Literature summary extracted from

Bemporad, F.; Capanni, C.; Calamai, M.; Tutino, M.L.; Stefani, M.; Chiti, F.
Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. A comparative analysis with other proteins from the same superfamily (2004), Biochemistry, 43, 9116-9126.

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.6.1.7	Saccharolobus solfataricus	-	-	-

Subunits

EC Number	Subunits	Comment	Organism
3.6.1.7	More	study on folding process of enzyme and comparison with other acylphosphatases. An ensemble of partially folded or misfolded species form rapidly on the submillisecond time scale after initiation of folding. Enzyme folds a rate constant of about 5 per s at pH 5.5 and 37°C	Saccharolobus solfataricus

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Release 2023.1 (January 2023)