Literature summary extracted from
Terauchi, Y.; Kim, Y.K.; Tanaka, T.; Nanatani, K.; Takahashi, T.; Abe, K.
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
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.1.1.74 |
D30S |
mutation increases the KD value for interaction with hydrophobin RolA |
Aspergillus oryzae |
3.1.1.74 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.1.1.74 |
Aspergillus oryzae |
I7GSC4 |
- |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.1.1.74 |
CutL1 |
- |
Aspergillus oryzae |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.1.1.74 |
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 |