3.6.1.7: acylphosphatase
This is an abbreviated version!
For detailed information about acylphosphatase, go to the full flat file.
Word Map on EC 3.6.1.7
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3.6.1.7
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horse
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native-like
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ca2+-atpase
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solfataricus
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trifluoroethanol
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phosphoenzyme
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acylphosphates
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thioflavine
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ototoxicity
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amyloid-like
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protofibrils
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medicine
- 3.6.1.7
- horse
-
native-like
- ca2+-atpase
- solfataricus
- trifluoroethanol
- phosphoenzyme
- acylphosphates
-
thioflavine
- ototoxicity
-
amyloid-like
-
protofibrils
- medicine
Reaction
Synonyms
1,3-diphosphoglycerate phosphatase, acetic phosphatase, acetyl phosphatase, acetylphosphatase, ACP, AcPDRo2, acyl phosphatase, acyl phosphate phosphohydrolase, Acylphosphatase, erythrocyte isozyme, Acylphosphatase, erythrocyte/testis isozyme, Acylphosphate phosphohydrolase, acylphosphate phosphomonohydrolase, Acyp, ACYP2, carbamoylphosphate phosphatase, carbamyl phosphate phosphatase, Ch1, Ch2, GP 1-3, GP1, GP2, GP3, Ho 1-3, Ho1, Ho2, Ho3, human common-type acylphosphatase, Isozyme CH1, Isozyme CH2, Isozyme TU1, More, muscle-type acylphosphatase 2, native acylphosphatase, PhAcP, phosphatase, acyl, Sso AcP, SSO0887, T1, TT0497
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General Information on EC 3.6.1.7 - acylphosphatase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
two isoforms of ACYP are characterized, the erythrocyte-type acylphosphatase 1 (ACYP1) and the muscle-type acylphosphatase 2 (ACYP2)
malfunction
physiological function
increased levels of ACYP have been revealed in fibroblasts from patients affected by Alzheimer's diseas. ACYP2 is involved in ion transport, cell differentiation, programmed cell death, and cancer
additional information
malfunction
upon inhibition of ACYP2 gene by siRNA, exposure to oxadion, that induces the ACYP2 gene, is no more able to exert an inhibitory effect on both neuritogenesis and on GAP43 protein expression stimulated by FGF2 or BDNF. The motility of HSP cells transfected with ACYP2 siRNA is tested by the scratch wound healing assay, exposure to oxadion fails to retard the closure of the wound, and cell-free area is quite completely closed after 24 h as observed in control untransfected cells grown in absence of oxadion. Polymorphisms in ACYP2 gene are associated with oxaliplatin-induced neurotoxicity and with altered telomere length/dysfunction. ACYP2 is a molecular target of neurotoxicity
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
malfunction
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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
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malfunction
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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
-
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
-
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
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additional information
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the disordered active site is converted to an ordered state upon ligand binding. Only one main conformation could bind ligand, and the relative population of these states is modulated by ligand concentration, pH-dependent conformations, overview
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
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
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
-
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
-
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
-
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
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