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Literature summary extracted from
- The flavonoid galangin inhibits the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia (2002), FEMS Microbiol. Lett., 208, 21-24.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.2.6 | galangin | flavonoid, inhibition is not reversible by addition of Zn2+, orientation in the active site, the 4-keto and the 5-hydroxy groups bind to the Zn1 atom of the enzyme | Stenotrophomonas maltophilia |  |
| 3.5.2.6 | quercetin | flavonoid | Stenotrophomonas maltophilia | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.2.6 | Zn2+ | enzyme possesses a binding site motif unique for metallo-beta-lactamases | Stenotrophomonas maltophilia | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.2.6 | Stenotrophomonas maltophilia | - |
enzyme L1 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.5.2.6 | partially | Stenotrophomonas maltophilia |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.5.2.6 | tetramer | molecular modeling for enzyme structure analysis | Stenotrophomonas maltophilia |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.2.6 | 37 | - |
assay at | Stenotrophomonas maltophilia |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.5.2.6 | 7 | - |
assay at | Stenotrophomonas maltophilia |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.5.2.6 | Stenotrophomonas maltophilia | isoelectric focusing | - |
7.1 |
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