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Literature summary extracted from

  • Soldi, G.; Bemporad, F.; Chiti, F.
    The degree of structural protection at the edge beta-strands determines the pathway of amyloid formation in globular proteins (2008), J. Am. Chem. Soc., 130, 4295-4302.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.6.1.7 additional information assembly of folded protein molecules into native-like aggregates is prevented by single-point mutations that introduce structural protections within one of the most flexible region of the protein, the peripheral edge beta-strand 4. The resulting mutants do not form native-like aggregates, but can still form thioflavin T-binding and beta-structured oligomers, albeit more slowly than the wild-type protein Saccharolobus solfataricus
3.6.1.7 V84D site-directed mutagenesis Saccharolobus solfataricus
3.6.1.7 V84P site-directed mutagenesis Saccharolobus solfataricus
3.6.1.7 Y86E site-directed mutagenesis Saccharolobus solfataricus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.7 additional information
-
additional information hydrodynamic parameters by dynamic light scattering, kinetics, wild-type and mutant enzymes, overview Saccharolobus solfataricus

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.7 Saccharolobus solfataricus Q97ZL0
-
-

Subunits

EC Number Subunits Comment Organism
3.6.1.7 More the enzyme has the ability to aggregate via the transient formation of oligomers in which the protein molecules retain native-like conformations, enzyme secondary and three-dimensional structure, topology, and comparison with acylphosphatases from other organisms, overview. beta-Structured oligomer formation proceeds via an alternative mechanism that is independent of the transient formation of native-like aggregates Saccharolobus solfataricus

Synonyms

EC Number Synonyms Comment Organism
3.6.1.7 ACP
-
Saccharolobus solfataricus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.7 25
-
assay at Saccharolobus solfataricus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.7 5.5
-
assay at Saccharolobus solfataricus