Any feedback?
Literature summary for 1.4.1.3 extracted from
- Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus (1999), J. Mol. Biol., 293, 1121-1132.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging drop method of vapour diffusion, crystals belong to space group C2 with a hexamer in the asymmetric unit and have lattice constants a = 141.9 A, b = 197.5 A and c = 125.7 A with beta = 113.6°, the crystal structure of the extremely thermostable glutamate dehydrogenase from Thermococcus litoralis determined at 2.5 A resolution is compared to that from the hyperthermophile Pyrococcus furiosus. The less stable Thermococcus litoralis enzyme has a decreased number of ion pair interactions; modified patterns of hydrogen bonding resulting from isosteric sequence changes; substitutions that decrease packing efficiency; and substitutions which give rise to subtle but distinct shifts in both main-chain and side-chain elements of the structure | Thermococcus litoralis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermococcus litoralis | Q56304 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GluDH | - |
Thermococcus litoralis |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
