Activating Compound | Comment | Organism | Structure |
---|---|---|---|
bovine serum albumin | 0.1% (w/v), 10-15% activation | Yamadazyma tenuis | |
Triton X-100 | 0.1% (w/v), 10-15% activation | Yamadazyma tenuis | |
Tween-20 | 0.1% (w/v), 10-15% activation | Yamadazyma tenuis | |
Tween-80 | 0.1% (w/v), 10-15% activation | Yamadazyma tenuis |
General Stability | Organism |
---|---|
stable enzyme at 25°C in phosphate and Tris buffer of various ionic strengths between pH 6.0 and 7.0 | Yamadazyma tenuis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
AMP | 2 mM, completely abolishes D-xylose reduction | Yamadazyma tenuis | |
ATP | 2 mM, completely abolishes D-xylose reduction, competitive | Yamadazyma tenuis | |
cholic acid | 0.1% (w/v), 30% inhibition | Yamadazyma tenuis | |
deoxycholic acid | 0.1% (w/v), 30% inhibition | Yamadazyma tenuis | |
dithiothreitol | 1 mM, 40% inhibition | Yamadazyma tenuis | |
EDTA | 1 mM, 30% inhibition | Yamadazyma tenuis | |
Mn2+ | 25 mM, 95% inhibition | Yamadazyma tenuis | |
additional information | no inhibition by NAD+. No effect: Na+, K+, NH4+, Mg2+, Ca2+ and Co2+ in the form of the chloride salt in 50 mM Tris, pH 7.0, as well the anions Cl-, PO43-, SO32-, NO3-, CO32-, citrate and tetraborate in the form of the sodium salt in 50 mM phosphate buffer, pH 7.0. Glucose 6-phosphate, fructose 6-phosphate, fructose 1,6-bisphosphate, 6-phosphogluconate, phosphoenolpyruvate, oxaloacetate (5 mM each) have no effect | Yamadazyma tenuis | |
NADP+ | 2 mM completely abolishes D-xylose reduction. Potent competitive inhibitor, inhibits both the NADH-dependent and the NADPH-dependent activity | Yamadazyma tenuis | |
pyridoxal 5'-phosphate | gradual inactivation. NADH, ATP or 2'-AMP protects. No protection by D-xylose | Yamadazyma tenuis | |
Zn2+ | 25 mM, 95% inhibition | Yamadazyma tenuis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0048 | - |
NADPH | pH 7, 25°C | Yamadazyma tenuis | |
0.0266 | - |
NADP+ | pH 7, 25°C | Yamadazyma tenuis | |
0.0587 | - |
NAD+ | pH 7, 25°C | Yamadazyma tenuis | |
0.254 | - |
NADH | pH 7, 25°C | Yamadazyma tenuis | |
72 | - |
D-xylose | pH 7, 25°C, cosubstrate: NADPH | Yamadazyma tenuis | |
87 | - |
D-xylose | pH 7, 25°C, cosubstrate: NADH | Yamadazyma tenuis | |
257 | - |
xylitol | pH 7, 25°C | Yamadazyma tenuis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | no effect: Na+, K+, NH4+, Mg2+, Ca2+ and Co2+ in the form of the chloride salt in 50 mM Tris, pH 7.0, as well the anions PO43-, SO32-, NO3-, CO32-, citrate and tetraborate in the form of the sodium salt in 50 mM phosphate buffer, pH 7.0 | Yamadazyma tenuis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
43000 | - |
1 * 43000, SDS-PAGE | Yamadazyma tenuis |
48000 | - |
gel filtration | Yamadazyma tenuis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-xylose + NADPH + H+ | Yamadazyma tenuis | - |
xylitol + NADP+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Yamadazyma tenuis | - |
- |
- |
Oxidation Stability | Organism |
---|---|
the enzyme undergoes thiol oxidation during storage or purification | Yamadazyma tenuis |
Purification (Comment) | Organism |
---|---|
- |
Yamadazyma tenuis |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
culture condition:D-xylose-grown cell | - |
Yamadazyma tenuis | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
20.64 | - |
- |
Yamadazyma tenuis |
Storage Stability | Organism |
---|---|
-20°C, pure enzyme preparation is stable for more than 4 months | Yamadazyma tenuis |
4°C, pure enzyme preparation is stable for more than 4 months | Yamadazyma tenuis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-erythrose + NADPH + H+ | catalytic efficiency is 100fold higher than the catalytic efficiency for D-xylose | Yamadazyma tenuis | erythritol + NADP+ | - |
? | |
D-glucosone + NADPH + H+ | catalytic efficiency is 22fold higher than the catalytic efficiency for D-xylose | Yamadazyma tenuis | D-fructose + NADP+ | - |
? | |
D-xylose + NADH + H+ | - |
Yamadazyma tenuis | xylitol + NAD+ | - |
r | |
D-xylose + NADPH + H+ | - |
Yamadazyma tenuis | xylitol + NADP+ | - |
? | |
D-xylose + NADPH + H+ | catalytic efficiency (kcat/Km) in D-xylose reduction at pH 7 is more than 60fold higher than that in xylitol oxidation. The enzyme prefers NADPH approximately 2fold to NADH | Yamadazyma tenuis | xylitol + NADP+ | - |
r | |
DL-glyceraldehyde + NADPH + H+ | catalytic efficiency is 37fold higher than the catalytic efficiency for D-xylose | Yamadazyma tenuis | glycerol + NADP+ | - |
? | |
L-arabinose + NADPH + H+ | catalytic efficiency is 2fold higher than the catalytic efficiency for D-xylose | Yamadazyma tenuis | L-arabinitol + NADP+ | - |
? | |
methylglyoxal + NADPH + H+ | catalytic efficiency is 20fold higher than the catalytic efficiency for D-xylose | Yamadazyma tenuis | ? | - |
? | |
additional information | prefers glyceraldehyde, D-erythrose and even some aliphatic and aromatic aldehydes to the pentose sugars D-xylose and L-arabinose. Aldosones such as D-glucosone or D-xylosone are good substrates, whereas the corresponding 2-deoxy-aldose sugars are reduced at hardly detectable rates | Yamadazyma tenuis | ? | - |
? | |
phenylglyoxal + NADPH + H+ | catalytic efficiency is 17fold higher than the catalytic efficiency for D-xylose | Yamadazyma tenuis | ? | - |
? | |
pyridine-2-aldehyde + NADPH + H+ | catalytic efficiency is 7fold higher than the catalytic efficiency for D-xylose | Yamadazyma tenuis | ? | - |
? | |
valeraldehyde + NADPH + H+ | catalytic efficiency is 13fold higher than the catalytic efficiency for D-xylose | Yamadazyma tenuis | ? | - |
? | |
xylosone + NADPH + H+ | catalytic efficiency is 20fold higher than the catalytic efficiency for D-xylose | Yamadazyma tenuis | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 43000, SDS-PAGE | Yamadazyma tenuis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
- |
Yamadazyma tenuis |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 40 | activity increases linearly from 25°C to 50°C | Yamadazyma tenuis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
non-ionic detergents and bovine serum albumin stabilize the enzyme to a significant extent during long-term incubation at 25°C, 30°C or 38°C | Yamadazyma tenuis |
25 | - |
half-life: more than 2 months | Yamadazyma tenuis |
30 | 35 | 48 h, stability starts to decrease above 30-35°C | Yamadazyma tenuis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.82 | - |
NADP+ | pH 7, 25°C | Yamadazyma tenuis | |
0.87 | - |
xylitol | pH 7, 25°C | Yamadazyma tenuis | |
0.89 | - |
NAD+ | pH 7, 25°C | Yamadazyma tenuis | |
18.1 | - |
NADH | pH 7, 25°C | Yamadazyma tenuis | |
18.2 | - |
D-xylose | pH 7, 25°C, cosubstrate: NADH | Yamadazyma tenuis | |
21.5 | - |
D-xylose | pH 7, 25°C, cosubstrate: NADPH | Yamadazyma tenuis | |
21.9 | - |
NADPH | pH 7, 25°C | Yamadazyma tenuis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
xylose reduction | Yamadazyma tenuis |
8.9 | - |
xylitol oxidation | Yamadazyma tenuis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4.5 | 7.5 | pH 4.5: about 55% of maximal activity, pH 7.5: about 50% of maximal activity | Yamadazyma tenuis |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
5 | 8 | below pH 5 and above pH 8.0 the enzyme is inactivated within 3-6 days | Yamadazyma tenuis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | prefers NADPH approximately 2fold to NADH, largely due to better apparent binding of the phosphorylated form of the coenzyme | Yamadazyma tenuis | |
NADPH | prefers NADPH approximately 2fold to NADH, largely due to better apparent binding of the phosphorylated form of the coenzyme | Yamadazyma tenuis |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0015 | - |
NADP+ | pH 7, 25°C, variable substrate: NADH | Yamadazyma tenuis | |
0.0239 | - |
ATP | pH 7, 25°C, variable substrate: NADH | Yamadazyma tenuis |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Yamadazyma tenuis | isoelectric focusing | - |
4.7 |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0034 | - |
xylitol | pH 7, 25°C | Yamadazyma tenuis | |
0.21 | - |
D-xylose | pH 7, 25°C, cosubstrate: NADH | Yamadazyma tenuis | |
0.296 | - |
D-xylose | pH 7, 25°C, cosubstrate: NADPH | Yamadazyma tenuis | |
15.2 | - |
NAD+ | pH 7, 25°C | Yamadazyma tenuis | |
30.9 | - |
NADP+ | pH 7, 25°C | Yamadazyma tenuis | |
713 | - |
NADH | pH 7, 25°C | Yamadazyma tenuis | |
4610 | - |
NADPH | pH 7, 25°C | Yamadazyma tenuis |