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Literature summary for 1.1.1.431 extracted from

  • Terebieniec, A.; Chroumpi, T.; Dilokpimol, A.; Aguilar-Pontes, M.V.; Maekelae, M.R.; de Vries, R.P.
    Characterization of D-xylose reductase, XyrB, from Aspergillus niger (2021), Biotechnol. Rep., 30, e00610 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene xyrB or NRRL3_10868, phylogenetic and transcriptome analysis, phylogenetic tree, codon optimization of NRRL3_10868 and recombinant expression of His-tagged enzyme in Escherichia coli strain L21(DE3)pLysS Aspergillus niger

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information comparison of kinetic constants of NADPH dependent D-xylose reductases and other pentose reductases from different fungal species, overview Aspergillus niger
3.3
-
D-xylose recombinant enzyme, pH 7.0, 25°C Aspergillus niger
9.9
-
L-arabinose recombinant enzyme, pH 7.0, 25°C Aspergillus niger

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-xylose + NADPH + H+ Aspergillus niger
-
xylitol + NADP+
-
r

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain L21(DE3)pLysS by nickel affinity chromatography and ultrafiltration Aspergillus niger

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
9.2
-
purified recombinant enzyme, substrate L-arabitol, pH 9.6, 25°C Aspergillus niger
9.8
-
purified recombinant enzyme, substrate galactitol, pH 9.6, 25°C Aspergillus niger
11.3
-
purified recombinant enzyme, substrate xylitol, pH 9.6, 25°C Aspergillus niger
83.9
-
purified recombinant enzyme, substrate D-xylose, pH 7.0, 25°C Aspergillus niger
98.5
-
purified recombinant enzyme, substrate L-arabinose, pH 7.0, 25°C Aspergillus niger
136
-
purified recombinant enzyme, substrate D-galactose, pH 7.0, 25°C Aspergillus niger

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-galactose + NADPH + H+
-
Aspergillus niger galactitol + NADP+
-
r
D-xylose + NADPH + H+
-
Aspergillus niger xylitol + NADP+
-
r
L-arabinose + NADPH + H+
-
Aspergillus niger arabitol + NADP+
-
r
additional information specific activity analysis of Aspergillus niger XyrB shows that the enzyme is able to convert a wide range of sugars and polyols. XyrB shows the highest specific activity towards D-galactose, D-xylose and L-arabinose. The enzyme is also active with D-glucose, D-mannose, D-fructose, L-sorbose, D-ribose, D-arabinose, L-xylose, and L-rhamnose in the reductive reaction, and with ribitol, D-arabitol, sorbitol, mannitol, and glycerol in the oxidative reaction Aspergillus niger ?
-
-

Subunits

Subunits Comment Organism
? x * 33470, about, sequence calculation Aspergillus niger

Synonyms

Synonyms Comment Organism
D-xylose reductase
-
Aspergillus niger
More cf. EC 1.1.1.21 Aspergillus niger
NADPH dependent D-xylose reductase
-
Aspergillus niger
NRRL3_10868
-
Aspergillus niger
XyrB
-
Aspergillus niger

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Aspergillus niger

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 80
-
Aspergillus niger

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 50
-
Aspergillus niger

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
9.65
-
D-xylose recombinant enzyme, pH 7.0, 25°C Aspergillus niger
15.61
-
L-arabinose recombinant enzyme, pH 7.0, 25°C Aspergillus niger

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
sugar reduction assay at Aspergillus niger
9.6
-
sugar alcohol oxidation assay at Aspergillus niger

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Aspergillus niger
NADPH
-
Aspergillus niger

pI Value

Organism Comment pI Value Maximum pI Value
Aspergillus niger sequence calculation
-
6.09

General Information

General Information Comment Organism
evolution D-xylose reductase is a member of the aldo-keto reductase family. Its catalytic mechanism is likely conserved in other AKRs that contain these amino acids. Expression profiles for D-xylose reductase xyrA, D-xylose reductase xyrB and L-arabinose reductase larA from Aspergillus niger, overview Aspergillus niger
malfunction expression of gene xyrB is strongly reduced in the xlnR deletion strain on D-xylose and in the araR deletion strain on L-arabinose, indicating control of its expression by both regulators Aspergillus niger
metabolism D-xylose reductase is involved in D-xylose and L-arabinose conversion through the pentose catabolic pathway (PCP) in fungi Aspergillus niger
additional information the enzyme contains an aldo/keto reductase (AKR) motif between positions 22-277. The mechanism of catalysis in AKRs involves a catalytic tetrad, His, Tyr, Lys and Asp, in which the tyrosine hydroxyl group is the general acid and appears to be a proton relay from the histidine or lysine Aspergillus niger

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.58
-
L-arabinose recombinant enzyme, pH 7.0, 25°C Aspergillus niger
2.92
-
D-xylose recombinant enzyme, pH 7.0, 25°C Aspergillus niger