Literature summary for 3.1.1.74 extracted from

Sehgal, P.; Bang Nielsen, S.; Pedersen, S.; Wimmer, R.; Otzen, D.E.
Modulation of cutinase stability and structure by phospholipid detergents (2007), Biochim. Biophys. Acta, 1774, 1544-1554.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli WK-6 strain	Fusarium solani

General Stability

General Stability	Organism
micelle-forming short-chain phospholipids significantly reduce cutinase stability (both below and above the critical micelle concentration) and rates of folding (only above critical micelle concentration), trapping cutinase in an inactive state which only regains activity over hours to days, rather than the few seconds required for refolding in the absence of detergent. Destabilization decreases with increasing chain length, and increases with critical micelle concentration, indicating that monomers and micelles cooperate in destabilizing cutinase	Fusarium solani

Organism

micelle-forming short-chain phospholipids significantly reduce cutinase stability (both below and above the critical micelle concentration) and rates of folding (only above critical micelle concentration), trapping cutinase in an inactive state which only regains activity over hours to days, rather than the few seconds required for refolding in the absence of detergent. Destabilization decreases with increasing chain length, and increases with critical micelle concentration, indicating that monomers and micelles cooperate in destabilizing cutinase

Fusarium solani

Organism

Organism	UniProt	Comment	Textmining
Fusarium solani	P00590	-	-

Synonyms

Synonyms	Comment	Organism
Cut1	-	Fusarium solani
cutinase-1	-	Fusarium solani

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Release 2023.1 (January 2023)