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Literature summary 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)

EC Number Cloned (Comment) Organism
3.4.19.1
-
 Aeropyrum pernix K1

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.19.1 crystals of the H367A mutant grown at 20°C in hanging drops, to 2.2 A resolution. Belongs to space group P212121 Aeropyrum pernix
3.4.19.1 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

EC Number Protein Variants Comment Organism
3.4.19.1 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
3.4.19.1 H367A mutant, displays significantly reduced catalytic activity Aeropyrum pernix K1

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.19.1 Ac-Phe-OH product-like inhibitor Aeropyrum pernix K1
3.4.19.1 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.19.1 0.0082
-
 N-acetyl-Phe-2-naphthylamide wild-type enzyme Aeropyrum pernix K1
3.4.19.1 0.0082
-
 acetyl-Phe-2-naphthylamide wild-type Aeropyrum pernix
3.4.19.1 0.1
-
 acetyl-Phe-2-naphthylamide mutant H367A Aeropyrum pernix
3.4.19.1 0.1
-
 N-acetyl-Phe-2-naphthylamide mutant H367A, larger than 0.1 Aeropyrum pernix K1

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.19.1 126100
-
 calculated, dimer Aeropyrum pernix K1

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.1 Aeropyrum pernix Q9YBQ2
-
-
3.4.19.1 Aeropyrum pernix K1 Q9YBQ2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.19.1
-
 Aeropyrum pernix K1

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.4.19.1 homodimer
-
 Aeropyrum pernix K1

Synonyms

EC Number Synonyms Comment Organism
3.4.19.1 AAP
-
 Aeropyrum pernix K1
3.4.19.1 AAP
-
 Aeropyrum pernix
3.4.19.1 acylaminoacyl peptidase
-
 Aeropyrum pernix K1
3.4.19.1 ApAAP
-
 Aeropyrum pernix K1

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.19.1 70
-
-
 Aeropyrum pernix K1
3.4.19.1 74
-
 wild-type Aeropyrum pernix

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.19.1 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.19.1 8
-
-
 Aeropyrum pernix K1

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.19.1 0.0105
-
 Ac-Phe-OH wild-type enzyme Aeropyrum pernix K1
3.4.19.1 0.0105
-
 Acetyl-Phe wild-type Aeropyrum pernix
3.4.19.1 0.0178
-
 Acetyl-Phe mutant H367A Aeropyrum pernix
3.4.19.1 0.0178
-
 Ac-Phe-OH mutant H367A Aeropyrum pernix K1