3.4.19.1 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 - ? 427894 3.4.19.1 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 - ? 427894 3.4.19.1 2-aminobenzoyl-EALFQGPF(NO2)A + H2O very good substrate Aeropyrum pernix K1 ? - ? 395436 3.4.19.1 2-aminobenzoyl-EFSPF(NO2)RA + H2O - Aeropyrum pernix K1 ? - ? 395437 3.4.19.1 2-aminobenzoyl-GFEPF(NO2)RA + H2O good substrate, displays greater kinetic specificity than acetyl-Phe-2-naphthylamide Aeropyrum pernix K1 ? - ? 395439 3.4.19.1 2-aminobenzoyl-KARVLF(NO2)EA-Nle + H2O poor substrate Aeropyrum pernix K1 ? - ? 395442 3.4.19.1 2-aminobenzoyl-RPIITTAGPSF(NO2)A + H2O - Aeropyrum pernix K1 ? - ? 395459 3.4.19.1 2-aminobenzoyl-SAVLQSGF(NO2)A + H2O good substrate Aeropyrum pernix K1 ? - ? 395468 3.4.19.1 2-naphthyl butyrate + H2O - Homo sapiens 2-naphthol + butanoate - ? 74051 3.4.19.1 4-nitrophenyl acetate + H2O - Homo sapiens 4-nitrophenol + acetate - ? 12514 3.4.19.1 4-nitrophenyl caprylate + H2O - Aeropyrum pernix 4-nitrophenol + caprylate - ? 363889 3.4.19.1 4-nitrophenyl caprylate + H2O - Homo sapiens 4-nitrophenol + caprylate - ? 363889 3.4.19.1 4-nitrophenyl caprylate + H2O - Aeropyrum pernix ATCC 700893 4-nitrophenol + caprylate - ? 363889 3.4.19.1 4-nitrophenyl caprylate + H2O - Aeropyrum pernix DSM 11879 4-nitrophenol + caprylate - ? 363889 3.4.19.1 4-nitrophenyl caprylate + H2O - Aeropyrum pernix JCM 9820 4-nitrophenol + caprylate - ? 363889 3.4.19.1 4-nitrophenyl caprylate + H2O - Aeropyrum pernix NBRC 100138 4-nitrophenol + caprylate - ? 363889 3.4.19.1 Abz-EFSPF(NO2)RA + H2O - Pyrococcus horikoshii ? - ? 404134 3.4.19.1 Abz-GFEPF(NO2)RA + H2O - Pyrococcus horikoshii ? - ? 404135 3.4.19.1 Abz-KARVLF(NO2)EANle + H2O - Pyrococcus horikoshii ? - ? 404136 3.4.19.1 Abz-SAVLQSGF(NO2)A + H2O - Pyrococcus horikoshii ? - ? 404151 3.4.19.1 Ac-Ala-4-nitroanilide + H2O - Mus musculus acetyl-Ala + 4-nitroaniline - ? 431556 3.4.19.1 Ac-Ala-7-amido-4-methylcoumarin + H2O - Pyrococcus horikoshii N-acetyl-L-Ala + 7-amino-4-methylcoumarin - ? 404156 3.4.19.1 Ac-Ala-Ala + H2O - Aeropyrum pernix Ac-Ala + Ala - ? 449475 3.4.19.1 Ac-Ala-Ala + H2O - Sulfurisphaera tokodaii Ac-Ala + Ala - ? 449475 3.4.19.1 Ac-Ala-Ala + H2O - Aeropyrum pernix ATCC 700893 Ac-Ala + Ala - ? 449475 3.4.19.1 Ac-Ala-Ala + H2O - Aeropyrum pernix DSM 11879 Ac-Ala + Ala - ? 449475 3.4.19.1 Ac-Ala-Ala + H2O - Aeropyrum pernix JCM 9820 Ac-Ala + Ala - ? 449475 3.4.19.1 Ac-Ala-Ala + H2O - Sulfurisphaera tokodaii 7 Ac-Ala + Ala - ? 449475 3.4.19.1 Ac-Ala-Ala + H2O - Sulfurisphaera tokodaii DSM 16993 Ac-Ala + Ala - ? 449475 3.4.19.1 Ac-Ala-Ala + H2O - Sulfurisphaera tokodaii JCM 10545 Ac-Ala + Ala - ? 449475 3.4.19.1 Ac-Ala-Ala + H2O - Aeropyrum pernix NBRC 100138 Ac-Ala + Ala - ? 449475 3.4.19.1 Ac-Ala-Ala + H2O - Sulfurisphaera tokodaii NBRC 100140 Ac-Ala + Ala - ? 449475 3.4.19.1 Ac-Ala-Ala-Ala + H2O - Aeropyrum pernix Ac-Ala + Ala-Ala - ? 449476 3.4.19.1 Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii Ac-Ala + Ala-Ala - ? 449476 3.4.19.1 Ac-Ala-Ala-Ala + H2O - Aeropyrum pernix ATCC 700893 Ac-Ala + Ala-Ala - ? 449476 3.4.19.1 Ac-Ala-Ala-Ala + H2O - Aeropyrum pernix DSM 11879 Ac-Ala + Ala-Ala - ? 449476 3.4.19.1 Ac-Ala-Ala-Ala + H2O - Aeropyrum pernix JCM 9820 Ac-Ala + Ala-Ala - ? 449476 3.4.19.1 Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii 7 Ac-Ala + Ala-Ala - ? 449476 3.4.19.1 Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii DSM 16993 Ac-Ala + Ala-Ala - ? 449476 3.4.19.1 Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii JCM 10545 Ac-Ala + Ala-Ala - ? 449476 3.4.19.1 Ac-Ala-Ala-Ala + H2O - Aeropyrum pernix NBRC 100138 Ac-Ala + Ala-Ala - ? 449476 3.4.19.1 Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii NBRC 100140 Ac-Ala + Ala-Ala - ? 449476 3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O - Aeropyrum pernix Ac-Ala + Ala-Ala-Ala - ? 449477 3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O - Sulfurisphaera tokodaii Ac-Ala + Ala-Ala-Ala - ? 449477 3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O - Aeropyrum pernix ATCC 700893 Ac-Ala + Ala-Ala-Ala - ? 449477 3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O - Aeropyrum pernix DSM 11879 Ac-Ala + Ala-Ala-Ala - ? 449477 3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O - Aeropyrum pernix JCM 9820 Ac-Ala + Ala-Ala-Ala - ? 449477 3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O - Sulfurisphaera tokodaii 7 Ac-Ala + Ala-Ala-Ala - ? 449477 3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O - Sulfurisphaera tokodaii DSM 16993 Ac-Ala + Ala-Ala-Ala - ? 449477 3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O - Sulfurisphaera tokodaii JCM 10545 Ac-Ala + Ala-Ala-Ala - ? 449477 3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O - Aeropyrum pernix NBRC 100138 Ac-Ala + Ala-Ala-Ala - ? 449477 3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O - Sulfurisphaera tokodaii NBRC 100140 Ac-Ala + Ala-Ala-Ala - ? 449477 3.4.19.1 Ac-Leu-4-nitroanilide + H2O - Pyrococcus horikoshii N-acetyl-L-Leu + 4-nitroaniline - ? 404166 3.4.19.1 Ac-Leu-4-nitroanilide + H2O - Aeropyrum pernix Ac-Leu + 4-nitroaniline - ? 449489 3.4.19.1 Ac-Leu-p-nitroanilide + H2O substrate peptidase assay Aeropyrum pernix K1 Ac-Leu + p-nitroaniline - ? 404169 3.4.19.1 Ac-Phe-2-naphthylamide + H2O - Pyrococcus horikoshii ? - ? 404171 3.4.19.1 Ac-Phe-2-naphthylamide + H2O - Pyrococcus horikoshii N-acetyl-L-Phe + 2-naphthylamine - ? 404172 3.4.19.1 Ac-Phe-4-nitroanilide + H2O - Pyrococcus horikoshii N-acetyl-L-Phe + 4-nitroaniline - ? 404173 3.4.19.1 acetyl-Ala-4-nitroanilide + H2O - Trematomus bernacchii acetyl-Ala + 4-nitroaniline - ? 355544 3.4.19.1 acetyl-Ala-4-nitroanilide + H2O the enzyme releases acetyl-Leu better than acetyl-Ala from acetyl-amino acid-4-nitroanilides Pyrococcus horikoshii acetyl-Ala + 4-nitroaniline - ? 355544 3.4.19.1 acetyl-Ala-7-amido-4-methylcoumarin + H2O very slow hydrolysis Aeropyrum pernix K1 ? - ? 396205 3.4.19.1 acetyl-Ala-7-amido-4-methylcoumarin + H2O - synthetic construct acetyl-Ala + 7-amino-4-methylcoumarin - ? 396206 3.4.19.1 acetyl-Ala-Ala + H2O - Cucumis sativus acetyl-Ala + Ala - ? 365073 3.4.19.1 acetyl-Ala-Ala + H2O - Arabidopsis thaliana acetyl-Ala + Ala - ? 365073 3.4.19.1 acetyl-Ala-Ala + H2O - Pyrococcus horikoshii acetyl-Ala + Ala - ? 365073 3.4.19.1 acetyl-Ala-Ala methyl ester + H2O - Homo sapiens ? - ? 74076 3.4.19.1 Acetyl-Ala-Ala-Ala + H2O native enzyme shows 147% of the activity compared to acetyl-Ala-Ala as substrate Cucumis sativus Acetyl-Ala + Ala-Ala - ? 14892 3.4.19.1 Acetyl-Ala-Ala-Ala + H2O native enzyme shows 81% of the activity compared to acetyl-Ala-Ala as substrate Arabidopsis thaliana Acetyl-Ala + Ala-Ala - ? 14892 3.4.19.1 acetyl-Ala-Ala-Ala-Ala + H2O - Pyrococcus horikoshii acetyl-Ala + Ala-Ala-Ala - ? 365074 3.4.19.1 acetyl-Ala-Ala-Ala-Ala + H2O native enzyme shows 126% of the activity compared to acetyl-Ala-Ala as substrate Arabidopsis thaliana acetyl-Ala + Ala-Ala-Ala - ? 365074 3.4.19.1 acetyl-Ala-Ala-Ala-Ala + H2O native enzyme shows 85.6% of the activity compared to acetyl-Ala-Ala as substrate Cucumis sativus acetyl-Ala + Ala-Ala-Ala - ? 365074 3.4.19.1 acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O - Pyrococcus horikoshii acetyl-Ala + Ala-Ala-Ala-Ala-Ala - ? 443008 3.4.19.1 acetyl-Ala-Ala-Phe-Gly + H2O - Oryctolagus cuniculus ? - ? 74036 3.4.19.1 acetyl-Ala-Gly-D-Ala-Ala + H2O - Oryctolagus cuniculus ? - ? 74038 3.4.19.1 acetyl-Ala-Met + H2O native enzyme shows 70.4% of the activity compared to acetyl-Ala-Ala as substrate Cucumis sativus acetyl-Ala + Met - ? 365081 3.4.19.1 acetyl-Gly-Gly + H2O native enzyme shows 37% of the activity compared to acetyl-Ala-Ala as substrate Cucumis sativus acetyl-Gly + Gly - ? 365080 3.4.19.1 acetyl-Gly-Gly + H2O native enzyme shows 4% of the activity compared to acetyl-Ala-Ala as substrate Arabidopsis thaliana acetyl-Gly + Gly - ? 365080 3.4.19.1 acetyl-Gly-Leu + H2O native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate Cucumis sativus acetyl-Gly + Leu - ? 365083 3.4.19.1 acetyl-Leu-4-nitroanilide + H2O - Trematomus bernacchii acetyl-Leu + 4-nitroaniline - ? 396335 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 - ? 396335 3.4.19.1 acetyl-Leu-4-nitroanilide + H2O the enzyme releases acetyl-Leu better than acetyl-Ala from acetyl-amino acid-4-nitroanilides Pyrococcus horikoshii acetyl-Leu + 4-nitroaniline - ? 396335 3.4.19.1 acetyl-Met-7-amido-4-methylcoumarin + H2O - Trematomus bernacchii acetyl-Met + 7-amino-4-methylcoumarin - ? 431565 3.4.19.1 acetyl-Met-Ala + H2O - Pyrococcus horikoshii acetyl-Met + Ala - ? 365077 3.4.19.1 acetyl-Met-Ala + H2O native enzyme shows 4% of the activity compared to acetyl-Ala-Ala as substrate Cucumis sativus acetyl-Met + Ala - ? 365077 3.4.19.1 acetyl-Met-Ala + H2O native enzyme shows 45% of the activity compared to acetyl-Ala-Ala as substrate Arabidopsis thaliana acetyl-Met + Ala - ? 365077 3.4.19.1 acetyl-Met-Ala-Ala-Ala-Ala-Ala + H2O - Pyrococcus horikoshii acetyl-Met + Ala-Ala-Ala-Ala-Ala - ? 443009 3.4.19.1 acetyl-Met-Asn + H2O native enzyme shows 34.1% of the activity compared to acetyl-Ala-Ala as substrate Cucumis sativus acetyl-Met + Asn - ? 365082 3.4.19.1 acetyl-Met-Glu + H2O native enzyme shows 4.3% of the activity compared to acetyl-Ala-Ala as substrate Cucumis sativus acetyl-Met + Glu - ? 365078 3.4.19.1 acetyl-Met-Glu + H2O native enzyme shows 6% of the activity compared to acetyl-Ala-Ala as substrate Arabidopsis thaliana acetyl-Met + Glu - ? 365078 3.4.19.1 acetyl-Met-Phe + H2O native enzyme shows 5% of the activity compared to acetyl-Ala-Ala as substrate Arabidopsis thaliana acetyl-Met + Phe - ? 365079 3.4.19.1 acetyl-Phe-2-naphthylamide + H2O classical substrate of AAP Aeropyrum pernix K1 ? - ? 396336 3.4.19.1 acetyl-Phe-2-naphthylamide + H2O - Aeropyrum pernix acetyl-Phe + 2-naphthylamine - ? 396337 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 - ? 396338 3.4.19.1 acetyl-Tyr-4-nitroanilide + H2O - Pyrococcus horikoshii acetyl-Tyr + 4-nitroaniline - ? 443010 3.4.19.1 Ala-Ala + H2O - Sulfurisphaera tokodaii Ala + Ala - ? 36448 3.4.19.1 Ala-Ala + H2O - Sulfurisphaera tokodaii 7 Ala + Ala - ? 36448 3.4.19.1 Ala-Ala-Ala + H2O - Sus scrofa Ala-Ala + Ala - ? 36604 3.4.19.1 Ala-Ala-Ala + H2O - Sulfurisphaera tokodaii Ala + Ala-Ala - ? 364820 3.4.19.1 Ala-Ala-Ala + H2O - Sulfurisphaera tokodaii 7 Ala + Ala-Ala - ? 364820 3.4.19.1 Ala-Ala-Ala-Ala + H2O - Sus scrofa Ala-Ala + Ala-Ala - ? 14898 3.4.19.1 Ala-Ala-Ala-Ala + H2O - Sulfurisphaera tokodaii Ala + Ala-Ala-Ala - ? 425900 3.4.19.1 Ala-beta-naphthylamide + H2O - Streptomyces morookaense Ala + 2-naphthylamine - ? 396359 3.4.19.1 Ala-beta-naphthylamide + H2O - Streptomyces morookaense JCM 4673 Ala + 2-naphthylamine - ? 396359 3.4.19.1 Ala-p-nitroanilide + H2O prefered substrate for PMH Streptomyces morookaense Ala + p-nitroaniline - ? 36246 3.4.19.1 Ala-p-nitroanilide + H2O prefered substrate for PMH Streptomyces morookaense JCM 4673 Ala + p-nitroaniline - ? 36246 3.4.19.1 alpha-melanocyte stimulating hormone + H2O - Bos taurus ? - ? 16611 3.4.19.1 amyloid-beta peptide + H2O - Homo sapiens ? - ? 367380 3.4.19.1 Asp-Ala-p-nitroanilide + H2O - Sus scrofa ? - ? 404370 3.4.19.1 Asp-Pro-p-nitroanilide + H2O - Sus scrofa ? - ? 404373 3.4.19.1 butyryl thiocholine + H2O - Homo sapiens ? - ? 74073 3.4.19.1 butyryl-Ala-Ala-Ala + H2O native enzyme shows 33.6% of the activity compared to acetyl-Ala-Ala as substrate Cucumis sativus butyryl-Ala + Ala-Ala - ? 365075 3.4.19.1 butyryl-Ala-Ala-Ala + H2O native enzyme shows 77% of the activity compared to acetyl-Ala-Ala as substrate Arabidopsis thaliana butyryl-Ala + Ala-Ala - ? 365075 3.4.19.1 formyl-Ala-Ala-Ala + H2O - Sulfurisphaera tokodaii formyl-Ala + Ala-Ala - ? 365076 3.4.19.1 formyl-Ala-Ala-Ala + H2O - Pyrococcus horikoshii formyl-Ala + Ala-Ala - ? 365076 3.4.19.1 formyl-Ala-Ala-Ala + H2O native enzyme shows 62.4% of the activity compared to acetyl-Ala-Ala as substrate Cucumis sativus formyl-Ala + Ala-Ala - ? 365076 3.4.19.1 formyl-Ala-Ala-Ala + H2O native enzyme shows 81% of the activity compared to acetyl-Ala-Ala as substrate Arabidopsis thaliana formyl-Ala + Ala-Ala - ? 365076 3.4.19.1 formyl-Ala-Ala-Ala + H2O - Sulfurisphaera tokodaii 7 formyl-Ala + Ala-Ala - ? 365076 3.4.19.1 formyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O - Pyrococcus horikoshii formyl-Ala + Ala-Ala-Ala-Ala-Ala - ? 443569 3.4.19.1 formyl-Gly-Val + H2O native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate Cucumis sativus formyl-Gly + Val - ? 365084 3.4.19.1 formyl-Met-Ala + H2O - Pyrococcus horikoshii formyl-Met + Ala - ? 443570 3.4.19.1 formyl-Met-Ala-Ala-Ala-Ala-Ala + H2O - Pyrococcus horikoshii formyl-Met + Ala-Ala-Ala-Ala-Ala - ? 443571 3.4.19.1 formyl-Met-Ala-Ser + H2O - Pyrococcus horikoshii formyl-Met + Ala-Ser - ? 443572 3.4.19.1 formyl-Met-Leu-Gly + H2O - Pyrococcus horikoshii formyl-Met + Leu-Gly - ? 443573 3.4.19.1 formylalanine-Ala-Ala + H2O - Pyrococcus horikoshii ? - ? 74063 3.4.19.1 formylalanine-Ala-Ala-Ala-Ala-Ala + H2O - Pyrococcus horikoshii ? - ? 74065 3.4.19.1 formylmethionine p-nitroanilide + H2O - Bos taurus formylmethionine + p-nitroaniline - ? 74066 3.4.19.1 formylmethionine-Ala + H2O - Pyrococcus horikoshii formylmethionine + Ala - ? 74061 3.4.19.1 formylmethionine-Ala-Ala-Ala-Ala-Ala + H2O - Pyrococcus horikoshii ? - ? 74064 3.4.19.1 formylmethionine-Ala-Ser + H2O - Pyrococcus horikoshii ? - ? 74060 3.4.19.1 formylmethionine-beta-naphthylamide + H2O - Rattus norvegicus formylmethionine + beta-naphthylamine - ? 74052 3.4.19.1 formylmethionine-Leu + H2O - Rattus norvegicus formylmethionine + Leu - ? 74059 3.4.19.1 formylmethionine-Leu-Gly + H2O - Pyrococcus horikoshii ? - ? 74062 3.4.19.1 formylmethionine-Leu-Phe + H2O - Rattus norvegicus ? - ? 74054 3.4.19.1 formylmethionine-Leu-Tyr + H2O - Rattus norvegicus ? - ? 74055 3.4.19.1 formylmethionine-Phe + H2O - Rattus norvegicus formylmethionine + Phe - ? 74058 3.4.19.1 formylmethionine-Trp + H2O - Rattus norvegicus formylmethionine + Trp - ? 74053 3.4.19.1 formylmethionine-Val + H2O - Rattus norvegicus formylmethionine + Val - ? 74057 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 ? - ? 397278 3.4.19.1 Gly-Ala-Ala + H2O - Sus scrofa Gly-Ala + Ala - ? 73972 3.4.19.1 Gly-Phe-2-naphthylamide + H2O - Pyrococcus horikoshii Gly-Phe + 2-naphthylamine - ? 36465 3.4.19.1 Gly-Phe-2-naphthylamide + H2O - Aeropyrum pernix K1 ? - ? 397339 3.4.19.1 glycated ribulose-1,5-diphosphate carboxylase/oxygenase protein + H2O no degradation of the native protein Cucumis sativus ? - ? 365085 3.4.19.1 isoAsp-Ala-p-nitroanilide + H2O - Sus scrofa ? - ? 405505 3.4.19.1 isoD/DAEFRHDSGYEVHHQKLVFFAEDVGSNKGA-NH2 + H2O - Sus scrofa ? - ? 405512 3.4.19.1 Leu-beta-naphthylamide + H2O - Streptomyces morookaense Leu + 2-naphthylamine - ? 397691 3.4.19.1 Leu-beta-naphthylamide + H2O - Streptomyces morookaense JCM 4673 Leu + 2-naphthylamine - ? 397691 3.4.19.1 additional information specific for N-terminal acylmethionine residues Rattus norvegicus ? - ? 89 3.4.19.1 additional information rapid removal of acetyl-Thr, acetyl-Ala, acetyl-Met, acetyl-Ser and more slowly acetyl-Gly from peptides of different lengths. Other N-acetylated amino acids, Cys, Tyr, Asp, Val, Phe, Ile, Leu, may be removed at 1% or less of the rate of the good substrates Oryctolagus cuniculus ? - ? 89 3.4.19.1 additional information the trypsin-modified enzyme is able to unblock alphaA-crystallin and displays endoprotease activity unlike the native enzyme Bos taurus ? - ? 89 3.4.19.1 additional information N-acetylated peptides with D-Ala in position 3 or 4 as are good substrates as those containing L-Ala. Peptides with Pro in position 2 are inactive, and most of the peptides with Pro in the third position are very good substrates. Only the peptide acetyl-AAP gives 30% of the activity of acetyl-AAA, which is reduced to 1-2% if additional residues are present at the C-terminus, acety-AAPA or acetyl-AAPAA. The presence of a positive charge in position 2,3,4,5 and 6 gives strong reduction in hydrolase activity, varying with the charge's distance from the N-terminus from 9 to 15-20% of the rate obtained with the reference peptides without positive charges. Deprotonation of His at high pH generates excellent substrates, and removal of the positive charges of Lys by acetylation or succinylation give improved substrate quality. Long peptides with 10-29 residues, are poor substrates, especially when they contain positive charges and Pro Oryctolagus cuniculus ? - ? 89 3.4.19.1 additional information peptidase activity is only exerted on peptides with Gly or Ala at their N-termini Sus scrofa ? - ? 89 3.4.19.1 additional information the enzyme might not only be involved in the catabolism of intracellular N-acylated protein catabolism but also be responsible for the biological utilization of N-acylated food proteins Sus scrofa ? - ? 89 3.4.19.1 additional information the enzyme may be involved in N-terminal deacylation of nascent polypeptide chains and of bioactive peptides Homo sapiens ? - ? 89 3.4.19.1 additional information the enzyme may be involved in regulation of neuropeptide turnover Sus scrofa ? - ? 89 3.4.19.1 additional information the enzyme might be involved in not only catalysis of the N-terminal hydrolysis of Nalpha-acylpeptides but also the elimination of glycated proteins Cucumis sativus ? - ? 89 3.4.19.1 additional information His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate Sus scrofa ? - ? 89 3.4.19.1 additional information catalyzes the NH2-terminal hydrolysis of N-acylpeptides to release N-acylated amino acids Sus scrofa ? - ? 89 3.4.19.1 additional information cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide Pyrococcus horikoshii ? - ? 89 3.4.19.1 additional information removal of an N-acylated amino acid from blocked peptides Aeropyrum pernix K1 ? - ? 89 3.4.19.1 additional information no activity with L-leucyl 4-nitroanilide or L-alanyl 4-nitroanilide. The enzyme is able to hydrolyse N-succinyl-Gly-Gly-Phe 4-nitroanilide, showing endopeptidase activity Saccharolobus solfataricus ? - ? 89 3.4.19.1 additional information no activity with L-leucyl 4-nitroanilide, L-alanyl 4-nitroanilide or L-phenylalanyl 4-nitroanilide. The enzyme also shows endopeptidase activity Saccharolobus solfataricus ? - ? 89 3.4.19.1 additional information hundreds nanosecond all-atom atomistic molecular dynamics simulations of a representative member of the acylaminoacyl peptidase subfamily (Aeropyrum pernix K1) allow to identify the presence of a tunnel which from the surrounding of the N-terminal alpha1-helix bring to the catalytic site and it is regulated by conformational changes of the N-terminal alpha-helix itself and its surroundings in the native conformational ensemble Aeropyrum pernix ? - ? 89 3.4.19.1 additional information no activity with L-Leu-4-nitroanilide, L-Ala-4-nitroanilide, or L-Phe-4-nitroanilide, succinyl-AAPF-4-nitroanilide, and succinyl-AAVA-4-nitroanilide Saccharolobus solfataricus ? - ? 89 3.4.19.1 additional information high hydrolytic activity for acylpeptides, no hydrolytic activity for Leu-4-nitroanilide and Ala-4-nitroanilide Pyrococcus horikoshii ? - ? 89 3.4.19.1 additional information APEH interacts with the amino-terminal domain of XRCC1 Homo sapiens ? - ? 89 3.4.19.1 additional information acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments Aeropyrum pernix ? - ? 89 3.4.19.1 additional information acylpeptide hydrolase (APEH) deacetylates N-alpha-acetylated peptides and selectively degrades oxidised protein Homo sapiens ? - ? 89 3.4.19.1 additional information enzyme APH catalyzes the N-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids Aeropyrum pernix ? - ? 89 3.4.19.1 additional information promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes Sulfurisphaera tokodaii ? - ? 89 3.4.19.1 additional information the acylaminoacyl peptidase from Bacillus subtilis strain 168 catalyzes the removal of an acylated amino acid from Nalpha-acylpeptides, but it also catalyzes the aldol reaction with high enantioselectivity providing optically active secondary alcohols with satisfying enantioselectivity of 84.6% enantiomeric excess Bacillus subtilis ? - ? 89 3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview Aeropyrum pernix ? - ? 89 3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition Sulfurisphaera tokodaii ? - ? 89 3.4.19.1 additional information the enzyme catalyzes the NH2-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids, but it also exhibits esterase activity and catalyzes the aldol reaction between acetone and 4-nitrobenzaldehyde. Comparison of kinetic parameters of ST0779- and porcine pancreatic lipase (PPL)-mediated aldol reaction between acetone and 4-nitrobenzaldehyde, catalytic reaction mechanism, overview Sulfurisphaera tokodaii ? - ? 89 3.4.19.1 additional information the enzyme is also active with fatty acid esters, e.g. with 4-nitrophenyl caprylate. Substrate binding mechanism analysis, and random acceleration and steered molecular dynamics simulations of ligands unbinding pathways from APH. Three main pathways are observed most frequently, namely P1, P2A, and P3, evaluation by comparing the average force profiles and potential of mean force calculations revealing that P3 is the unbinding pathway. Overview Aeropyrum pernix ? - ? 89 3.4.19.1 additional information acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments Aeropyrum pernix ATCC 700893 ? - ? 89 3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview Aeropyrum pernix ATCC 700893 ? - ? 89 3.4.19.1 additional information hundreds nanosecond all-atom atomistic molecular dynamics simulations of a representative member of the acylaminoacyl peptidase subfamily (Aeropyrum pernix K1) allow to identify the presence of a tunnel which from the surrounding of the N-terminal alpha1-helix bring to the catalytic site and it is regulated by conformational changes of the N-terminal alpha-helix itself and its surroundings in the native conformational ensemble Aeropyrum pernix DSM 11879 ? - ? 89 3.4.19.1 additional information acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments Aeropyrum pernix DSM 11879 ? - ? 89 3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview Aeropyrum pernix DSM 11879 ? - ? 89 3.4.19.1 additional information no activity with L-leucyl 4-nitroanilide or L-alanyl 4-nitroanilide. The enzyme is able to hydrolyse N-succinyl-Gly-Gly-Phe 4-nitroanilide, showing endopeptidase activity Saccharolobus solfataricus P2 ? - ? 89 3.4.19.1 additional information no activity with L-leucyl 4-nitroanilide, L-alanyl 4-nitroanilide or L-phenylalanyl 4-nitroanilide. The enzyme also shows endopeptidase activity Saccharolobus solfataricus P2 ? - ? 89 3.4.19.1 additional information no activity with L-Leu-4-nitroanilide, L-Ala-4-nitroanilide, or L-Phe-4-nitroanilide, succinyl-AAPF-4-nitroanilide, and succinyl-AAVA-4-nitroanilide Saccharolobus solfataricus P2 ? - ? 89 3.4.19.1 additional information the acylaminoacyl peptidase from Bacillus subtilis strain 168 catalyzes the removal of an acylated amino acid from Nalpha-acylpeptides, but it also catalyzes the aldol reaction with high enantioselectivity providing optically active secondary alcohols with satisfying enantioselectivity of 84.6% enantiomeric excess Bacillus subtilis 168 ? - ? 89 3.4.19.1 additional information acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments Aeropyrum pernix JCM 9820 ? - ? 89 3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview Aeropyrum pernix JCM 9820 ? - ? 89 3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition Sulfurisphaera tokodaii 7 ? - ? 89 3.4.19.1 additional information promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes Sulfurisphaera tokodaii 7 ? - ? 89 3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition Sulfurisphaera tokodaii DSM 16993 ? - ? 89 3.4.19.1 additional information promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes Sulfurisphaera tokodaii DSM 16993 ? - ? 89 3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition Sulfurisphaera tokodaii JCM 10545 ? - ? 89 3.4.19.1 additional information promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes Sulfurisphaera tokodaii JCM 10545 ? - ? 89 3.4.19.1 additional information the enzyme catalyzes the NH2-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids, but it also exhibits esterase activity and catalyzes the aldol reaction between acetone and 4-nitrobenzaldehyde. Comparison of kinetic parameters of ST0779- and porcine pancreatic lipase (PPL)-mediated aldol reaction between acetone and 4-nitrobenzaldehyde, catalytic reaction mechanism, overview Sulfurisphaera tokodaii JCM 10545 ? - ? 89 3.4.19.1 additional information acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments Aeropyrum pernix NBRC 100138 ? - ? 89 3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview Aeropyrum pernix NBRC 100138 ? - ? 89 3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition Sulfurisphaera tokodaii NBRC 100140 ? - ? 89 3.4.19.1 additional information promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes Sulfurisphaera tokodaii NBRC 100140 ? - ? 89 3.4.19.1 additional information the enzyme catalyzes the NH2-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids, but it also exhibits esterase activity and catalyzes the aldol reaction between acetone and 4-nitrobenzaldehyde. Comparison of kinetic parameters of ST0779- and porcine pancreatic lipase (PPL)-mediated aldol reaction between acetone and 4-nitrobenzaldehyde, catalytic reaction mechanism, overview Sulfurisphaera tokodaii 7T ? - ? 89 3.4.19.1 N-acetyl-Ala ethyl ester + H2O - Homo sapiens N-acetyl-Ala + ethanol - ? 74048 3.4.19.1 N-acetyl-Ala p-nitroanilide + H2O - Homo sapiens N-acetyl-Ala + p-nitroaniline - ? 74045 3.4.19.1 N-acetyl-Ala p-nitroanilide + H2O - Rattus norvegicus N-acetyl-Ala + p-nitroaniline - ? 74045 3.4.19.1 N-acetyl-Ala p-nitroanilide + H2O - Sus scrofa N-acetyl-Ala + p-nitroaniline - ? 74045 3.4.19.1 N-acetyl-Ala p-nitroanilide + H2O - Bos taurus N-acetyl-Ala + p-nitroaniline - ? 74045 3.4.19.1 N-acetyl-Ala p-nitroanilide + H2O - Pyrococcus horikoshii N-acetyl-Ala + p-nitroaniline - ? 74045 3.4.19.1 N-acetyl-Ala-Ala + H2O - Homo sapiens N-acetyl-Ala + Ala - ? 74002 3.4.19.1 N-acetyl-Ala-Ala + H2O - Rattus norvegicus N-acetyl-Ala + Ala - ? 74002 3.4.19.1 N-acetyl-Ala-Ala + H2O - Sus scrofa N-acetyl-Ala + Ala - ? 74002 3.4.19.1 N-acetyl-Ala-Ala + H2O - Oryctolagus cuniculus N-acetyl-Ala + Ala - ? 74002 3.4.19.1 N-acetyl-Ala-Ala + H2O - Pyrococcus horikoshii N-acetyl-Ala + Ala - ? 74002 3.4.19.1 N-acetyl-Ala-Ala + H2O - Sulfurisphaera tokodaii N-acetyl-Ala + Ala - ? 74002 3.4.19.1 N-acetyl-Ala-Ala + H2O N-acetyl-Ala-Ala Homo sapiens N-acetyl-Ala + Ala - ? 74002 3.4.19.1 N-acetyl-Ala-Ala + H2O - Sulfurisphaera tokodaii 7 N-acetyl-Ala + Ala - ? 74002 3.4.19.1 N-acetyl-Ala-Ala-Ala + H2O - Homo sapiens N-acetyl-Ala + Ala-Ala - ? 64967 3.4.19.1 N-acetyl-Ala-Ala-Ala + H2O - Rattus norvegicus N-acetyl-Ala + Ala-Ala - ? 64967 3.4.19.1 N-acetyl-Ala-Ala-Ala + H2O - Sus scrofa N-acetyl-Ala + Ala-Ala - ? 64967 3.4.19.1 N-acetyl-Ala-Ala-Ala + H2O - Oryctolagus cuniculus N-acetyl-Ala + Ala-Ala - ? 64967 3.4.19.1 N-acetyl-Ala-Ala-Ala + H2O - Ovis aries N-acetyl-Ala + Ala-Ala - ? 64967 3.4.19.1 N-acetyl-Ala-Ala-Ala + H2O - Sulfurisphaera tokodaii N-acetyl-Ala + Ala-Ala - ? 64967 3.4.19.1 N-acetyl-Ala-Ala-Ala + H2O N-acetyl-Ala-Ala-Ala Homo sapiens N-acetyl-Ala + Ala-Ala - ? 64967 3.4.19.1 N-acetyl-Ala-Ala-Ala + H2O - Sulfurisphaera tokodaii 7 N-acetyl-Ala + Ala-Ala - ? 64967 3.4.19.1 N-acetyl-Ala-Ala-Ala-Ala + H2O - Homo sapiens N-acetyl-Ala + Ala-Ala-Ala - ? 74024 3.4.19.1 N-acetyl-Ala-Ala-Ala-Ala + H2O - Sus scrofa N-acetyl-Ala + Ala-Ala-Ala - ? 74024 3.4.19.1 N-acetyl-Ala-Ala-Ala-Ala + H2O - Oryctolagus cuniculus N-acetyl-Ala + Ala-Ala-Ala - ? 74024 3.4.19.1 N-acetyl-Ala-Ala-Ala-Ala + H2O - Pyrococcus horikoshii N-acetyl-Ala + Ala-Ala-Ala - ? 74024 3.4.19.1 N-acetyl-Ala-Ala-Ala-Ala-Ala + H2O - Homo sapiens ? - ? 74025 3.4.19.1 N-acetyl-Ala-Ala-Ala-Ala-Ala + H2O - Oryctolagus cuniculus ? - ? 74025 3.4.19.1 N-acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O - Homo sapiens ? - ? 74026 3.4.19.1 N-acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O - Oryctolagus cuniculus ? - ? 74026 3.4.19.1 N-acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O - Pyrococcus horikoshii ? - ? 74026 3.4.19.1 N-acetyl-Ala-Ala-Ala-Ala-Glu-Glu-Glu-Lys + H2O - Homo sapiens ? - ? 74027 3.4.19.1 N-acetyl-Ala-Ala-Arg-Gly + H2O - Oryctolagus cuniculus N-acetyl-Ala + Ala-Arg-Gly - ? 452939 3.4.19.1 N-acetyl-Ala-Ala-Gln-Nepsilon-acetyl-Lys + H2O - Oryctolagus cuniculus ? - ? 74041 3.4.19.1 N-acetyl-Ala-Ala-Gln-Nepsilon-succinyl-Lys + H2O - Oryctolagus cuniculus ? - ? 74042 3.4.19.1 N-acetyl-Ala-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu + H2O - Oryctolagus cuniculus ? - ? 74040 3.4.19.1 N-acetyl-Ala-Ala-His-Ala + H2O - Oryctolagus cuniculus ? - ? 74035 3.4.19.1 N-acetyl-Ala-Ala-Phe-Gly + H2O - Oryctolagus cuniculus N-acetyl-Ala + Ala-Phe-Gly - ? 452940 3.4.19.1 N-acetyl-Ala-Ala-Pro + H2O - Oryctolagus cuniculus ? - ? 74037 3.4.19.1 N-acetyl-Ala-Ala-Pro-Ala + H2O - Oryctolagus cuniculus N-acetyl-Ala + Ala-Pro-Ala - ? 452941 3.4.19.1 N-acetyl-Ala-Asp + H2O - Rattus norvegicus N-acetyl-Ala + Asp - ? 74017 3.4.19.1 N-acetyl-Ala-beta-naphthylamide + H2O - Rattus norvegicus N-acetyl-Ala + beta-naphthylamine - ? 74030 3.4.19.1 N-acetyl-Ala-Gly + H2O - Rattus norvegicus N-acetyl-Ala + Gly - ? 74016 3.4.19.1 N-acetyl-Ala-Gly-Ala-D-Ala-Ala + H2O - Oryctolagus cuniculus ? - ? 74039 3.4.19.1 N-acetyl-Ala-His-Ala + H2O - Oryctolagus cuniculus ? - ? 74034 3.4.19.1 N-acetyl-Ala-Leu + H2O - Rattus norvegicus N-acetyl-Ala + Leu - ? 74015 3.4.19.1 N-acetyl-Ala-Lys + H2O - Homo sapiens N-acetyl-Ala + Lys - ? 74018 3.4.19.1 N-acetyl-Ala-Met + H2O - Rattus norvegicus N-acetyl-Ala + Met - ? 74014 3.4.19.1 N-acetyl-Ala-p-nitroanilide + H2O - Sus scrofa N-acetyl-Ala + p-nitroaniline - ? 365070 3.4.19.1 N-acetyl-Ala-p-nitroanilide + H2O substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide Cucumis sativus N-acetyl-Ala + p-nitroaniline - ? 365070 3.4.19.1 N-acetyl-Ala-p-nitroanilide + H2O substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide Arabidopsis thaliana N-acetyl-Ala + p-nitroaniline - ? 365070 3.4.19.1 N-acetyl-Ala-Phe + H2O - Rattus norvegicus N-acetyl-Ala + Phe - ? 74010 3.4.19.1 N-acetyl-Ala-Ser + H2O - Rattus norvegicus N-acetyl-Ala + Ser - ? 74012 3.4.19.1 N-acetyl-Ala-Thr + H2O - Rattus norvegicus N-acetyl-Ala + Thr - ? 74013 3.4.19.1 N-acetyl-Ala-Trp + H2O - Rattus norvegicus N-acetyl-Ala + Trp - ? 74009 3.4.19.1 N-acetyl-Ala-Tyr + H2O - Rattus norvegicus N-acetyl-Ala + Tyr - ? 74011 3.4.19.1 N-acetyl-Ala-Tyr-Ile + H2O - Homo sapiens ? - ? 74029 3.4.19.1 N-acetyl-alanyl-4-nitroanilide + H2O - Homo sapiens N-acetyl-L-Ala + 4-nitroaniline - ? 397850 3.4.19.1 N-acetyl-Glu p-nitroanilide + H2O - Homo sapiens N-acetyl-Glu + p-nitroaniline - ? 74049 3.4.19.1 N-acetyl-Gly-Ala + H2O weak activity Rattus norvegicus N-acetyl-Gly + Ala - ? 74007 3.4.19.1 N-acetyl-Gly-p-nitroanilide + H2O substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide Cucumis sativus N-acetyl-Gly + p-nitroaniline - ? 365072 3.4.19.1 N-acetyl-Gly-p-nitroanilide + H2O substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide Arabidopsis thaliana N-acetyl-Gly + p-nitroaniline - ? 365072 3.4.19.1 N-acetyl-L-Ala-4-nitroanilide + H2O - Saccharolobus solfataricus N-acetyl-L-Ala + 4-nitroaniline - ? 432175 3.4.19.1 N-acetyl-L-Ala-4-nitroanilide + H2O - Bombyx mori N-acetyl-L-Ala + 4-nitroaniline - ? 432175 3.4.19.1 N-acetyl-L-alanine 4-nitroanilide + H2O - Rattus norvegicus N-acetyl-L-alanine + 4-nitroaniline - ? 412491 3.4.19.1 N-acetyl-L-alanyl 4-nitroanilide + H2O - Saccharolobus solfataricus N-acetyl-L-alanine + 4-nitroaniline - ? 421017 3.4.19.1 N-acetyl-L-alanyl 4-nitroanilide + H2O - Saccharolobus solfataricus P2 N-acetyl-L-alanine + 4-nitroaniline - ? 421017 3.4.19.1 N-acetyl-L-alanyl-p-nitroanilide + H2O - Mus musculus N-acetyl-L-alanine + p-nitroaniline - ? 385238 3.4.19.1 N-acetyl-L-alanyl-p-nitroanilide + H2O - Homo sapiens N-acetyl-L-alanine + p-nitroaniline - ? 385238 3.4.19.1 N-acetyl-L-Leu-4-nitroanilide + H2O - Aeropyrum pernix N-acetyl-L-Leu + 4-nitroaniline - ? 432178 3.4.19.1 N-acetyl-L-Leu-4-nitroanilide + H2O - Saccharolobus solfataricus N-acetyl-L-Leu + 4-nitroaniline - ? 432178 3.4.19.1 N-acetyl-L-Leu-4-nitroanilide + H2O - Homo sapiens N-acetyl-L-Leu + 4-nitroaniline - ? 432178 3.4.19.1 N-acetyl-L-Leu-4-nitroanilide + H2O - Aeropyrum pernix ATCC 700893 N-acetyl-L-Leu + 4-nitroaniline - ? 432178 3.4.19.1 N-acetyl-L-Leu-4-nitroanilide + H2O - Aeropyrum pernix DSM 11879 N-acetyl-L-Leu + 4-nitroaniline - ? 432178 3.4.19.1 N-acetyl-L-Leu-4-nitroanilide + H2O - Aeropyrum pernix JCM 9820 N-acetyl-L-Leu + 4-nitroaniline - ? 432178 3.4.19.1 N-acetyl-L-Leu-4-nitroanilide + H2O - Aeropyrum pernix NBRC 100138 N-acetyl-L-Leu + 4-nitroaniline - ? 432178 3.4.19.1 N-acetyl-L-leucyl 4-nitroanilide + H2O - Saccharolobus solfataricus N-acetyl-L-leucine + 4-nitroaniline - ? 421020 3.4.19.1 N-acetyl-L-leucyl 4-nitroanilide + H2O preference for N-acetyl-L-leucyl 4-nitroanilide over N-acetyl-L-alanyl 4-nitroanilide Saccharolobus solfataricus N-acetyl-L-leucine + 4-nitroaniline - ? 421020 3.4.19.1 N-acetyl-L-leucyl 4-nitroanilide + H2O preference for N-acetyl-L-leucyl 4-nitroanilide over N-acetyl-L-alanyl 4-nitroanilide Saccharolobus solfataricus P2 N-acetyl-L-leucine + 4-nitroaniline - ? 421020 3.4.19.1 N-acetyl-L-leucyl 4-nitroanilide + H2O - Saccharolobus solfataricus P2 N-acetyl-L-leucine + 4-nitroaniline - ? 421020 3.4.19.1 N-acetyl-L-Met-alpha-L-Lys-Ala-NH2 + H2O - Sus scrofa N-acetyl-L-Met + L-Lys-Ala-NH2 - ? 74021 3.4.19.1 N-acetyl-L-Met-epsilon-L-Lys-Ala-NH2 + H2O - Sus scrofa N-acetyl-L-Met + L-Lys-L-Ala-NH2 - ? 74022 3.4.19.1 N-acetyl-L-Phe-4-nitroanilide + H2O - Saccharolobus solfataricus N-acetyl-L-Phe + 4-nitroaniline - ? 432179 3.4.19.1 N-acetyl-L-phenylalanyl 4-nitroanilide + H2O - Saccharolobus solfataricus N-acetyl-L-phenylalanine + 4-nitroaniline - ? 421023 3.4.19.1 N-acetyl-L-phenylalanyl 4-nitroanilide + H2O - Saccharolobus solfataricus P2 N-acetyl-L-phenylalanine + 4-nitroaniline - ? 421023 3.4.19.1 N-acetyl-Leu p-nitroanilide + H2O - Pyrococcus horikoshii N-acetyl-Leu + p-nitroaniline - ? 74046 3.4.19.1 N-acetyl-Leu-4-nitroanilide + H2O - Saccharolobus solfataricus N-acetyl-Leu + 4-nitroaniline - ? 426731 3.4.19.1 N-acetyl-Leu-4-nitroanilide + H2O switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase Aeropyrum pernix N-acetyl-L-Leu + 4-nitroaniline - ? 428801 3.4.19.1 N-acetyl-Leu-4-nitroanilide + H2O switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase Aeropyrum pernix DSM 11879 N-acetyl-L-Leu + 4-nitroaniline - ? 428801 3.4.19.1 N-acetyl-Leu-Ala + H2O - Rattus norvegicus N-acetyl-Leu + Ala - ? 74005 3.4.19.1 N-acetyl-Leu-p-nitroanilide + H2O esterase activity of wild-type enzyme with p-nitrophenyl caprylate as substrate is 7times higher than peptidase activity with N-acetyl-Leu-p-nitroanilide as substrate, 150fold higher for mutant enzyme R526V, peptidase activity for mutant R526E is abolished Aeropyrum pernix N-acetyl-Leu + p-nitroaniline - ? 385245 3.4.19.1 N-acetyl-Met-Ala + H2O - Rattus norvegicus N-acetyl-Met + Ala - ? 74003 3.4.19.1 N-acetyl-Met-Ala + H2O - Sus scrofa N-acetyl-Met + Ala - ? 74003 3.4.19.1 N-acetyl-Met-Ala + H2O - Pyrococcus horikoshii N-acetyl-Met + Ala - ? 74003 3.4.19.1 N-acetyl-Met-Ala-Ala-Ala-Ala-Ala + H2O - Pyrococcus horikoshii ? - ? 74028 3.4.19.1 N-acetyl-Met-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu + H2O - Oryctolagus cuniculus ? - ? 74043 3.4.19.1 N-acetyl-Met-Asp-Arg-Val-Leu-Ser-Arg-Tyr + H2O - Bos taurus ? - ? 74074 3.4.19.1 N-acetyl-Met-Asp-Glu-Thr-Gly-Asp-Thr-Ala-Leu-Val-Ala + H2O - Oryctolagus cuniculus ? - ? 74044 3.4.19.1 N-acetyl-Met-epsilon-Lys + H2O - Sus scrofa N-acetyl-Met + Lys - ? 74020 3.4.19.1 N-acetyl-Met-Leu + H2O - Rattus norvegicus ? - ? 74068 3.4.19.1 N-acetyl-Met-Leu-Gly + H2O - Oryctolagus cuniculus ? - ? 74077 3.4.19.1 N-acetyl-Met-Leu-Phe + H2O - Rattus norvegicus ? - ? 74067 3.4.19.1 N-acetyl-Met-Lys + H2O - Sus scrofa N-acetyl-Met + Lys - ? 74019 3.4.19.1 N-acetyl-Met-p-nitroanilide + H2O substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide Cucumis sativus N-acetyl-Met + p-nitroaniline - ? 365071 3.4.19.1 N-acetyl-Met-p-nitroanilide + H2O substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide Arabidopsis thaliana N-acetyl-Met + p-nitroaniline - ? 365071 3.4.19.1 N-acetyl-Phe-2-naphthylamide + H2O kinetic assay Aeropyrum pernix K1 N-acetyl-L-Phe + 2-naphthylamine - ? 405940 3.4.19.1 N-acetyl-Phe-2-naphthylamide + H2O - Aeropyrum pernix N-acetyl-Phe + 2-naphthylamine - ? 428802 3.4.19.1 N-acetyl-Phe-2-naphthylamide + H2O - Aeropyrum pernix DSM 11879 N-acetyl-Phe + 2-naphthylamine - ? 428802 3.4.19.1 N-acetyl-Phe-Ala + H2O weak activity Rattus norvegicus N-acetyl-Phe + Ala - ? 74006 3.4.19.1 N-acetyl-Ser-Ala + H2O - Rattus norvegicus N-acetyl-Ser + Ala - ? 74004 3.4.19.1 N-acetyl-Tyr p-nitroanilide + H2O - Pyrococcus horikoshii N-acetyl-Tyr + p-nitroaniline - ? 74047 3.4.19.1 N-acetyl-Tyr-Ala + H2O weak activity Rattus norvegicus N-acetyl-Tyr + Ala - ? 74008 3.4.19.1 N-acylpeptide + H2O acylpeptide hydrolase catalyzes the hydrolysis of short peptides of the type Nalpha-acyl to form an acyl amino acid and a peptide with a free N-terminus Sus scrofa ? - ? 397860 3.4.19.1 naphthyl butyrate + H2O - Homo sapiens naphthol + butyrate - ? 36060 3.4.19.1 p-nitrophenyl acetate + H2O - Homo sapiens 4-nitrophenol + acetate - ? 74069 3.4.19.1 p-nitrophenyl butyrate + H2O - Homo sapiens ? - ? 74070 3.4.19.1 p-nitrophenyl caprylate + H2O esterase activity of wild-type enzyme with p-nitrophenyl caprylate as substrate is 7times higher than peptidase activity with N-acetyl-Leu-p-nitroanilide as substrate, 150fold higher for mutant enzyme R526V, peptidase activity for mutant R526E is abolished Aeropyrum pernix nitrophenol + caprylate - ? 385494 3.4.19.1 p-nitrophenyl hexanoate + H2O - Homo sapiens p-nitrophenol + hexanoate - ? 74072 3.4.19.1 p-nitrophenyl propionate + H2O - Homo sapiens p-nitrophenol + propionate - ? 74050 3.4.19.1 p-nitrophenyl valerate + H2O - Homo sapiens p-nitrophenol + pentanoate - ? 74071 3.4.19.1 Phe-beta-naphthylamide + H2O - Streptomyces morookaense Phe + 2-naphthylamine - ? 398096 3.4.19.1 Phe-p-nitroanilide + H2O prefered substrate for PMH Streptomyces morookaense Phe + p-nitroaniline - ? 398097 3.4.19.1 Pro-beta-naphthylamide + H2O - Streptomyces morookaense Pro + 2-naphthylamine - ? 398149 3.4.19.1 puromycin + H2O - Streptomyces morookaense ? - ? 398215 3.4.19.1 succinyl-AAA-4-nitroanilide + H2O - Saccharolobus solfataricus succinyl-AAA + 4-nitroaniline - ? 432394 3.4.19.1 succinyl-AAPF-2-naphthylamide + H2O hydrolysed at a significantly slower rate than acetyl-Phe-2-naphthylamide Aeropyrum pernix K1 ? - ? 398355 3.4.19.1 succinyl-GGF-4-nitroanilide + H2O - Saccharolobus solfataricus succinyl-GGF + 4-nitroaniline - ? 432407 3.4.19.1 Tyr-beta-naphthylamide + H2O - Streptomyces morookaense Tyr + 2-naphthylamine - ? 398467 3.4.19.1 Tyr-Leu + H2O - Streptomyces morookaense Tyr + Leu - ? 358894 3.4.19.1 Tyr-Leu + H2O - Streptomyces morookaense JCM 4673 Tyr + Leu - ? 358894 3.4.19.1 Tyr-Phe + H2O - Streptomyces morookaense Tyr + Phe - ? 358889 3.4.19.1 Tyr-Phe + H2O - Streptomyces morookaense JCM 4673 Tyr + Phe - ? 358889 3.4.19.1 Z-GGL-4-nitroanilide + H2O - Saccharolobus solfataricus Z-GGL + 4-nitroaniline - ? 432496