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 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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-xylose + NADPH + H+ | Aspergillus niger | - |
xylitol + NADP+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus niger | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain L21(DE3)pLysS by nickel affinity chromatography and ultrafiltration | Aspergillus niger |
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 | 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 | Comment | Organism |
---|---|---|
? | x * 33470, about, sequence calculation | Aspergillus niger |
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 Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Aspergillus niger |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 80 | - |
Aspergillus niger |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 50 | - |
Aspergillus niger |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
sugar reduction assay at | Aspergillus niger |
9.6 | - |
sugar alcohol oxidation assay at | Aspergillus niger |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Aspergillus niger | |
NADPH | - |
Aspergillus niger |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Aspergillus niger | sequence calculation | - |
6.09 |
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 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 |