Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Longhi, S.; Cambillau, C.
    Structure-activity of cutinase, a small lipolytic enzyme (1999), Biochim. Biophys. Acta, 1441, 185-196.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.74 additional information absence of interfacial activation Fusarium solani

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.74
-
Fusarium solani

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.74 N84A 26.5% of the activity of the wild-type enzyme with p-nitrophenylbutanoate as substrate Fusarium solani
3.1.1.74 N84D 0.16% of the activity of the wild-type enzyme with p-nitrophenylbutanoate as substrate Fusarium solani
3.1.1.74 N84L 3.0% of the activity of the wild-type enzyme with p-nitrophenylbutanoate as substrate Fusarium solani
3.1.1.74 N84W 0.11% of the activity of the wild-type enzyme with p-nitrophenylbutanoate as substrate Fusarium solani
3.1.1.74 S42A 0.22% of the activity of the wild-type enzyme with p-nitrophenylbutanoate as substrate Fusarium solani

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.74 Fusarium solani
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.74 cutin + H2O
-
Fusarium solani additional information
-
?
3.1.1.74 p-nitrophenylbutanoate + H2O
-
Fusarium solani p-nitrophenol + butanoate
-
?