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Literature summary extracted from
- Immobilization of L-arabinitol dehydrogenase on aldehyde-functionalized silicon oxide nanoparticles for L-xylulose production (2014), Appl. Microbiol. Biotechnol., 98, 1095-1104.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.1.1.12 | additional information | covalent immobilization of purified enzyme HjLAD onto glutaraldehyde-activated silicon oxide nanoparticles shows the a high immobilization efficiency of 94.7%, comparative characterization of free and immobilized enzyme HjLAD, including its thermostability and kinetic parameters, overview. Thermostability of immobilized enzyme is 14.2-fold higher than for free HjLAD, the t1/2 of HjLAD at 25°C is enhanced from 190 min (free) to 45 h (immobilized). The immobilized HjLAD retains 94% of its initial activity after 10 cycles. Immobilization efficiencies of HjLAD onto different supports, silicon oxide nanoparticles (4830HT) show the highest efficiency, method optimization, overview | Trichoderma reesei |
| 1.1.1.12 | synthesis | immobilization of HjLAD onto silicon oxide nanoparticles has the potential for use in the industrial production of rare sugars, e.g. L-xylulose, due to the thermostability and reusability of the immobilized enzyme | Trichoderma reesei |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.1.1.12 | gene lad1, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Trichoderma reesei |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.1.1.12 | soluble | - |
Trichoderma reesei | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.12 | L-arabinitol + NAD+ | Trichoderma reesei | - |
L-xylulose + NADH + H+ | - |
? |  |
| 1.1.1.12 | L-arabinitol + NAD+ | Trichoderma reesei YSM 768 | - |
L-xylulose + NADH + H+ | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.12 | Trichoderma reesei | Q96V44 | i.e Trichoderma reesei | - |
| 1.1.1.12 | Trichoderma reesei YSM 768 | Q96V44 | i.e Trichoderma reesei | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.1.1.12 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) | Trichoderma reesei |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.12 | L-arabinitol + NAD+ | - |
Trichoderma reesei | L-xylulose + NADH + H+ | - |
? | |
| 1.1.1.12 | L-arabinitol + NAD+ | - |
Trichoderma reesei YSM 768 | L-xylulose + NADH + H+ | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.1.1.12 | More | three-dimensional structure homology modelling, overview | Trichoderma reesei |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.1.12 | HjLAD | - |
Trichoderma reesei |
| 1.1.1.12 | L-arabinitol dehydrogenase | - |
Trichoderma reesei |
| 1.1.1.12 | Lad1 | - |
Trichoderma reesei |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.12 | 65 | - |
both free and immobilized enzyme HjLAD | Trichoderma reesei |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.12 | 25 | 70 | activity range of both free and immobilized enzymes | Trichoderma reesei |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.12 | 25 | - |
half-life of free enzyme is 190 min, of immobilized enzyme 31.5 h | Trichoderma reesei |
| 1.1.1.12 | 30 | - |
half-life of free enzyme is 165 min, of immobilized enzyme 24.5 h | Trichoderma reesei |
| 1.1.1.12 | 40 | - |
half-life of free enzyme is 26 min, of immobilized enzyme 4.25 h | Trichoderma reesei |
| 1.1.1.12 | 50 | - |
half-life of free enzyme is 20 min, of immobilized enzyme 3.17 h | Trichoderma reesei |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.12 | 9.5 | - |
assay at | Trichoderma reesei |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.12 | 6 | 10 | activity range of both free and immobilized enzymes | Trichoderma reesei |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.12 | NAD+ | - |
Trichoderma reesei | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.1.1.12 | additional information | three-dimensional structure homology modelling, overview | Trichoderma reesei |
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