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Literature summary for 3.1.1.74 extracted from
- Asp30 of Aspergillus oryzae cutinase CutL1 is involved in the ionic interaction with fungal hydrophobin RolA (2017), Biosci. Biotechnol. Biochem., 81, 1363-1368 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D30S | mutation increases the KD value for interaction with hydrophobin RolA | Aspergillus oryzae |
| D30S/E31S/D142S/D171S | mutation D30S increases the KD value for interaction with hydrophobin RolA in comparison with mutant E31S/D142S/D171S | Aspergillus oryzae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus oryzae | I7GSC4 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CutL1 | - |
Aspergillus oryzae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | Aspergillus oryzae hydrophobin RolA adheres to the substrate polybutylene succinate co-adipate and promotes degradation by interacting with polyesterase CutL1 and recruiting it to the substrate surface. Residue D30 of CutL is involved in the CutL1-RolA interaction | Aspergillus oryzae |
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Release 2023.1 (January 2023)
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