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

BRENDA support

Literature summary for 1.1.1.307 extracted from

  • Häcker, B.; Habenicht, A.; Kiess, M.; Mattes, R.
    Xylose utilisation: cloning and characterisation of the xylose reductase from Candida tenuis (1999), Biol. Chem., 380, 1395-1403.
    View publication on PubMed
Search for more literature for 1.1.1.307

Application

Application Comment Organism
synthesis production of xylitol Yamadazyma tenuis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Yamadazyma tenuis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
90.44
-
 D-xylose pH 6.0, 25°C, cosubstrate: NADH 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 xylose reductases catalyse the initial reaction in the xylose utilisation pathway, the NAD(P)H dependent reduction of xylose to xylitol xylitol + NADP+
-
 ?
D-xylose + NADPH + H+ Yamadazyma tenuis CBS 4435 xylose reductases catalyse the initial reaction in the xylose utilisation pathway, the NAD(P)H dependent reduction of xylose to xylitol xylitol + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Yamadazyma tenuis O74237
-
-
Yamadazyma tenuis CBS 4435 O74237
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Yamadazyma tenuis

Renatured (Commentary)

Renatured (Comment) Organism
denaturation buffers of either pH 6.0 or 8.0, containing urea in concentrations of 2, 4, 6, and 8 M, are used and analysed in SDS-PAGE. Optimal solvation of the XylR giving the lowest background of Escherichia coli proteins is performed with 4 M urea at pH 8.0. For renaturation, a set of buffers containing 0, 0.1, 0.5, 1 and 1.5 mM glutathione (red:ox = 1:1) at pH values of 5.0, 6.0, 7.0, and 8.0 are tested. Refolding occurrs at 8°C and its progress is analysed by assaying the volumetric activity in the respective buffers. Best renaturation results are obtained in a 20 mM Tris/HCl buffer at pH 7.0 without glutathione. After 4 days about 70% of the activity of the XylR is recovered. Buffers at pH 8.0 work slightly less efficient compared to that of pH 7.0. At pH 5.0 and 6.0 refolding is drastically reduced. Increasing concentrations of glutathione do not improve renaturation Yamadazyma tenuis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-xylose + NADH + H+
-
 Yamadazyma tenuis xylitol + NAD+
-
 ?
D-xylose + NADH + H+
-
 Yamadazyma tenuis CBS 4435 xylitol + NAD+
-
 ?
D-xylose + NADPH + H+
-
 Yamadazyma tenuis xylitol + NADP+
-
 ?
D-xylose + NADPH + H+ xylose reductases catalyse the initial reaction in the xylose utilisation pathway, the NAD(P)H dependent reduction of xylose to xylitol Yamadazyma tenuis xylitol + NADP+
-
 ?
D-xylose + NADPH + H+
-
 Yamadazyma tenuis CBS 4435 xylitol + NADP+
-
 ?
D-xylose + NADPH + H+ xylose reductases catalyse the initial reaction in the xylose utilisation pathway, the NAD(P)H dependent reduction of xylose to xylitol Yamadazyma tenuis CBS 4435 xylitol + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
XylR
-
 Yamadazyma tenuis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
18.11
-
 D-xylose pH 6.0, 25°C, cosubstrate: NADH Yamadazyma tenuis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.2
-
 D-xylose pH 6.0, 25°C, cosubstrate: NADH Yamadazyma tenuis