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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.
    View publication on PubMed

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