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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 .
    View publication on PubMed

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