Literature summary for 3.1.1.1 extracted from

Sehgal, A.C.; Tompson, R.; Cavanagh, J.; Kelly, R.M.
Structural and catalytic response to temperature and cosolvents of carboxylesterase EST1 from the extremely thermoacidophilic archaeon Sulfolobus solfataricus P1 (2002), Biotechnol. Bioeng., 80, 784-793.

Search for more literature for 3.1.1.1

Activating Compound

Activating Compound	Comment	Organism	Structure
DMSO	optimal activation at 3.5% v/v with an increase in kcat of 20-30%, no dramatic changes in conformation of the enzyme at 3.5% v/v DMSO and 50-80°C, but significant changes at small DMSO concentrations	Saccharolobus solfataricus

Application

Application	Comment	Organism
biotechnology	the enzyme can be used as a biocatalyst at suboptimal temperatures through addition of DMSO as an activator	Saccharolobus solfataricus

Inhibitors

Inhibitors	Comment	Organism	Structure
acetonitrile	inactivation	Saccharolobus solfataricus
Dimethyl formamide	inactivation	Saccharolobus solfataricus
dioxane	inactivation	Saccharolobus solfataricus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics	Saccharolobus solfataricus

Organic Solvent Stability

Organic Solvent	Comment	Organism
acetonitrile	inactivation	Saccharolobus solfataricus
dimethyl formamide	inactivation	Saccharolobus solfataricus
dioxane	inactivation	Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	-	enzyme Est1	-
Saccharolobus solfataricus P1	-	enzyme Est1	-

Synonyms

Synonyms	Comment	Organism
Est1	-	Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
50	80	-	Saccharolobus solfataricus

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Release 2023.1 (January 2023)