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Literature summary extracted from

  • Kiss, A.L.; Hornung, B.; Radi, K.; Gengeliczki, Z.; Sztaray, B.; Juhasz, T.; Szeltner, Z.; Harmat, V.; Polgar, L.
    The acylaminoacyl peptidase from Aeropyrum pernix K1 thought to be an exopeptidase displays endopeptidase activity (2007), J. Mol. Biol., 368, 509-520.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.4.19.1 degradation AAP displays both exo- and endopeptidase activities Aeropyrum pernix K1

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.19.1 into pET22b vector and transformed into Rozetta DE3 Escherichia coli strain Aeropyrum pernix K1

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.19.1 by hanging drop method. AAP crystallized with the product-like inhibitors Ac-Phe and Gly-Phe, as well as with the substrate Abz-GFEPF(NO2)RA. Mutant S445A crystallized with Abz-GFEPF(NO2)RA. Complexes belong to P212121. Crystal structures of AAP–inhibitor complexes reveal the oxyanion-binding site and the specificities of the S1, S2 and S3 subsites. Substrate-binding site extends beyond the S2 subsite, being capable of binding peptides with a longer N-terminus. The S2 subsite displays a non-polar character. The S3 site reveals a hydrophobic region that does not form hydrogen bonds with the inhibitor P3 residue. The enzyme–inhibitor complexes reveal that, upon ligand-binding, the S1 subsite undergoes significant conformational changes Aeropyrum pernix K1

Protein Variants

EC Number Protein Variants Comment Organism
3.4.19.1 S445A nearly inactive. Remaining activity of the mutant can cause cleavage in the peptide Aeropyrum pernix K1

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.19.1 Acetyl-Phe
-
 Aeropyrum pernix K1
3.4.19.1 Gly-Phe
-
 Aeropyrum pernix K1

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.19.1 2-aminobenzoyl-EALFQGPF(NO2)A + H2O very good substrate Aeropyrum pernix K1 ?
-
 ?
3.4.19.1 2-aminobenzoyl-EFSPF(NO2)RA + H2O
-
 Aeropyrum pernix K1 ?
-
 ?
3.4.19.1 2-aminobenzoyl-GFEPF(NO2)RA + H2O good substrate, displays greater kinetic specificity than acetyl-Phe-2-naphthylamide Aeropyrum pernix K1 ?
-
 ?
3.4.19.1 2-aminobenzoyl-KARVLF(NO2)EA-Nle + H2O poor substrate Aeropyrum pernix K1 ?
-
 ?
3.4.19.1 2-aminobenzoyl-RPIITTAGPSF(NO2)A + H2O
-
 Aeropyrum pernix K1 ?
-
 ?
3.4.19.1 2-aminobenzoyl-SAVLQSGF(NO2)A + H2O good substrate Aeropyrum pernix K1 ?
-
 ?
3.4.19.1 acetyl-Ala-7-amido-4-methylcoumarin + H2O very slow hydrolysis Aeropyrum pernix K1 ?
-
 ?
3.4.19.1 acetyl-Leu-4-nitroanilide + H2O specificity rate constant is lower by one order of magnitude for acetyl-Leu-4-nitroanilide than for acetyl-Phe-4-nitroanilide Aeropyrum pernix K1 acetyl-Leu + 4-nitroaniline
-
 ?
3.4.19.1 acetyl-Phe-2-naphthylamide + H2O classical substrate of AAP Aeropyrum pernix K1 ?
-
 ?
3.4.19.1 acetyl-Phe-4-nitroanilide + H2O specificity rate constant is lower by one order of magnitude for acetyl-Leu-4-nitroanilide than for acetyl-Phe-4-nitroanilide Aeropyrum pernix K1 acetyl-Phe + 4-nitroaniline
-
 ?
3.4.19.1 glutaryl-GGF-7-amido-4-methylcoumarin + H2O has a rate constant comparable to that of acetyl-Phe-2-naphthylamide Aeropyrum pernix K1 ?
-
 ?
3.4.19.1 Gly-Phe-2-naphthylamide + H2O
-
 Aeropyrum pernix K1 ?
-
 ?
3.4.19.1 succinyl-AAPF-2-naphthylamide + H2O hydrolysed at a significantly slower rate than acetyl-Phe-2-naphthylamide Aeropyrum pernix K1 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.19.1 dimer crystallography Aeropyrum pernix K1

Synonyms

EC Number Synonyms Comment Organism
3.4.19.1 AAP
-
 Aeropyrum pernix K1