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Literature summary for 3.6.1.7 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)

Cloned (Comment) Organism
C21S mutant Homo sapiens

Protein Variants

Protein Variants Comment Organism
C21S
-
Homo sapiens

General Stability

General Stability Organism
addition of very low concentrations of phosphate causes a strong stabilisation of AcP against chemical denaturation Homo sapiens
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
muscular enzyme, sensitive to urea: urea denaturation Homo sapiens
study of unfolding and refolding kinetics, kinetic studies of stabilization Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic characterization, kinetic data Homo sapiens

Organic Solvent Stability

Organic Solvent Comment Organism
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
1-propanol accelerator of both folding and unfolding, stabilizer of alpha-helical structure in AcP Homo sapiens
2,2,2-trifluoroethanol most effective accelerator of both folding and unfolding, strongest stabilizer of alpha-helical structure in AcP Homo sapiens
2-propanol accelerator of both folding and unfolding, stabilizer of alpha-helical structure in AcP Homo sapiens
Ethanol accelerator of both folding and unfolding, stabilizer of alpha-helical structure in AcP Homo sapiens
Methanol accelerator of both folding and unfolding, stabilizer of alpha-helical structure in AcP Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
human
-
Homo sapiens
-
C21S mutant
-

Purification (Commentary)

Purification (Comment) Organism
C21S mutant Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
an acylphosphate + H2O = a carboxylate + phosphate reaction mechanism Homo sapiens
an acylphosphate + H2O = a carboxylate + phosphate thermodynamic data Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Homo sapiens carboxylate + phosphate
-
?

Subunits

Subunits Comment Organism
monomer monomeric alpha,beta protein Homo sapiens