Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta | Debaryomyces nepalensis |
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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | thermodynamics, recombinant enzyme | Debaryomyces nepalensis |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Debaryomyces nepalensis | A0A0M4HL56 | - |
- |
Debaryomyces nepalensis NCYC 3413 | A0A0M4HL56 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain Rosetta | Debaryomyces nepalensis |
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 | 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 | Comment | Organism |
---|---|---|
homodimer | - |
Debaryomyces nepalensis |
Synonyms | Comment | Organism |
---|---|---|
DnXR | - |
Debaryomyces nepalensis |
xylose reductase | - |
Debaryomyces nepalensis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
sugar reduction | Debaryomyces nepalensis |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
xylose reduction | Debaryomyces nepalensis |
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 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 | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Debaryomyces nepalensis | |
NADPH | - |
Debaryomyces nepalensis |
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 |