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Literature summary 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

EC Number Activating Compound Comment Organism Structure
1.1.1.21 bovine serum albumin 10-15% increased activity Yamadazyma tenuis
1.1.1.21 Na2SO4
-
 Yamadazyma tenuis
1.1.1.21 Tween Tween-20, Tween-80, Tween-100, each 0.1% (w/v) Yamadazyma tenuis
1.1.1.307 bovine serum albumin 0.1% (w/v), 10-15% activation Yamadazyma tenuis
1.1.1.307 Triton X-100 0.1% (w/v), 10-15% activation Yamadazyma tenuis
1.1.1.307 Tween-20 0.1% (w/v), 10-15% activation Yamadazyma tenuis
1.1.1.307 Tween-80 0.1% (w/v), 10-15% activation Yamadazyma tenuis

General Stability

EC Number General Stability Organism
1.1.1.21 25°C, 0.3 M phosphate or Tris, pH 6.0, more than 2 months Yamadazyma tenuis
1.1.1.307 stable enzyme at 25°C in phosphate and Tris buffer of various ionic strengths between pH 6.0 and 7.0 Yamadazyma tenuis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.21 AMP
-
 Yamadazyma tenuis
1.1.1.21 ATP
-
 Yamadazyma tenuis
1.1.1.21 dithiothreitol
-
 Yamadazyma tenuis
1.1.1.21 EDTA
-
 Yamadazyma tenuis
1.1.1.21 ionic detergents
-
 Yamadazyma tenuis
1.1.1.21 Mn2+
-
 Yamadazyma tenuis
1.1.1.21 NADP+
-
 Yamadazyma tenuis
1.1.1.21 pyridoxal 5'-phosphate
-
 Yamadazyma tenuis
1.1.1.21 Zn2+
-
 Yamadazyma tenuis
1.1.1.307 AMP 2 mM, completely abolishes D-xylose reduction Yamadazyma tenuis
1.1.1.307 ATP 2 mM, completely abolishes D-xylose reduction, competitive Yamadazyma tenuis
1.1.1.307 cholic acid 0.1% (w/v), 30% inhibition Yamadazyma tenuis
1.1.1.307 deoxycholic acid 0.1% (w/v), 30% inhibition Yamadazyma tenuis
1.1.1.307 dithiothreitol 1 mM, 40% inhibition Yamadazyma tenuis
1.1.1.307 EDTA 1 mM, 30% inhibition Yamadazyma tenuis
1.1.1.307 Mn2+ 25 mM, 95% inhibition Yamadazyma tenuis
1.1.1.307 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
1.1.1.307 NADP+ 2 mM completely abolishes D-xylose reduction. Potent competitive inhibitor, inhibits both the NADH-dependent and the NADPH-dependent activity Yamadazyma tenuis
1.1.1.307 pyridoxal 5'-phosphate gradual inactivation. NADH, ATP or 2'-AMP protects. No protection by D-xylose Yamadazyma tenuis
1.1.1.307 Zn2+ 25 mM, 95% inhibition Yamadazyma tenuis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.21 additional information
-
 additional information brief investigation of steady state kinetic Yamadazyma tenuis
1.1.1.307 0.0048
-
 NADPH pH 7, 25°C Yamadazyma tenuis
1.1.1.307 0.0266
-
 NADP+ pH 7, 25°C Yamadazyma tenuis
1.1.1.307 0.0587
-
 NAD+ pH 7, 25°C Yamadazyma tenuis
1.1.1.307 0.254
-
 NADH pH 7, 25°C Yamadazyma tenuis
1.1.1.307 72
-
 D-xylose pH 7, 25°C, cosubstrate: NADPH Yamadazyma tenuis
1.1.1.307 87
-
 D-xylose pH 7, 25°C, cosubstrate: NADH Yamadazyma tenuis
1.1.1.307 257
-
 xylitol pH 7, 25°C Yamadazyma tenuis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.307 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.21 43000
-
 gel filtration Yamadazyma tenuis
1.1.1.307 43000
-
 1 * 43000, SDS-PAGE Yamadazyma tenuis
1.1.1.307 48000
-
 gel filtration Yamadazyma tenuis

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.21 Yamadazyma tenuis
-
-
-
1.1.1.307 Yamadazyma tenuis
-
-
-

Oxidation Stability

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.21
-
 Yamadazyma tenuis
1.1.1.307
-
 Yamadazyma tenuis

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.21 alditol + NAD(P)+ = aldose + NAD(P)H + H+ reaction mechanism Yamadazyma tenuis
a

Source Tissue

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.21 1.5
-
-
 Yamadazyma tenuis
1.1.1.21 28.64
-
 purified enzyme Yamadazyma tenuis
1.1.1.307 20.64
-
-
 Yamadazyma tenuis

Storage Stability

EC Number Storage Stability Organism
1.1.1.307 -20°C, pure enzyme preparation is stable for more than 4 months Yamadazyma tenuis
1.1.1.307 4°C, pure enzyme preparation is stable for more than 4 months Yamadazyma tenuis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.21 alditol + NAD(P)+ 10% oxidation activity compared to reduction reaction Yamadazyma tenuis aldose + NAD(P)H
-
 r
1.1.1.21 aldose + NAD(P)H wide specificity Yamadazyma tenuis alditol + NAD(P)+
-
 r
1.1.1.21 D-xylose + NAD(P)H
-
 Yamadazyma tenuis xylitol + NAD(P)+
-
 r
1.1.1.21 pentose + NADPH
-
 Yamadazyma tenuis pentitol + NADP+
-
 r
1.1.1.21 xylitol + NAD(P)+
-
 Yamadazyma tenuis D-xylose + NAD(P)H + H+
-
 r
1.1.1.307 D-erythrose + NADPH + H+ catalytic efficiency is 100fold higher than the catalytic efficiency for D-xylose Yamadazyma tenuis erythritol + NADP+
-
 ?
1.1.1.307 D-glucosone + NADPH + H+ catalytic efficiency is 22fold higher than the catalytic efficiency for D-xylose Yamadazyma tenuis D-fructose + NADP+
-
 ?
1.1.1.307 D-xylose + NADH + H+
-
 Yamadazyma tenuis xylitol + NAD+
-
 r
1.1.1.307 D-xylose + NADPH + H+
-
 Yamadazyma tenuis xylitol + NADP+
-
 ?
1.1.1.307 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
1.1.1.307 DL-glyceraldehyde + NADPH + H+ catalytic efficiency is 37fold higher than the catalytic efficiency for D-xylose Yamadazyma tenuis glycerol + NADP+
-
 ?
1.1.1.307 L-arabinose + NADPH + H+ catalytic efficiency is 2fold higher than the catalytic efficiency for D-xylose Yamadazyma tenuis L-arabinitol + NADP+
-
 ?
1.1.1.307 methylglyoxal + NADPH + H+ catalytic efficiency is 20fold higher than the catalytic efficiency for D-xylose Yamadazyma tenuis ?
-
 ?
1.1.1.307 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 ?
-
 ?
1.1.1.307 phenylglyoxal + NADPH + H+ catalytic efficiency is 17fold higher than the catalytic efficiency for D-xylose Yamadazyma tenuis ?
-
 ?
1.1.1.307 pyridine-2-aldehyde + NADPH + H+ catalytic efficiency is 7fold higher than the catalytic efficiency for D-xylose Yamadazyma tenuis ?
-
 ?
1.1.1.307 valeraldehyde + NADPH + H+ catalytic efficiency is 13fold higher than the catalytic efficiency for D-xylose Yamadazyma tenuis ?
-
 ?
1.1.1.307 xylosone + NADPH + H+ catalytic efficiency is 20fold higher than the catalytic efficiency for D-xylose Yamadazyma tenuis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.21 monomer 1 * 43000, SDS-PAGE Yamadazyma tenuis
1.1.1.307 monomer 1 * 43000, SDS-PAGE Yamadazyma tenuis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.21 50
-
-
 Yamadazyma tenuis
1.1.1.307 50
-
-
 Yamadazyma tenuis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.21 25 50
-
 Yamadazyma tenuis
1.1.1.307 25 40 activity increases linearly from 25°C to 50°C Yamadazyma tenuis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.21 30 35 after 48 h incubation activity decreases Yamadazyma tenuis
1.1.1.307 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
1.1.1.307 25
-
 half-life: more than 2 months Yamadazyma tenuis
1.1.1.307 30 35 48 h, stability starts to decrease above 30-35°C Yamadazyma tenuis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.307 0.82
-
 NADP+ pH 7, 25°C Yamadazyma tenuis
1.1.1.307 0.87
-
 xylitol pH 7, 25°C Yamadazyma tenuis
1.1.1.307 0.89
-
 NAD+ pH 7, 25°C Yamadazyma tenuis
1.1.1.307 18.1
-
 NADH pH 7, 25°C Yamadazyma tenuis
1.1.1.307 18.2
-
 D-xylose pH 7, 25°C, cosubstrate: NADH Yamadazyma tenuis
1.1.1.307 21.5
-
 D-xylose pH 7, 25°C, cosubstrate: NADPH Yamadazyma tenuis
1.1.1.307 21.9
-
 NADPH pH 7, 25°C Yamadazyma tenuis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.21 6
-
 reduction of D-xylose, NADH Yamadazyma tenuis
1.1.1.21 8.9
-
 oxidation of xylitol, NAD+ Yamadazyma tenuis
1.1.1.307 6
-
 xylose reduction Yamadazyma tenuis
1.1.1.307 8.9
-
 xylitol oxidation Yamadazyma tenuis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.21 5 8 below pH 5.0 and above pH 8.0 inactivation at 25°C within 3-6 days Yamadazyma tenuis
1.1.1.307 4.5 7.5 pH 4.5: about 55% of maximal activity, pH 7.5: about 50% of maximal activity Yamadazyma tenuis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.307 5 8 below pH 5 and above pH 8.0 the enzyme is inactivated within 3-6 days Yamadazyma tenuis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.21 NADH
-
 Yamadazyma tenuis
1.1.1.21 NADP+ 2.2fold higher activity than with NAD+ Yamadazyma tenuis
1.1.1.21 NADPH 5.3fold higher activity than with NAD(H) Yamadazyma tenuis
1.1.1.307 NADH prefers NADPH approximately 2fold to NADH, largely due to better apparent binding of the phosphorylated form of the coenzyme Yamadazyma tenuis
1.1.1.307 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]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.1.307 0.0015
-
 NADP+ pH 7, 25°C, variable substrate: NADH Yamadazyma tenuis
1.1.1.307 0.0239
-
 ATP pH 7, 25°C, variable substrate: NADH Yamadazyma tenuis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.1.1.307 Yamadazyma tenuis isoelectric focusing
-
 4.7

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.307 0.0034
-
 xylitol pH 7, 25°C Yamadazyma tenuis
1.1.1.307 0.21
-
 D-xylose pH 7, 25°C, cosubstrate: NADH Yamadazyma tenuis
1.1.1.307 0.296
-
 D-xylose pH 7, 25°C, cosubstrate: NADPH Yamadazyma tenuis
1.1.1.307 15.2
-
 NAD+ pH 7, 25°C Yamadazyma tenuis
1.1.1.307 30.9
-
 NADP+ pH 7, 25°C Yamadazyma tenuis
1.1.1.307 713
-
 NADH pH 7, 25°C Yamadazyma tenuis
1.1.1.307 4610
-
 NADPH pH 7, 25°C Yamadazyma tenuis