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Literature summary for 3.1.1.3 extracted from
- Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 angstroms resolution (1996), J. Mol. Biol., 259, 704-717.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystallized by vapor diffusion in sitting drops using polyethylene glycol and methyl-pentane-diol as precipitants in the presence of beta-octyl-glycopyranoside. Crystal structure of the enzyme is determined by isomorphous replacement and refined at 1.6 A resolution to an R-factor of 17.8% | Burkholderia glumae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Burkholderia glumae | Q05489 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | catalytic triad of the active center consists of the residues Ser87, Asp263 and His285. These residues are not exposed to the solvent, but a narrow channel connects them with the molecular surface | Burkholderia glumae | ? | - |
? |  |
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