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Literature summary for 3.4.19.1 extracted from

  • Harmat, V.; Domokos, K.; Menyhard, D.K.; Pallo, A.; Szeltner, Z.; Szamosi, I.; Beke-Somfai, T.; Naray-Szabo, G., Polgar, L.
    Structure and catalysis of acylaminoacyl peptidase: closed and open subunits of a dimer oligopeptidase (2011), J. Biol. Chem., 286, 1987-1998.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop method, crystal structure determination of the native and two mutant structures (D524N and D524A) Aeropyrum pernix

Protein Variants

Protein Variants Comment Organism
D524A the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme Aeropyrum pernix
D524N the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme Aeropyrum pernix

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00129
-
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala pH 7.0, 70°C, wild-type enzyme Aeropyrum pernix
0.00281
-
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala pH 7.0, 70°C, mutant enzyme D524N Aeropyrum pernix
0.00566
-
N-acetyl-Phe-2-naphthylamide pH 7.0, 70°C, wild-type enzyme Aeropyrum pernix
0.0071
-
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala pH 7.0, 70°C, mutant enzyme D524A Aeropyrum pernix

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
63030
-
-
Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YBQ2
-
-
Aeropyrum pernix DSM 11879 Q9YBQ2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O endopeptidase activity Aeropyrum pernix 2-aminobenzoyl-Ala-Leu-Phe + Gln-Gly-Pro-Phe(NO2)-Ala
-
?
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O endopeptidase activity Aeropyrum pernix DSM 11879 2-aminobenzoyl-Ala-Leu-Phe + Gln-Gly-Pro-Phe(NO2)-Ala
-
?
N-acetyl-Phe-2-naphthylamide + H2O
-
Aeropyrum pernix N-acetyl-Phe + 2-naphthylamine
-
?
N-acetyl-Phe-2-naphthylamide + H2O
-
Aeropyrum pernix DSM 11879 N-acetyl-Phe + 2-naphthylamine
-
?

Subunits

Subunits Comment Organism
homodimer the monomer subunit is composed of one hydrolase and one propeller domain. In the homodimeric structures only one subunit displayed the closed form of the enzyme. The other subunit exhibits an open gate to the catalytic site, thus revealing the structural basis that controls the oligopeptidase activity Aeropyrum pernix

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.000917
-
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala pH 7.0, 70°C, mutant enzyme D524A Aeropyrum pernix
0.00525
-
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala pH 7.0, 70°C, mutant enzyme D524N Aeropyrum pernix
4.28
-
N-acetyl-Phe-2-naphthylamide pH 7.0, 70°C, wild-type enzyme Aeropyrum pernix
8.2
-
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala pH 7.0, 70°C, wild-type enzyme Aeropyrum pernix

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
wild-type enzyme Aeropyrum pernix
9
-
the rate constants for the D524A and D524N variants increase to about pH 9 Aeropyrum pernix

pH Range

pH Minimum pH Maximum Comment Organism
5.8 8.8 pH 5.8: about% of maximal activity, pH 8.8: about% of maximal activity Aeropyrum pernix

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.129
-
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala pH 7.0, 70°C, mutant enzyme D524A Aeropyrum pernix
0.414
-
N-acetyl-Phe-2-naphthylamide pH 7.0, 70°C, mutant enzyme D524A, measured under first-order conditions Aeropyrum pernix
1.31
-
N-acetyl-Phe-2-naphthylamide pH 7.0, 70°C, mutant enzyme D524N, measured under first-order conditions Aeropyrum pernix
1.87
-
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala pH 7.0, 70°C, mutant enzyme D524N Aeropyrum pernix
865
-
N-acetyl-Phe-2-naphthylamide pH 7.0, 70°C, wild-type enzyme Aeropyrum pernix
6347
-
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala pH 7.0, 70°C, wild-type enzyme Aeropyrum pernix