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Literature summary for 1.5.99.13 extracted from
- Design of a multi-enzyme reaction on an electrode surface for an L-glutamate biofuel anode (2017), Biotechnol. Lett., 39, 235-240 .
Application
| Application | Comment | Organism |
|---|---|---|
| energy production | a bio-anode using L-glutamate as the fuel is constructed. To oxidize L-glutamate at the anode, glutamate dehydrogenase, derived from Pyrobaculum islandicum, and proline dehydrogenase derived from Pyrococcus horikoshii, are immobilized for a two-enzyme conjugate enzymatic and redox reaction. To achieve an efficient enzyme reaction and electron transfer, the immobilization ratio of proline dehydrogenase to glutamate dehydrogenase is controlled by varying the molar ratios of dithiobis succinimidyl undecanoate and nitrilotriacetic acid dihydrochloride | Pyrococcus horikoshii |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21 | Pyrococcus horikoshii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus horikoshii | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme | Pyrococcus horikoshii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dye-dependent proline dehydrogenase | - |
Pyrococcus horikoshii |
| PDH | - |
Pyrococcus horikoshii |
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Release 2023.1 (January 2023)
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