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Literature summary for 3.6.1.7 extracted from

  • Elia, F.; Cantini, F.; Chiti, F.; Dobson, C.M.; Bemporad, F.
    Direct conversion of an enzyme from native-like to amyloid-like aggregates within inclusion bodies (2017), Biophys. J., 112, 2540-2551 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.1.7

Cloned(Commentary)

Cloned (Comment) Organism
gene acyP, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli in inclusion bodies. Wild-type enzyme Sso AcP is initially expressed as a native, folded protein, which then undergoes aggregation to form inclusion bodies Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
L65A construction of L65A, DELTAN11, and DELTAN11-L65A enzyme mutants, site-directed mutagenesis. L65A is a strongly destabilized protein variant, in which a leucine residue in the hydrophobic core of the protein is substituted by an alanine residue. DELTAN11 Sso AcP is a variant lacking the unstructured N-terminal segment. And a protein variant with the globular unit destabilized by the L65A mutation but lacking the N-terminal segment is DELTAN11-L65A Sso AcP. Comparison of conformational stability of DELTAN11 L65A Sso AcP is assessed by means of equilibrium GndHCl-induced unfolding curves in 50 mM acetate buffer at pH 5.5 and 37°C and compared to those of wild-type Sso AcP, DELTAN11 Sso AcP, and L65A Sso AcP. NMR analysis reveals that the tested variants are folded in cell extracts before aggregation Saccharolobus solfataricus
additional information direct conversion of an enzyme from native-like to amyloid-like aggregates within inclusion bodies. Shortly after the initiation of expression, Sso AcP is incorporated into inclusion bodies as a native-like protein, still exhibiting small but significant enzymatic activity. This overall process of aggregation is enhanced by the presence of the unfolded N-terminal region of the sequence and by destabilization of the globular segment of the protein. At later times, the Sso AcP molecules in the inclusion bodies lose their native-like properties and convert into beta-sheet-rich amyloid-like structures, as indicated by their ability to bind thioflavin T and Congo red Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97ZL0 i.e. Sulfolobus solfataricus
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Saccharolobus solfataricus ATCC 35092 Q97ZL0 i.e. Sulfolobus solfataricus
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Saccharolobus solfataricus DSM 1617 Q97ZL0 i.e. Sulfolobus solfataricus
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Saccharolobus solfataricus JCM 11322 Q97ZL0 i.e. Sulfolobus solfataricus
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Saccharolobus solfataricus P2 Q97ZL0 i.e. Sulfolobus solfataricus
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Subunits

Subunits Comment Organism
More wild-type enzyme Sso AcP is initially expressed as a native, folded protein, which then undergoes aggregation to form inclusion bodies that show small but significant enzymatic activity and are unable to bind ThT, but subsequently become ThT binding and enzymatically inactive. The aggregation of Sso AcP is induced in vitro by the presence of a destabilizing co-solvent, namely 2,2,2-trifluoroethanol, at concentrations as high as 20% v/v Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
ACP
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 Saccharolobus solfataricus
Acyp
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 Saccharolobus solfataricus
Sso AcP
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

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

pH Optimum

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

General Information

General Information Comment Organism
malfunction wild-type enzyme Sso AcP is initially expressed as a native, folded protein, which then undergoes aggregation to form inclusion bodies that show small but significant enzymatic activity and are unable to bind ThT, but subsequently become ThT binding and enzymatically inactive. The aggregation of Sso AcP is induced in vitro by the presence of a destabilizing co-solvent, namely 2,2,2-trifluoroethanol, at concentrations as high as 20% v/v Saccharolobus solfataricus
additional information the acylphosphatase from Sulfolobus solfataricus (Sso AcP) is a globular protein able to aggregate in vitro from a native-like conformational ensemble without the need for a transition across the major unfolding energy barrier. This process leads to the formation of assemblies in which the protein retains its native-like structure, which subsequently convert into amyloid-like aggregates. Analysis of the mechanism by which Sso AcP aggregates in vivo to form bacterial inclusion bodies after expression in Escherichia coli, overview. The aggregation behavior of the protein is similar in vivo to that observed in vitro, and, at least for a predominant part of the protein population, the transition from a native to an amyloid-like structure occurs within the aggregate state Saccharolobus solfataricus