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Gene Review:

Acyp2 - Acylphosphatase 2

Drosophila melanogaster

Synonyms: AcPDro2, Acylphosphatase-2, Acylphosphate phosphohydrolase 2, CG18505, Dmel\CG18505

Soldi, G. et al., Soldi, G. et al., Degl'Innocenti, D. et al.

Degl'Innocenti, Ramazzotti, Marzocchini, Chiti, Raugei, Ramponi,

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High impact information on Acyp2

The acylphosphatases from Sulfolobus solfataricus and Drosophila melanogaster (Sso AcP and AcPDro2) were previously shown to form amyloid-like aggregates without the need to unfold initially [1].
Inorganic phosphate (P(i)), a competitive inhibitor binding specifically to the active site of these proteins, was found to stabilize, upon binding, the native state of AcPDro2 and to inhibit its conversion into amyloid-like fibrils [1].
In 5% (v/v) trifluoroethanol, pH 5.5, 25 degrees C one of the acylphosphatases from Drosophila melanogaster (AcPDro2) forms fibrillar aggregates that bind thioflavin T and Congo red and have an extensive beta-sheet structure, as revealed by circular dichroism [2].

Other interactions of Acyp2

Analysis of the Drosophila melanogaster EST database led to the characterization of a novel acylphosphatase (AcPDro2) [3].

References

Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway. Soldi, G., Plakoutsi, G., Taddei, N., Chiti, F. J. Med. Chem. (2006) [Pubmed]
Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state. Soldi, G., Bemporad, F., Torrassa, S., Relini, A., Ramazzotti, M., Taddei, N., Chiti, F. Biophys. J. (2005) [Pubmed]
Characterization of a novel Drosophila melanogaster acylphosphatase. Degl'Innocenti, D., Ramazzotti, M., Marzocchini, R., Chiti, F., Raugei, G., Ramponi, G. FEBS Lett. (2003) [Pubmed]

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