Literature summary extracted from
Chiti, F.; Taddei, N.; van Nuland, N.A.J.; Magherini, F.; Stefani, M.; Ramponi, G.; Dobson, C.M.
Structural characterization of the transition state for folding of muscle acylphosphatase (1998), J. Mol. Biol., 283, 893-903.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.6.1.7 |
C21S mutant |
Homo sapiens |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.6.1.7 |
C21S |
- |
Homo sapiens |
General Stability
EC Number |
General Stability |
Organism |
---|
3.6.1.7 |
addition of very low concentrations of phosphate causes a strong stabilisation of AcP against chemical denaturation |
Homo sapiens |
3.6.1.7 |
glucose stabilizes, denaturation midpoint of AcP shifts towards higher urea concentration upon the progressive addition of glucose, confirming that the conformational stability of the protein is higher in the presence of sugars |
Homo sapiens |
3.6.1.7 |
muscular enzyme, sensitive to urea: urea denaturation |
Homo sapiens |
3.6.1.7 |
study of unfolding and refolding kinetics, kinetic studies of stabilization |
Homo sapiens |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.6.1.7 |
phosphate |
competitive inhibition; phosphate: competitive inhibition, addition of very low concentrations of phosphate causes a strong stabilisation of AcP against chemical denaturation |
Homo sapiens |
|
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
3.6.1.7 |
additional information |
- |
additional information |
kinetic characterization, kinetic data |
Homo sapiens |
|
Organic Solvent Stability
EC Number |
Organic Solvent |
Comment |
Organism |
---|
3.6.1.7 |
1,1,1,3,3,3-hexafluoro-2-propanol |
most effective accelerator of both folding and unfolding, strongest stabilizer of alpha-helical structure in AcP. Strongest secondary structure stabilizer and most powerful folding accelerator when used at low concentrations, suggesting that the stabilisation of native-like secondary structure, in particular alpha-helical structure, is likely to play a role in AcP folding |
Homo sapiens |
3.6.1.7 |
1-propanol |
accelerator of both folding and unfolding, stabilizer of alpha-helical structure in AcP |
Homo sapiens |
3.6.1.7 |
2,2,2-trifluoroethanol |
most effective accelerator of both folding and unfolding, strongest stabilizer of alpha-helical structure in AcP |
Homo sapiens |
3.6.1.7 |
2-propanol |
accelerator of both folding and unfolding, stabilizer of alpha-helical structure in AcP |
Homo sapiens |
3.6.1.7 |
Ethanol |
accelerator of both folding and unfolding, stabilizer of alpha-helical structure in AcP |
Homo sapiens |
3.6.1.7 |
Methanol |
accelerator of both folding and unfolding, stabilizer of alpha-helical structure in AcP |
Homo sapiens |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.6.1.7 |
Homo sapiens |
- |
human |
- |
3.6.1.7 |
Homo sapiens |
- |
C21S mutant |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.6.1.7 |
C21S mutant |
Homo sapiens |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
3.6.1.7 |
an acylphosphate + H2O = a carboxylate + phosphate |
reaction mechanism |
Homo sapiens |
|
3.6.1.7 |
an acylphosphate + H2O = a carboxylate + phosphate |
thermodynamic data |
Homo sapiens |
|
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
3.6.1.7 |
muscle |
- |
Homo sapiens |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.6.1.7 |
acylphosphate + H2O |
specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates |
Homo sapiens |
carboxylate + phosphate |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.6.1.7 |
monomer |
monomeric alpha,beta protein |
Homo sapiens |