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Literature summary for 1.4.3.2 extracted from
- Antibacterial action of a heat-stable form of l-amino acid oxidase isolated from king cobra (Ophiophagus hannah) venom (2010), Comp. Biochem. Physiol. C, 153, 237-242.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Ophiophagus hannah | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| venom | - |
Ophiophagus hannah | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| LAAO | - |
Ophiophagus hannah |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Ophiophagus hannah |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Ophiophagus hannah |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | venom LAAO is very effective in inhibiting the two Gram-positive bacteria Staphylococcus aureus and Staphylococcus epidermidis with MICs of 0.000006 mM and 0.000012 mM, respetively. LAAO is only moderately effective against three Gram-negative bacteria tested, Pseudomonas aeruginosa, Klebsiella pneumoniae, and Escherichia coli, overview. Binding to bacteria is important for the potent antibacterial activity of the enzyme | Ophiophagus hannah |
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Release 2023.1 (January 2023)
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