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
ECTree
3.6.1.7 acylphosphataseAdvanced search results
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results (Engineering
Engineering on EC 3.6.1.7 - acylphosphatase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C5A/C49A
site-directed mutagenesis, the folding of the mutant lacking the disulfide bond is impaired and conformational stability is decreased compared to the wild-type enzyme, mutEcoAcP folds about 1500fold slower and a partially folded species accumulates int he mutant expressing strain
C21A
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reduced specific activity, 60% compared with wild-type enzyme, kinetic and structural properties similar to those of wild-type recombinant enzyme, urea and thermal stabilities reduced: Cys21 possible involved in stabilization of enzyme active-site conformation, involved in enzyme structure stabilization, not involved in substrate binding
C21S
DELTA1-6 deletion mutant
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N-terminus truncated mutant lacks the first six residues: reduced specific activity and native-like structure
R23Q
R97Q
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reduced specific activity, kinetic and structural properties of R97Q mutant indicate possible role of Arg-97 in the stabilisation of the active site correct conformation, most likely via back-bone and side chain interactions with Arg-23, the residue involved in phosphate binding by the enzyme
Y98Q
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reduced specific activity, kinetic and structural properties of Y98Q mutant indicate possible involvement of Tyr-98 in stabilisation of acylphosphatase overall structure
G91A
A18G
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site-directed mutagenesis, thermodynamic and kinetic parameters
A37G
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site-directed mutagenesis, thermodynamic and kinetic parameters
A46G
A58G
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site-directed mutagenesis, thermodynamic and kinetic parameters
D6C
the mutant recovers enzymatic activity following refolding, suggesting reversible unfolding processes
D85C
the mutant recovers enzymatic activity following refolding, suggesting reversible unfolding processes
E59A
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site-directed mutagenesis, thermodynamic and kinetic parameters
F29L
F88A
F98L
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site-directed mutagenesis, thermodynamic and kinetic parameters
G52A
G93A
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site-directed mutagenesis, thermodynamic and kinetic parameters
I42V
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site-directed mutagenesis, thermodynamic and kinetic parameters
I72V
K47A
single substitution of residue from the flexible region 44-61
K92A
L49A
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site-directed mutagenesis, thermodynamic and kinetic parameters
L65A
L68A
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site-directed mutagenesis, thermodynamic and kinetic parameters
M16A
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site-directed mutagenesis, thermodynamic and kinetic parameters
N48A
P50A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
P76A
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site-directed mutagenesis, thermodynamic and kinetic parameters
P77A
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site-directed mutagenesis, thermodynamic and kinetic parameters
R15A
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site-directed mutagenesis, thermodynamic and kinetic parameters
R19A
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site-directed mutagenesis, thermodynamic and kinetic parameters
R30A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
R71A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
S89A
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site-directed mutagenesis, thermodynamic and kinetic parameters
V20A
V24A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
V27A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
V54A
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site-directed mutagenesis, thermodynamic and kinetic parameters
V81A
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site-directed mutagenesis, thermodynamic and kinetic parameters
V84A
V84D
V84P
V9A/F10A
double substitution within the region 1-12 that appears to be susceptible to proteolysis
Y45A
single substitution of residue from the flexible region 44-61
Y61A
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site-directed mutagenesis, thermodynamic and kinetic parameters
Y61L
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site-directed mutagenesis, thermodynamic and kinetic parameters
Y86A
single substitution of residue from the flexible region 83-91
Y86E
L65A
V84D
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mutation provides protection against aggregation by the insertion of an edge negative charge
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V84P
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mutation provides protection against aggregation in edge beta-strand B4
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Y86E
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mutation provides protection against aggregation by the insertion of an edge negative charge
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C20R
additional information
C21S
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reduced specific activity, 85% compared with wild-type enzyme, kinetic and structural properties similar to those of wild-type recombinant enzyme, urea and thermal stabilities reduced: Cys21 possible involved in stabilization of enzyme active-site conformation, involved in enzyme structure stabilization, not involved in substrate binding
C21S
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the mutant avoids complexity arising from the presence of free thiol groups
R23Q
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mutant of muscle type enzyme is totally inactive using benzoylphosphate as a substrate and not able to bind the phosphate moiety of that substrate
R23Q
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mutant inactive on DNA, Arg23 possible has a central role for muscle type acylphosphatase activity on DNA
G91A
at 10°C the mutant enzyme G91A lacking the salt-bridge retains a significantly greater kcat value than the wild-type enzyme
G91A
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at 10°C the mutant enzyme G91A lacking the salt-bridge retains a significantly greater kcat value than the wild-type enzyme
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A46G
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states
A46G
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site-directed mutagenesis, thermodynamic and kinetic parameters
F29L
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site-directed mutagenesis, thermodynamic and kinetic parameters
F88A
single substitution of residue from the flexible region 83-91
F88A
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site-directed mutagenesis, thermodynamic and kinetic parameters
G52A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
G52A
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site-directed mutagenesis, thermodynamic and kinetic parameters
I72V
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site-directed mutagenesis, thermodynamic and kinetic parameters
K92A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
K92A
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site-directed mutagenesis, thermodynamic and kinetic parameters
L65A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states
L65A
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site-directed mutagenesis, thermodynamic and kinetic parameters
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
N48A
single substitution of residue from the flexible region 44-61
N48A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states, thermodynamic and kinetic parameters
V20A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme both in native an partially unfolded states
V20A
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site-directed mutagenesis, thermodynamic and kinetic parameters
V84A
single substitution of residue from the flexible region 83-91
V84A
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site-directed mutagenesis, thermodynamic and kinetic parameters
V84D
mutation provides protection against aggregation by the insertion of an edge negative charge
V84P
mutation provides protection against aggregation in edge beta-strand B4
Y86E
mutation provides protection against aggregation by the insertion of an edge negative charge
L65A
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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
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L65A
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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
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L65A
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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
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L65A
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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
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C20R
the mutant is nearly 100000 times more efficient in catalysis than the wild type protein
C20R
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the mutant is nearly 100000 times more efficient in catalysis than the wild type protein
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additional information
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the native state of the enzyme presents two alpha-helices. Equilibrium and kinetic measurements for folding indicate that only helix-2, spanning residues 55-67, is largely stabilized in the transition state for folding therfore playing a relevant role in this process. The aggregation rate appears to vary only for the variants in which the propensity of the region corresponding to helix-1, spanning residues 22-32, is changed. Mutations that stabilize the first helix slow down the aggregation process while those that destabilize it increase the aggregation rate
additional information
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construction of 50 mutants with changes in hydrophobicity, secondary-structure propensity and net charge for mutational analysis of aggregation and disaggregation of amyloid-like protofibrils of human muscle acylphosphatase, overview
additional information
enzyme silencing (99%) by ACYP2 siRNA-transfected HSP cells. Polymorphisms in ACYP2 gene are associated with oxaliplatin-induced neurotoxicity and with altered telomere length/dysfunction
additional information
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enzyme silencing (99%) by ACYP2 siRNA-transfected HSP cells. Polymorphisms in ACYP2 gene are associated with oxaliplatin-induced neurotoxicity and with altered telomere length/dysfunction
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
additional information
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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
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
additional information
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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
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
-
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
-
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
-
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
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