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Literature summary for 3.4.19.1 extracted from

  • Kiss, A.L.; Pallo, A.; Naray-Szabo, G.; Harmat, V.; Polgar, L.
    Structural and kinetic contributions of the oxyanion binding site to the catalytic activity of acylaminoacyl peptidase (2008), J. Struct. Biol., 162, 312-323.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Aeropyrum pernix K1

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of the H367A mutant grown at 20°C in hanging drops, to 2.2 A resolution. Belongs to space group P212121 Aeropyrum pernix
the crystal structure of the H367A variant of ApAAP is determined and refined to a resolution of 2.2 A Aeropyrum pernix K1

Protein Variants

Protein Variants Comment Organism
H367A displays significantly reduced catalytic activity. Unlike the reaction of the wild-type, the reaction of the mutant displays completely linear temperature dependence. Its reaction is associated with unfavourable entropy of activation Aeropyrum pernix
H367A mutant, displays significantly reduced catalytic activity Aeropyrum pernix K1

Inhibitors

Inhibitors Comment Organism Structure
Ac-Phe-OH product-like inhibitor Aeropyrum pernix K1
Acetyl-Phe forms hydrogen bonds with both NH groups of the oxyanion binding site of AAP. In the mutant enzyme the NH bond of Gly369 points in a different direction Aeropyrum pernix

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0082
-
N-acetyl-Phe-2-naphthylamide wild-type enzyme Aeropyrum pernix K1
0.0082
-
acetyl-Phe-2-naphthylamide wild-type Aeropyrum pernix
0.1
-
acetyl-Phe-2-naphthylamide mutant H367A Aeropyrum pernix
0.1
-
N-acetyl-Phe-2-naphthylamide mutant H367A, larger than 0.1 Aeropyrum pernix K1

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
126100
-
calculated, dimer Aeropyrum pernix K1

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YBQ2
-
-
Aeropyrum pernix K1 Q9YBQ2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Aeropyrum pernix K1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-Phe-2-naphthylamide + H2O
-
Aeropyrum pernix acetyl-Phe + 2-naphthylamine
-
?
N-acetyl-Phe-2-naphthylamide + H2O kinetic assay Aeropyrum pernix K1 N-acetyl-L-Phe + 2-naphthylamine
-
?

Subunits

Subunits Comment Organism
homodimer
-
Aeropyrum pernix K1

Synonyms

Synonyms Comment Organism
AAP
-
Aeropyrum pernix K1
AAP
-
Aeropyrum pernix
acylaminoacyl peptidase
-
Aeropyrum pernix K1
ApAAP
-
Aeropyrum pernix K1

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
-
Aeropyrum pernix K1
74
-
wild-type Aeropyrum pernix

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
90
-
both the wild-type and the H367A mutant are stable up to 90°C but tend to denature at higher temperature, more readily with the mutant. At lower temperature the wild-type has more flexible structural elements, particularly at 25°C, but differences diminish with increase of temperature Aeropyrum pernix

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Aeropyrum pernix K1

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0105
-
Ac-Phe-OH wild-type enzyme Aeropyrum pernix K1
0.0105
-
Acetyl-Phe wild-type Aeropyrum pernix
0.0178
-
Acetyl-Phe mutant H367A Aeropyrum pernix
0.0178
-
Ac-Phe-OH mutant H367A Aeropyrum pernix K1