Literature summary for 3.6.1.7 extracted from

Bemporad, F.; Vannocci, T.; Varela, L.; Azuaga, A.I.; Chiti, F.
A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state (2008), Biochim. Biophys. Acta, 1784, 1986-1996.

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Protein Variants

Protein Variants	Comment	Organism
D6C	the mutant recovers enzymatic activity following refolding, suggesting reversible unfolding processes	Saccharolobus solfataricus
D85C	the mutant recovers enzymatic activity following refolding, suggesting reversible unfolding processes	Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	Q97ZL0	-	-

Subunits

Subunits	Comment	Organism
More	aggregation process: mechanism, structure and topology, conversion of these initial aggregates into amyloid-like protofibrils is an intra-molecular process in which the AcP molecules undergo conformational modifications, model for the assembly of Sso AcP into amyloid-like aggregates at a molecular level, several models of aggregation are excluded, overview	Saccharolobus solfataricus

Synonyms

Synonyms	Comment	Organism
ACP	-	Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5.5	-	assay at	Saccharolobus solfataricus

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Release 2023.1 (January 2023)