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Literature summary extracted from

  • Menyhard, D.K.; Orgovan, Z.; Szeltner, Z.; Szamosi, I.; Harmat, V.
    Catalytically distinct states captured in a crystal lattice the substrate-bound and scavenger states of acylaminoacyl peptidase and their implications for functionality (2015), Acta Crystallogr. Sect. D, 71, 461-472 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.19.1 purified enzyme in complex with chloromethyl ketone inhibitor, hanging drop vapour diffusion method, for the complex crystal form: mixing of 0.003 ml of protein solution containing 0.221 mM ApAAP protein, and 0.56 mM inhibitor CMK in 20 mM Tris pH 7.5 buffer, with 0.003 ml of reservoir solution containing 78 mM sodium acetate, pH 4.5, 2.4% w/v PEG 4000, 6.7 mM dithiothreitol, and 0.44 mM EDTA, for apoenzyme crystal form: mixing of 0.003 ml of protein solution containing 0.158 mM ApAAP protein in 20 mM Tris pH 7.5 buffer, with 0.003 ml of reservoir solution containing 78 mM sodium acetate, pH 5.0, 2.2% w/v PEG 4000, 5.2 mM dithiothreitol, and 0.34 mM EDTA, 20°C, X-ray diffraction structure determination and analysis at 1.90A and 2.55A resolution, modeling Aeropyrum pernix

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.19.1 benzyloxycarbonyl-Gly-Gly-Phe-chloromethyl ketone CMK, chloromethyl ketone inhibitor, enzyme binding structure analysis, molecular dynamics studies, overview Aeropyrum pernix

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.1 Aeropyrum pernix Q9YBQ2
-
-
3.4.19.1 Aeropyrum pernix ATCC 700893 Q9YBQ2
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-
3.4.19.1 Aeropyrum pernix DSM 11879 Q9YBQ2
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-
3.4.19.1 Aeropyrum pernix JCM 9820 Q9YBQ2
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-
3.4.19.1 Aeropyrum pernix NBRC 100138 Q9YBQ2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.19.1 additional information acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments Aeropyrum pernix ?
-
 ?
3.4.19.1 additional information acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments Aeropyrum pernix ATCC 700893 ?
-
 ?
3.4.19.1 additional information acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments Aeropyrum pernix DSM 11879 ?
-
 ?
3.4.19.1 additional information acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments Aeropyrum pernix JCM 9820 ?
-
 ?
3.4.19.1 additional information acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments Aeropyrum pernix NBRC 100138 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.19.1 AAP
-
 Aeropyrum pernix
3.4.19.1 acylaminoacyl peptidase
-
 Aeropyrum pernix
3.4.19.1 acylpeptide hydrolase
-
 Aeropyrum pernix
3.4.19.1 ApAAP
-
 Aeropyrum pernix
3.4.19.1 APEH
-
 Aeropyrum pernix

General Information

EC Number General Information Comment Organism
3.4.19.1 evolution acylaminoacyl peptidase is a member of the prolyl oligopeptidase protein family Aeropyrum pernix
3.4.19.1 additional information the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview Aeropyrum pernix