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Literature summary extracted from
- An atypical alpha/beta-hydrolase fold revealed in the crystal structure of pimeloyl-acyl carrier protein methyl esterase BioG from Haemophilus influenzae (2016), Biochemistry, 55, 6705-6717 .
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.1.1.85 | sitting drop vapor diffusion method at 16 °C. The crystal structure is determined at at 1.26 A. The BioG structure is similar to the BioH structure (from Escherichia coli) and is composed of an alpha-helical lid domain and a core domain that contains a central seven-stranded beta-pleated sheet. However, four of the six alpha-helices that flank both sides of the BioH core beta-sheet are replaced with long loops in BioG, thus forming an unusual alpha/beta-hydrolase fold | Haemophilus influenzae |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.85 | Haemophilus influenzae | P44251 | - |
- |
| 3.1.1.85 | Haemophilus influenzae ATCC 51907 | P44251 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.1.85 | - |
Haemophilus influenzae |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.1.85 | BioG | - |
Haemophilus influenzae |
| 3.1.1.85 | pimeloyl-ACP methyl esterase | - |
Haemophilus influenzae |
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