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Literature summary extracted from
- Ionic interaction of positive amino acid residues of fungal hydrophobin RolA with acidic amino acid residues of cutinase CutL1 (2015), Mol. Microbiol., 96, 14-27 .
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.74 | Aspergillus oryzae | I7GSC4 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.74 | polybutylene succinate co-adipate + H2O | - |
Aspergillus oryzae | ? | - |
? |  |
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 | in a liquid medium containing the polybutylene succinate co-adipate, Aspergillus oryzae produces RolA, a hydrophobin, and cutinase CutL1, which degrades polybutylene succinate co-adipate. Secreted RolA attaches to the surface of the polybutylene succinate co-adipate particles and recruits CutL1. Residues Asp142, Asp171 and Glu31, located on the hydrophilic molecular surface of CutL1, and His32 and Lys34, located in the N-terminus of RolA, play crucial roles in the RolA-CutL1 interaction via ionic interactions | Aspergillus oryzae |
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Release 2023.1 (January 2023)
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