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Literature summary for 1.1.1.430 extracted from

  • Nidetzky, B.; Brueggler, K.; Kratzer, R.; Mayr, P.
    Multiple forms of xylose reductase in Candida intermedia comparison of their functional properties using quantitative structure-activity relationships, steady-state kinetic analysis, and pH studies (2003), J. Agric. Food Chem., 51, 7930-7935 .
    View publication on PubMed
Search for more literature for 1.1.1.430

Application

Application Comment Organism
synthesis dual specific xylose reductase (dsXR) has an about 4fold higher specificity for NADH than NADPH. This fact could make this enzyme an interesting candidate to be used in metabolic engineering of the yeast xylose metabolism, likely in Saccharomyces cerevisiae. Increased levels of dsXR activity could contribute to an improvement of ethanol production from D-xylose by reducing the cofactor imbalance of the initial catabolic pathway [Candida] intermedia

Inhibitors

Inhibitors Comment Organism Structure
NAD+ for dual specific xylose reductase (dsXR) NAD+ behaves as a competitive inhibitor against NADH. Competitive inhibition of is observed both at unsaturating and saturating concentrations of xylose [Candida] intermedia
NADH for dual specific xylose reductase (dsXR) NADH behaves as a competitive inhibitor against NAD+. Competitive inhibition of is observed both at unsaturating and saturating concentrations of xylitol [Candida] intermedia
NADP+ for monospecific xylose reductase (msXR) and dual specific xylose reductase (dsXR) NADP+ behaves as a competitive inhibitor against NADPH. Competitive inhibition of is observed both at unsaturating and saturating concentrations of xylose [Candida] intermedia
NADPH for monospecific xylose reductase (msXR) and dual specific xylose reductase (dsXR) NADPH behaves as a competitive inhibitor against NADP+. Competitive inhibition of is observed both at unsaturating and saturating concentrations of xylitol [Candida] intermedia

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.007
-
 D-fucose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
0.01
-
 D-xylose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
0.015
-
 D-galactose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
0.02
-
 D-erythrose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
0.028
-
 L-arabinose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
0.033
-
 D-glucose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
0.068
-
 D-ribose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
0.126
-
 2-deoxy-D-galactose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
0.144
-
 L-Lyxose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
2.43
-
 DL-glyceraldehyde pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
13.2
-
 propionaldehyde pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
14.7
-
 pentanal pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
33
-
 Butanal pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia

Organism

Organism UniProt Comment Textmining
[Candida] intermedia
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-deoxy-D-galactose + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia ?
-
 ?
2-deoxy-D-ribose + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia ?
-
 ?
butanal + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia ?
-
 ?
D-erythrose + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia ?
-
 ?
D-fucose + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia ?
-
 ?
D-galactose + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia ?
-
 ?
D-glucose + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia ?
-
 ?
D-lyxose + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia ?
-
 ?
D-ribose + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia ?
-
 ?
D-xylose + NADH + H+ reaction is catalyzed by dual specific xylose reductase (dsXR), reaction is not catalyzed by NADPH-dependent monospecific xylose reductase (msXR) [Candida] intermedia xylitol + NAD+
-
 ?
D-xylose + NADPH + H+ reaction is catalyzed by NADPH-dependent monospecific xylose reductase (msXR), and by dual specific xylose reductase (dsXR) [Candida] intermedia xylitol + NADP+
-
 ?
DL-glyceraldehyde + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia glycerol + NAD+
-
 ?
L-arabinose + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia L-arabinitol + NAD+
-
 ?
L-lyxose + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia ?
-
 ?
additional information Candida intermedia produces two isoforms of xylose reductase: one is NADPH-dependent (monospecific xylose reductase, msXR, cf. 1.1.1.431), and another prefers NADH about 4fold over NADPH (dual specific xylose reductase, dsXR) [Candida] intermedia ?
-
-
pentanal + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia ?
-
 ?
propionaldehyde + NADH + H+ dual specific xylose reductase (dsXR) [Candida] intermedia ?
-
 ?

Synonyms

Synonyms Comment Organism
dsXR Candida intermedia produces two isoforms of xylose reductase: one is NADPH-dependent (monospecific xylose reductase, msXR, cf. 1.1.1.431), and another prefers NADH about 4fold over NADPH (dual specific xylose reductase, dsXR) [Candida] intermedia

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at [Candida] intermedia

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5
-
 2-deoxy-D-galactose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
4.6
-
 propionaldehyde pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
4.9
-
 D-ribose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
5.4
-
 Butanal pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
5.6
-
 D-glucose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
5.9
-
 pentanal pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
6.6
-
 L-Lyxose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
9.4
-
 D-galactose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
10.2
-
 D-fucose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
13.5
-
 L-arabinose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
14.1
-
 DL-glyceraldehyde pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
16.9
-
 D-xylose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
27.5
-
 D-erythrose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at [Candida] intermedia

Cofactor

Cofactor Comment Organism Structure
NADH dual specific xylose reductase (dsXR) has an about 4fold higher specificity for NADH than NADPH [Candida] intermedia
NADPH dual specific xylose reductase (dsXR) has an about 4fold higher specificity for NADH than NADPH. NADPH-dependent monospecific xylose reductase (msXR) shows non activity with NADH [Candida] intermedia

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.008
-
 NADH pH 7.0, 25°C, dual specific xylose reductase (dsXR) [Candida] intermedia
0.014
-
 NADPH pH 7.0, 25°C, dual specific xylose reductase (dsXR) [Candida] intermedia
0.053
-
 NADP+ pH 7.0, 25°C, dual specific xylose reductase (dsXR) [Candida] intermedia
0.074
-
 NAD+ pH 7.0, 25°C, dual specific xylose reductase (dsXR) [Candida] intermedia

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.035
-
 propionaldehyde pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
0.16
-
 Butanal pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
0.4
-
 pentanal pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
5.8
-
 DL-glyceraldehyde pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
28
-
 2-deoxy-D-galactose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
46
-
 L-Lyxose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
72
-
 D-ribose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
170
-
 D-glucose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
482
-
 L-arabinose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
627
-
 D-galactose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
1380
-
 D-erythrose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
1457
-
 D-fucose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia
1690
-
 D-xylose pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH [Candida] intermedia