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Literature summary for 1.1.1.27 extracted from
- Interface residues that drive allosteric transitions also control the assembly of L-lactate dehydrogenase (2018), J. Phys. Chem. B, 122, 11195-11205 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bifidobacterium longum subsp. Longum | - |
- |
- |
| Bifidobacterium longum subsp. Longum DSM 20219 | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| LDH2 | - |
Bifidobacterium longum subsp. Longum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | predominantly the conformational changes in the T to R transition start from the region near the active site, comprised of helix alphaC, helix alpha1/2G, helix alpha3G, and helix alpha2F, and proceed to other structural units, thus completing the global motion. The bottleneck for assembly is the formation of the correct orientational registry between the subunits, requiring contacts between the interface residues. These residues are part of the allostery wiring diagram | Bifidobacterium longum subsp. Longum |
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