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Literature summary for 1.1.1.12 extracted from
- Protein-inorganic hybrid system for efficient his-tagged enzymes immobilization and its application in l-xylulose production (2017), RSC Adv., 7, 3488-3494 .
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Trichoderma reesei |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | preparation of a metal-protein hybrid nanoflower system for efficient immobilization of the recombinant enzyme L-arabinitol 4-dehydrogenase from Hypocrea jecorina (HjLAD). Synthesis of enzyme-Cu(PO4)2 x 3H2O hybrid nanoflowers and encapsulation of His-tagged enzyme, FESEM images, overview. Compared with the free enzyme, the synthesized hybrid nanoflower exhibit enhanced enzymatic activity of 246% for HjLAD. The immobilized enzyme retains high catalytic activity and shows improved he tolerance towards pH and temperature changes. Synthesized nanoflowers also retain high storage stability and reusability. In addition, the immobilized enzyme exhibits significantly enhanced L-xylulose production under cofactor regeneration conditions compared to the free enzyme combination | Trichoderma reesei |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 18 | - |
L-arabinitol | pH 8.0, 25°C, free recombinant enzyme | Trichoderma reesei |  |
| 21.3 | - |
L-arabinitol | pH 8.0, 25°C, immobilzed recombinant enzyme in nanoflowers | Trichoderma reesei | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-arabinitol + NAD+ | Trichoderma reesei | - |
L-xylulose + NADH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Trichoderma reesei | Q96V44 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Trichoderma reesei |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-arabinitol + NAD+ | - |
Trichoderma reesei | L-xylulose + NADH + H+ | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HjLAD | - |
Trichoderma reesei |
| LAD | - |
Trichoderma reesei |
| Lad1 | - |
Trichoderma reesei |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
recombinant enzyme | Trichoderma reesei |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 70 | activity range, free recombinant enzyme and immobilized recombinant enzyme in nanoflowers, profile overview | Trichoderma reesei |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | 9.5 | oxidation of L-arabinitol with NAD+, recombinant enzyme, assay at | Trichoderma reesei |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 10 | activity range, immobilized recombinant enzyme in nanoflowers, profile overview | Trichoderma reesei |
| 7 | 10 | activity range, free recombinant enzyme, profile overview | Trichoderma reesei |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Trichoderma reesei | |
| NADH | - |
Trichoderma reesei | |
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