Literature summary for 3.1.1.74 extracted from

Ternstrom, T.; Svendsen, A.; Akke, M.; Adlercreutz, P.
Unfolding and inactivation of cutinases by AOT and guanidine hydrochloride (2005), Biochim. Biophys. Acta, 1748, 74-83.

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Protein Variants

Protein Variants	Comment	Organism
additional information	mutant myHiC, obtained by localised random mutagenesis, shows increased activity and decreased surfactanct sensitivity	Humicola insolens

General Stability

General Stability	Organism
in bis(2-ethylhexyl) sodium sulfosuccinate reverse micelles, enzyme unfolds with mono-exponential rates, indicating a two-state process. After unfolding in reverse micelles, enzyme is less destabilised than in guanidinium hydrochloride-denatured state, which is supported by fluorescence data. NMR studies indicate a molten globule structure	Humicola insolens
in bis(2-ethylhexyl) sodium sulfosuccinate reverse micelles, enzyme unfolds with mono-exponential rates, indicating a two-state process. After unfolding in reverse micelles, enzyme is less destabilised than in guanidinium hydrochloride-denatured state, which is supported by fluorescence data. NMR studies indicate a molten globule structure	Fusarium solani

Organism

Organism	UniProt	Comment	Textmining
Fusarium solani	-	-	-
Humicola insolens	-	native enzyme and mutant myHiC with increased activity and decreased surfactanct sensitivity	-

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Release 2023.1 (January 2023)