Literature summary extracted from

Deryabin, D.; Gryazeva, I.; Davydova, O.; El-Registan, G.
Effect of alkylresorcinols on thermal denaturation and refolding of bacterial luciferase and synthesis of heat shock proteins revealed in the luminescent molecular and cellular test systems (2014), Mikrobiologiia, 83, 640-652 .

General Stability

EC Number	General Stability	Organism
1.14.14.3	longchain alkylresorcinol homologues exhibit a protective effect at micromolar concentrations only, while their millimolar concentrations increase the sensitivity of the model proteins to thermal treatment	Aliivibrio fischeri
1.14.14.3	longchain alkylresorcinol homologues exhibit a protective effect at micromolar concentrations only, while their millimolar concentrations increase the sensitivity of the model proteins to thermal treatment	Photobacterium leiognathi

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.14.3	Aliivibrio fischeri	-	-	-
1.14.14.3	Photobacterium leiognathi	-	-	-

Renatured (Commentary)

EC Number	Renatured (Comment)	Organism
1.14.14.3	the functional activity of heat-inactivated enzyme is restored by micromolar concentrations of shortchain alkylresorcinols, while longchain homologues inhibit refolding over a wide concentration range. The preincubation of bacterial cells with longchain alkylresorcinols leads to the dose-dependent stimulation of heat shock protein synthesis	Aliivibrio fischeri

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Release 2023.1 (January 2023)