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Literature summary for 1.13.12.5 extracted from
- Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR (2020), Sci. Rep., 10, 20069 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| solution structure of fully active, recombinant GLuc. GLuc is an all-alphahelix protein made of nine helices. Two homologous sequential repeats form two anti-parallel bundles made by 4 helices and tied together by three disulfide bonds. The N-terminal helix 1 is grabbed by these 4 helices | Gaussia princeps |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Gaussia princeps | Q9BLZ2 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| side-chain modification | natively folded GLuc possesses ten cysteines that form five disulfide bonds. Bonding occurs at C59/C120, C65/C77, and C136/C148. Additionally, C52/C127 and C56/C123 are the most favored pairs | Gaussia princeps |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| natively folded GLuc is obtained by bacterial expression and efficient refolding using a solubility enhancement petide tag | Gaussia princeps |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 19062, MALDI-TOF, x * 19056, calcuated from sequence | Gaussia princeps |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GLuc | - |
Gaussia princeps |
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Release 2023.1 (January 2023)
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