Literature summary for 3.6.1.7 extracted from

Plakoutsi, G.; Taddei, N.; Stefani, M.; Chiti, F.
Aggregation of the acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation (2004), J. Biol. Chem., 279, 14111-14119.

Search for more literature for 3.6.1.7

Application

Application	Comment	Organism
medicine	protein aggregation is associated with a number of human pathologies including Alzheimers and Creutzfeldt-Jakob diseases and the systemic amyloidoses. In presence of 1525% (v/v) trifluoroethanol, enzyme forms aggregates able to bind specific dyes such as thioflavine T, Congo red, and 1-anilino-8-naphthalenesulfonic acid. The monomeric form adopted by the enzyme prior to aggregation under these conditions retains enzymatic activity, in addition, folding was remarkably faster than unfolding. Electron microscopy reveals the presence of small aggregates generally referred to as amyloid protofibrils	Saccharolobus solfataricus

Inhibitors

Inhibitors	Comment	Organism	Structure
trifluoroethanol	in presence of 1525% (v/v) trifluoroethanol, enzyme forms aggregates able to bind specific dyes such as thioflavine T, Congo red, and 1-anilino-8-naphthalenesulfonic acid. The monomeric form adopted by the enzyme prior to aggregation under these conditions retains enzymatic activity, in addition, folding was remarkably faster than unfolding. Electron microscopy reveals the presence of small aggregates generally referred to as amyloid protofibrils	Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	-	-	-

Subunits

Subunits	Comment	Organism
More	in presence of 1525% (v/v) trifluoroethanol, enzyme forms aggregates able to bind specific dyes such as thioflavine T, Congo red, and 1-anilino-8-naphthalenesulfonic acid. The monomeric form adopted by the enzyme prior to aggregation under these conditions retains enzymatic activity, in addition, folding was remarkably faster than unfolding. Electron microscopy reveals the presence of small aggregates generally referred to as amyloid protofibrils	Saccharolobus solfataricus

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Release 2023.1 (January 2023)