ec-XylE) and the NADPH-dependent xylose reductase from Candida boidinii (Cb-XR). Simultaneous activation of xylose uptake and matching of cofactor specificity enables an average xylitol yield of 0.9 g/g xylose and a maximum productivity of about 0.15 g/l/day/OD with increased level of xylose supply. High-density conversion of xylose to xylitol using concentrated resting cells further pushes the titer of xylitol formation to 33 g/l in six days with 85% of maximum theoretical yield. Comparison of the efficiencies of the two routes for xylitol biosynthesis, detailed overview Scheffersomyces stipitis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Scheffersomyces stipitis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-xylulose + NADH + H+ Scheffersomyces stipitis
-
xylitol + NAD+
-
r
D-xylulose + NADH + H+ Scheffersomyces stipitis NRRL Y-11545
-
xylitol + NAD+
-
r
D-xylulose + NADH + H+ Scheffersomyces stipitis NBRC 10063
-
xylitol + NAD+
-
r
D-xylulose + NADH + H+ Scheffersomyces stipitis ATCC 58785
-
xylitol + NAD+
-
r

Organism

Organism UniProt Comment Textmining
Scheffersomyces stipitis P22144 Pichia stipitis
-
Scheffersomyces stipitis ATCC 58785 P22144 Pichia stipitis
-
Scheffersomyces stipitis NBRC 10063 P22144 Pichia stipitis
-
Scheffersomyces stipitis NRRL Y-11545 P22144 Pichia stipitis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
enzyme activities in different engineered Synechococcus elongatus strain PCC7942 variants, overview Scheffersomyces stipitis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-xylulose + NADH + H+
-
Scheffersomyces stipitis xylitol + NAD+
-
r
D-xylulose + NADH + H+
-
Scheffersomyces stipitis NRRL Y-11545 xylitol + NAD+
-
r
D-xylulose + NADH + H+
-
Scheffersomyces stipitis NBRC 10063 xylitol + NAD+
-
r
D-xylulose + NADH + H+
-
Scheffersomyces stipitis ATCC 58785 xylitol + NAD+
-
r

Synonyms

Synonyms Comment Organism
NADH-dependent XDH
-
Scheffersomyces stipitis
NADH-dependent xylitol dehydrogenase
-
Scheffersomyces stipitis
Ps-XDH
-
Scheffersomyces stipitis
XYL2
-
Scheffersomyces stipitis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
in vivo assay at Scheffersomyces stipitis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Scheffersomyces stipitis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Scheffersomyces stipitis
NADH
-
Scheffersomyces stipitis

General Information

General Information Comment Organism
metabolism biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR, EC 1.1.1.307), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway Scheffersomyces stipitis