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Literature summary for 3.6.1.7 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.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
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Subunits

Subunits Comment Organism
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