Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.307 extracted from

  • Neuhauser, W.; Haltrich, D.; Kulbe, K.D.; Nidetzky, B.
    NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis (1997), Biochem. J., 326, 683-692.
    View publication on PubMedView publication on EuropePMC

Activating Compound

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

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

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 [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

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 [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
1 * 43000, SDS-PAGE Yamadazyma tenuis
48000
-
gel filtration Yamadazyma tenuis

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Yamadazyma tenuis
-
-
-

Oxidation Stability

Oxidation Stability Organism
the enzyme undergoes thiol oxidation during storage or purification Yamadazyma tenuis

Purification (Commentary)

Purification (Comment) Organism
-
Yamadazyma tenuis

Source Tissue

Source Tissue Comment Organism Textmining
culture condition:D-xylose-grown cell
-
Yamadazyma tenuis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
20.64
-
-
Yamadazyma tenuis

Storage Stability

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 and Products (Substrate)

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

Subunits Comment Organism
monomer 1 * 43000, SDS-PAGE Yamadazyma tenuis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Yamadazyma tenuis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 40 activity increases linearly from 25°C to 50°C Yamadazyma tenuis

Temperature Stability [°C]

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 [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
xylose reduction Yamadazyma tenuis
8.9
-
xylitol oxidation Yamadazyma tenuis

pH Range

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 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

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 [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

pI Value

Organism Comment pI Value Maximum pI Value
Yamadazyma tenuis isoelectric focusing
-
4.7

kcat/KM [mM/s]

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