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Literature summary for 3.4.19.1 extracted from

  • Senthilkumar, R.; Sharma, K.K.
    Effect of chaotropic agents on the structure-function of recombinant acylpeptide hydrolase (2002), J. Protein Chem., 21, 323-332.
    View publication on PubMed

General Stability

General Stability Organism
1 M guanidine-HCl, activity is completely abolished. Dialysis results in 15-20% recovery of enzyme activity. In 1 M guanidine HCl the enzyme loses both its secondary and tertiary structures and dissociates into monomers of 70000 Da. Both monomeric and dimeric species are observed after 24 h dialysis of the enzyme denatured with guanidine-HCl. Both the monomer and dimer forms recovered after dialysis are active Sus scrofa
8 M urea, 1 h, 25°C, 85% loss of activity. Complete recovery on dialysis or 50fold dilution of the denatured enzyme. The enzyme lost its secondary structure at urea concentrations of 2 M and higher, whereas the tertiary structure is minimally perturbed below 4 M urea Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.006
-
N-acetyl-Ala-p-nitroanilide pH 7.5 Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
4 * 70000 Sus scrofa
300000
-
gel filtration Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
complete recovery of enzyme denatured with 8 M urea on dialysis or 50fold dilution. The enzyme loses its secondary structure at urea concentrations of 2 M and higher, whereas the tertiary structure is minimally perturbed below 4 M urea. Dialysis of the enzyme denatured with 1 M guanidine-HCl results in 15-20% recovery of enzyme activity. In 1 M guanidine HCl the enzyme loses both its secondary and tertiary structures and dissociates into monomers of 70000 Da. Both monomeric and dimeric species are observed after 24 h dialysis of the enzyme denatured with guanidine-HCl. Both the monomeric and dimeric forms recovered after dialysis are active Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-Ala-p-nitroanilide + H2O
-
Sus scrofa N-acetyl-Ala + p-nitroaniline
-
?

Subunits

Subunits Comment Organism
More both monomeric and dimeric species are observed after 24 h dialysis of the enzyme denatured with guanidine-HCl. Both the monomeric and dimeric forms recovered after dialysis are active Sus scrofa
tetramer 4 * 70000 Sus scrofa

Synonyms

Synonyms Comment Organism
APH
-
Sus scrofa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
461
-
N-acetyl-Ala-p-nitroanilide pH 7.5 Sus scrofa