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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Subunits
Subunits on EC 3.6.1.7 - acylphosphatase
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dimer
monomer
additional information
dimer
2 * 10128, in the crystal structure via antiparallel association of strand 4 with formation of nine interchain hydrogen bonds
dimer
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2 * 10128, in the crystal structure via antiparallel association of strand 4 with formation of nine interchain hydrogen bonds
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monomer
1 * 10129, calculated from sequence, although the enzyme exists as a monomer in solution, it can dimerize via antiparallel association of strand 4, the protein forms a dimer in the crystal structure via antiparallel association of strand 4
monomer
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1 * 10129, calculated from sequence, although the enzyme exists as a monomer in solution, it can dimerize via antiparallel association of strand 4, the protein forms a dimer in the crystal structure via antiparallel association of strand 4
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the structure of BsAcP is sensitive to pH and it has multiple conformations in equilibrium at acidic pH below pH 5.8
additional information
structure determination and protein folding analysis of wild-type and mutant enzymes by far-UV and near-UV circular dichroism and dynamic light-scattering measurements, the protein folding of AcP is enhanced by disulfide bonds, overview
additional information
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structure determination and protein folding analysis of wild-type and mutant enzymes by far-UV and near-UV circular dichroism and dynamic light-scattering measurements, the protein folding of AcP is enhanced by disulfide bonds, overview
additional information
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mutational analysis of aggregation and disaggregation of amyloid-like protofibrils of human muscle acylphosphatase, overview
additional information
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rapid oligomer formation of muscle acylphosphatase induced by heparan sulfate, aggregation at pH 5.5, 25°C, monitoring by stopped-flow device coupled to turbidometry detection, modeling, overview. The oligomers show bet-sheet structure
additional information
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in presence of 1525% (v/v) trifluoroethanol, enzyme forms aggregates able to bind specific dyes such as thioflavine T, Congo red, and 1-anilino-8-naphthalenesulfonic acid. The monomeric form adopted by the enzyme prior to aggregation under these conditions retains enzymatic activity, in addition, folding was remarkably faster than unfolding. Electron microscopy reveals the presence of small aggregates generally referred to as amyloid protofibrils
additional information
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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
additional information
aggregation process: mechanism, structure and topology, conversion of these initial aggregates into amyloid-like protofibrils is an intra-molecular process in which the AcP molecules undergo conformational modifications, model for the assembly of Sso AcP into amyloid-like aggregates at a molecular level, several models of aggregation are excluded, overview
additional information
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aggregation process: mechanism, structure and topology, conversion of these initial aggregates into amyloid-like protofibrils is an intra-molecular process in which the AcP molecules undergo conformational modifications, model for the assembly of Sso AcP into amyloid-like aggregates at a molecular level, several models of aggregation are excluded, overview
additional information
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
additional information
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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
additional information
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The partially folded ensemble of AcP displays enzymatic activity
additional information
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
additional information
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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
additional information
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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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additional information
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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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additional information
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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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additional information
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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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additional information
structure modelling, multiple conformations of the side chains of amino-acid residues
additional information
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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structure modelling, multiple conformations of the side chains of amino-acid residues
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