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Literature summary for 1.1.1.431 extracted from

  • Malla, S.; Gummadi, S.N.
    Counteraction of osmolytes on pH-induced unfolding of xylose reductase from Debaryomyces nepalensis NCYC 3413 (2020), Eur. Biophys. J., 49, 267-277 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta Debaryomyces nepalensis

General Stability

General Stability Organism
the four osmolytes, glycerol, sucrose, trehalose and sorbitol, are effective in enhancing enzyme stability by several folds at extreme pH with sorbitol being the most efficient, which increased enzyme half-life by 11fold at pH 10.0 and 8fold at pH 5.0 Debaryomyces nepalensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information thermodynamics, recombinant enzyme Debaryomyces nepalensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-xylose + NADPH + H+ Debaryomyces nepalensis
-
xylitol + NADP+
-
r
D-xylose + NADPH + H+ Debaryomyces nepalensis NCYC 3413
-
xylitol + NADP+
-
r

Organism

Organism UniProt Comment Textmining
Debaryomyces nepalensis A0A0M4HL56
-
-
Debaryomyces nepalensis NCYC 3413 A0A0M4HL56
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain Rosetta Debaryomyces nepalensis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
134
-
purified recombinant His-tagged enzyme, pH 6.5, 55°C, xylose reduction Debaryomyces nepalensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-xylose + NADPH + H+
-
Debaryomyces nepalensis xylitol + NADP+
-
r
D-xylose + NADPH + H+
-
Debaryomyces nepalensis NCYC 3413 xylitol + NADP+
-
r

Subunits

Subunits Comment Organism
homodimer
-
Debaryomyces nepalensis

Synonyms

Synonyms Comment Organism
DnXR
-
Debaryomyces nepalensis
xylose reductase
-
Debaryomyces nepalensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
sugar reduction Debaryomyces nepalensis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
7
-
the purified recombinant enzyme is catalytically and structurally stable showing a melting temperature of 50°C Debaryomyces nepalensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
xylose reduction Debaryomyces nepalensis

pH Range

pH Minimum pH Maximum Comment Organism
5 10 over 50% of maximal activity at pH 5.0-10.0, recombinant enzyme Debaryomyces nepalensis

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
alteration in both secondary and tertiary structures cause enzyme deactivation in acidic pH, while increased deactivation rates at alkaline pH are attributed to the variation of tertiary structure over time. The secondary structure of enzyme DnXR is completely affected at pH 5.0 and is retained at pH 5.5 with altered signature. Negative ellipticity values are reduced at pH 6.0 and 10.0 without alteration in secondary signatures. Overlapping spectra are obtained at pH 7.0, pH 8.0, and pH 9.0 with the highest signals. Effect of pH on thermodynamic parameters, overview Debaryomyces nepalensis
7
-
the purified recombinant enzyme is catalytically and structurally stable at pH 7.0 with half-life of 250 min Debaryomyces nepalensis

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Debaryomyces nepalensis
NADPH
-
Debaryomyces nepalensis

General Information

General Information Comment Organism
malfunction alteration in both secondary and tertiary structures cause enzyme deactivation in acidic pH, while increased deactivation rates at alkaline pH are attributed to the variation of tertiary structure over time Debaryomyces nepalensis