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Literature summary for 3.1.1.74 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

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

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Fusarium solani

Protein Variants

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

Organism

Organism UniProt Comment Textmining
Fusarium solani
-
-
-

Substrates and Products (Substrate)

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