3.4.23.1 ((7-methoxycoumarin-4-yl)acetyl)-Lys-Lys-Pro-Ala-Glu-Phe-Phe-Ala-Leu-Lys-(2,4-dinitrophenyl) + H2O - Shewanella denitrificans ((7-methoxycoumarin-4-yl)acetyl)-Lys-Lys-Pro-Ala-Glu-Phe + Phe-Ala-Leu-Lys-(2,4-dinitrophenyl) - ? 449064 3.4.23.1 (R)-(+)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde + 1,3-dihydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4R)-4-(2,2-dimethyl-1,3-dioxolan-4-yl)-1,3,4-trihydroxybutan-2-one - ? 449120 3.4.23.1 2 pQLSK-(7-methoxycoumarin-4-yl)-GYDEKSTGISK-[Nepsilon-(2,4-dinitrophenyl)]-P-NH2 + 2 H2O - Sus scrofa pQLSK-(7-methoxycoumarin-4-yl)-GYDEKSTG + ISK-[Nepsilon-(2,4-dinitrophenyl)]-P-NH2 + pQLSK-(7-methoxycoumarin-4-yl)-GY + DEKSTGISK-[Nepsilon-(2,4-dinitrophenyl)]-P-NH2 - ? 450487 3.4.23.1 2,6-dichlorobenzaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-4-(2,6-dichlorophenyl)-3,4-dihydroxybutan-2-one - ? 449195 3.4.23.1 2-chlorobenzaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-4-(2-chlorophenyl)-3,4-dihydroxybutan-2-one - ? 449258 3.4.23.1 2-nitrobenzaldehyde + 1,3-dihydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-1,3,4-trihydroxy-4-(2-nitrophenyl)butan-2-one - ? 449264 3.4.23.1 2-nitrobenzaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-3,4-dihydroxy-4-(2-nitrophenyl)butan-2-one - ? 449265 3.4.23.1 2-nitrobenzaldehyde + 1-methoxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-4-hydroxy-3-methoxy-4-(2-nitrophenyl)butan-2-one - ? 449266 3.4.23.1 2-nitrobenzaldehyde + cyclohexanone in MeCN buffer, at 30°C Sus scrofa (2S)-2-[(R)-hydroxy(2-nitrophenyl)methyl]cyclohexan-1-one - ? 449267 3.4.23.1 2-nitrobenzaldehyde + cyclopentanone in MeCN buffer, at 30°C Sus scrofa (2S)-2-[(R)-hydroxy(2-nitrophenyl)methyl]cyclopentan-1-one - ? 449268 3.4.23.1 3-bromobenzaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-4-(3-bromophenyl)-3,4-dihydroxybutan-2-one - ? 449278 3.4.23.1 3-methylbutanal + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-3,4-dihydroxy-6-methylheptan-2-one - ? 449286 3.4.23.1 3-nitrobenzaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-3,4-dihydroxy-4-(3-nitrophenyl)butan-2-one - ? 449288 3.4.23.1 3-nitrobenzaldehyde + cyclohexanone in MeCN buffer, at 30°C Sus scrofa (2S)-2-[(R)-hydroxy(3-nitrophenyl)methyl]cyclohexan-1-one - ? 449289 3.4.23.1 4-(trifluoromethyl)benzaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-3,4-dihydroxy-4-[4-(trifluoromethyl)phenyl]butan-2-one - ? 449308 3.4.23.1 4-bromobenzaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-4-(4-bromophenyl)-3,4-dihydroxybutan-2-one - ? 449310 3.4.23.1 4-bromobenzaldehyde + propan-2-one in MeCN buffer, at 30°C Sus scrofa (4R)-4-(4-bromophenyl)-4-hydroxybutan-2-one - ? 449311 3.4.23.1 4-chlorobenzaldehyde + 1-(benzyloxy)propan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-3-(benzyloxy)-4-(4-chlorophenyl)-4-hydroxybutan-2-one - ? 449312 3.4.23.1 4-chlorobenzaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-4-(4-chlorophenyl)-3,4-dihydroxybutan-2-one - ? 449313 3.4.23.1 4-chlorobenzaldehyde + cyclohexanone in MeCN buffer, at 30°C Sus scrofa (2S)-2-[(R)-(4-chlorophenyl)(hydroxy)methyl]cyclohexan-1-one - ? 449314 3.4.23.1 4-chlorobenzaldehyde + cyclopentanone in MeCN buffer, at 30°C Sus scrofa (2S)-2-[(R)-(4-chlorophenyl)(hydroxy)methyl]cyclopentan-1-one - ? 449315 3.4.23.1 4-fluorobenzaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-4-(4-fluorophenyl)-3,4-dihydroxybutan-2-one - ? 449317 3.4.23.1 4-formylbenzonitrile + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa 4-[(1S,2R)-1,2-dihydroxy-3-oxobutyl]benzonitrile - ? 449318 3.4.23.1 4-methylbenzaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-3,4-dihydroxy-4-(4-methylphenyl)butan-2-one - ? 449321 3.4.23.1 4-nitrobenzaldehyde + 1,3-dihydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-1,3,4-trihydroxy-4-(4-nitrophenyl)butan-2-one - ? 449327 3.4.23.1 4-nitrobenzaldehyde + 1-(benzyloxy)propan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-3-(benzyloxy)-4-hydroxy-4-(4-nitrophenyl)butan-2-one - ? 449328 3.4.23.1 4-nitrobenzaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-3,4-dihydroxy-4-(4-nitrophenyl)butan-2-one - ? 449329 3.4.23.1 4-nitrobenzaldehyde + 1-methoxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-4-hydroxy-3-methoxy-4-(4-nitrophenyl)butan-2-one - ? 449330 3.4.23.1 4-nitrobenzaldehyde + cyclohexanone in MeCN buffer, at 30°C Sus scrofa (2S)-2-[(R)-hydroxy(4-nitrophenyl)methyl]cyclohexan-1-one - ? 449331 3.4.23.1 4-nitrobenzaldehyde + cyclopentanone in MeCN buffer, at 30°C Sus scrofa (2S)-2-[(R)-hydroxy(4-nitrophenyl)methyl]cyclopentan-1-one - ? 449332 3.4.23.1 4-nitrobenzaldehyde + oxan-4-one in MeCN buffer, at 30°C Sus scrofa (3S)-3-[(R)-hydroxy(4-nitrophenyl)methyl]oxan-4-one - ? 449333 3.4.23.1 4-nitrobenzaldehyde + propan-2-one in MeCN buffer, at 30°C Sus scrofa (4R)-4-hydroxy-4-(4-nitrophenyl)butan-2-one - ? 449334 3.4.23.1 4-nitrobenzaldehyde + tert-butyl 4-oxopiperidine-1-carboxylate in MeCN buffer, at 30°C Sus scrofa tert-butyl (3S)-3-[(R)-hydroxy(4-nitrophenyl)methyl]-4-oxopiperidine-1-carboxylate - ? 449335 3.4.23.1 4-nitrobenzaldehyde + thian-4-one in MeCN buffer, at 30°C Sus scrofa (3S)-3-[(R)-hydroxy(4-nitrophenyl)methyl]thian-4-one - ? 449336 3.4.23.1 acetyl-Ala-Ala-Lys-Phe(4-NO2)-Ala-Ala-NH2 + H2O - Sus scrofa ? - ? 37070 3.4.23.1 acetyl-L-phenylalanyl-L-diiodotyrosine + H2O - Sus scrofa acetyl-L-phenylalanine + L-diiodotyrosine - ? 37066 3.4.23.1 acetyl-L-phenylalanyl-L-diiodotyrosine + H2O - Macaca fuscata fuscata acetyl-L-phenylalanine + L-diiodotyrosine - ? 37066 3.4.23.1 acetyl-L-phenylalanyl-L-diiodotyrosine + H2O - Scombridae gen. sp. acetyl-L-phenylalanine + L-diiodotyrosine - ? 37066 3.4.23.1 acetyl-L-phenylalanyl-L-diiodotyrosine + H2O - Pelodiscus sinensis acetyl-L-phenylalanine + L-diiodotyrosine - ? 37066 3.4.23.1 acetyl-L-phenylalanyl-L-diiodotyrosine + H2O - Ursus thibetanus acetyl-L-phenylalanine + L-diiodotyrosine - ? 37066 3.4.23.1 acetyl-L-phenylalanyl-L-diiodotyrosine + H2O low activity Gallus gallus acetyl-L-phenylalanine + L-diiodotyrosine - ? 37066 3.4.23.1 acetyl-L-phenylalanyl-L-diiodotyrosine + H2O low activity Rattus norvegicus acetyl-L-phenylalanine + L-diiodotyrosine - ? 37066 3.4.23.1 Acid-denatured hemoglobin + H2O - Oncorhynchus mykiss ? - ? 15914 3.4.23.1 AFPLEFEREL + H2O - Homo sapiens AFPLEF + EREL - ? 411579 3.4.23.1 AFPLEFEREL + H2O - Sus scrofa AFPLEF + EREL - ? 411579 3.4.23.1 AFPLEFFREL + H2O - Homo sapiens AFPLEF + FREL - ? 411580 3.4.23.1 AFPLEFFREL + H2O - Sus scrofa AFPLEF + FREL - ? 411580 3.4.23.1 AFPLEFIREL + H2O - Homo sapiens AFPLEF + IREL - ? 411581 3.4.23.1 AFPLEFIREL + H2O - Sus scrofa AFPLEF + IREL - ? 411581 3.4.23.1 benzaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-3,4-dihydroxy-4-phenylbutan-2-one - ? 449632 3.4.23.1 benzyloxycarbonyl-Gly-Ala-(4-nitro)Phe-Trp-NHCH2CH2OH + H2O - Sus scrofa ? - ? 37058 3.4.23.1 benzyloxycarbonyl-Gly-Gly-Phe-Phe 3-(4-pyridyl)propyl ester + H2O - Sus scrofa benzyloxycarbonyl-Gly-Gly-Phe + Phe 3-(4-pyridyl)propyl ester - ? 449652 3.4.23.1 benzyloxycarbonyl-Gly-Phe-Phe 3-(4-pyridyl)propyl ester + H2O - Sus scrofa benzyloxycarbonyl-Gly-Phe + Phe 3-(4-pyridyl)propyl ester - ? 449653 3.4.23.1 benzyloxycarbonyl-His-(4-nitro)Phe-Phe-OMet + H2O - Sus scrofa ? - ? 37055 3.4.23.1 benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O - Gallus gallus benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester - ? 37067 3.4.23.1 benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O - Sus scrofa benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester - ? 37067 3.4.23.1 benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O - salmon benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester - ? 37067 3.4.23.1 benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O - shark benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester - ? 37067 3.4.23.1 benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O - Scombridae gen. sp. benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester - ? 37067 3.4.23.1 benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O - dogfish benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester - ? 37067 3.4.23.1 benzyloxycarbonyl-His-Phe-Phe-NH2 + H2O - Sus scrofa ? - ? 37051 3.4.23.1 benzyloxycarbonyl-His-Phe-Phe-O-ethyl ester + H2O - Sus scrofa ? - ? 453122 3.4.23.1 benzyloxycarbonyl-His-Phe-Phe-O-methyl ester + H2O - Sus scrofa ? - ? 37050 3.4.23.1 benzyloxycarbonyl-His-Phe-Trp-OEt + H2O - Sus scrofa ? - ? 37054 3.4.23.1 benzyloxycarbonyl-His-Trp-Phe-O-methyl ester + H2O - Sus scrofa ? - ? 453123 3.4.23.1 benzyloxycarbonyl-His-Tyr-Phe-O-methyl ester + H2O - Sus scrofa ? - ? 37049 3.4.23.1 benzyloxycarbonyl-Phe-Phe 3-(4-pyridyl)propyl ester + H2O - Sus scrofa benzyloxycarbonyl-Phe + Phe 3-(4-pyridyl)propyl ester - ? 449663 3.4.23.1 benzyloxycarbonyl-Phe-Phe-OEt + H2O - Sus scrofa benzyloxycarbonyl-Phe + Phe-OEt - ? 449664 3.4.23.1 bis-phenyl sulfite + H2O - Gallus gallus ? - ? 37048 3.4.23.1 Bovine hemoglobin + H2O - Sus scrofa ? - ? 16882 3.4.23.1 Bovine serum albumin + H2O - Sus scrofa ? - ? 16295 3.4.23.1 bovine type I collagen + H2O pepsin cleaves type I collagen at various sites in the N-terminal and in the C-terminal telopeptides Sus scrofa ? - ? 449713 3.4.23.1 bovine type I collagen alpha1 chain + H2O the enzyme preferentially cleaves Tyr6-Asp7 and less preferentially Gly12-Ile13 Sus scrofa pQLSYGY + pQLSYGYDEKSTG - ? 449714 3.4.23.1 casein + H2O - Gallus gallus ? - ? 15445 3.4.23.1 casein + H2O - Capra hircus ? - ? 15445 3.4.23.1 casein + H2O - Sus scrofa L-tyrosine + ? - ? 391589 3.4.23.1 cinnamaldehyde + 1,4-dithiane-2,5-diol asymmetric domino thia-Michael/aldol condensation in MeCN buffer, at 30°C Sus scrofa (2R)-2-phenyl-2,5-dihydrothiophene-3-carbaldehyde - ? 449764 3.4.23.1 cowpea protein + H2O - Sus scrofa cowpea protein hydrolysate - ? 449779 3.4.23.1 crude cheese whey + H2O the porcine pepsin digests of crude cheese whey lead the production of the three peptides with antibacterial activity against Bacillus subtilis (lactoferrin f(20-30) and beta-lactoglobulin f(14-22)) and Escherichia coli (beta-lactoglobulin f(82-103)) Sus scrofa lactoferrin f(20-30) + beta-lactoglobulin f(14-22) + beta-lactoglobulin f(92-103) + ? - ? 449781 3.4.23.1 Cry1A(b) protein + H2O from transgenic maize or from Bacillus thuringiensis Sus scrofa ? - ? 414461 3.4.23.1 curcumin + H2O i.e. diferuloylmethane Sus scrofa ? - ? 448529 3.4.23.1 dynorphin A (1-7) + H2O - Homo sapiens ? - ? 116059 3.4.23.1 dynorphin A (1-7) + H2O - Sus scrofa ? - ? 116059 3.4.23.1 Hemoglobin + H2O - Gallus gallus ? - ? 15450 3.4.23.1 Hemoglobin + H2O - Homo sapiens ? - ? 15450 3.4.23.1 Hemoglobin + H2O - Sus scrofa ? - ? 15450 3.4.23.1 Hemoglobin + H2O - Anas platyrhynchos ? - ? 15450 3.4.23.1 Hemoglobin + H2O - Scombridae gen. sp. ? - ? 15450 3.4.23.1 Hemoglobin + H2O - dogfish ? - ? 15450 3.4.23.1 Hemoglobin + H2O - Pelodiscus sinensis ? - ? 15450 3.4.23.1 Hemoglobin + H2O - Parona signata ? - ? 15450 3.4.23.1 Hemoglobin + H2O - Micropterus salmoides ? - ? 15450 3.4.23.1 Hemoglobin + H2O - Albatrossia pectoralis ? - ? 15450 3.4.23.1 Hemoglobin + H2O - Monopterus albus ? - ? 15450 3.4.23.1 Hemoglobin + H2O - Lateolabrax japonicus ? - ? 15450 3.4.23.1 Hemoglobin + H2O - Homo sapiens ? TCA-soluble peptides ? 15450 3.4.23.1 Hemoglobin + H2O - Sus scrofa ? TCA-soluble peptides ? 15450 3.4.23.1 Hemoglobin + H2O bovine Homo sapiens ? - ? 15450 3.4.23.1 HPHLSFMAI + H2O best substrate Homo sapiens HPHLSF + Met-Ala-Ile + ? - ? 418537 3.4.23.1 HPHLSFMAI + H2O best substrate Sus scrofa HPHLSF + Met-Ala-Ile + ? - ? 418537 3.4.23.1 insulin + H2O B-chain of oxidized insulin Sus scrofa ? - ? 36836 3.4.23.1 insulin + H2O B-chain of oxidized insulin Pelodiscus sinensis ? - ? 36836 3.4.23.1 KPAEFF(NO2)-AL + H2O - Sus scrofa ? - ? 392319 3.4.23.1 KPAEFF(NO2)AL + H2O - Sus scrofa ? - ? 366917 3.4.23.1 KPAEFFRL + H2O - Homo sapiens KPAEF + FRL - ? 418729 3.4.23.1 KPAEFFRL + H2O - Sus scrofa KPAEF + FRL - ? 418729 3.4.23.1 KPAEFFRL + H2O - Micropterus salmoides KPAEF + FRL - ? 418729 3.4.23.1 KPAEFIRL + H2O - Micropterus salmoides KPAEF + IRL - ? 450111 3.4.23.1 KPAEFIRL + H2O best substrate for pepsin A1 Micropterus salmoides KPAEF + IRL - ? 450111 3.4.23.1 KPAEFRRL + H2O - Sus scrofa KPAEF + RRL - ? 450112 3.4.23.1 KPAEFRRL + H2O - Micropterus salmoides KPAEF + RRL - ? 450112 3.4.23.1 KPAEFWRL + H2O - Micropterus salmoides KPAEF + WRL - ? 450113 3.4.23.1 KPAEFWRL + H2O best substrate for pepsin A2 Micropterus salmoides KPAEF + WRL - ? 450113 3.4.23.1 KPAQFFRL + H2O best substrate Sus scrofa KPAQF + FRL - ? 450114 3.4.23.1 KPIEF(NO2)RL + H2O - Sus scrofa ? - ? 366912 3.4.23.1 KPIKF(NO2)RL + H2O - Sus scrofa ? - ? 366914 3.4.23.1 KPILF(NO2)RL + H2O - Sus scrofa ? - ? 366911 3.4.23.1 KPIQF(NO2)RL + H2O - Sus scrofa ? - ? 366913 3.4.23.1 KPPEF(NO2)RL + H2O - Sus scrofa ? - ? 366915 3.4.23.1 KYSSWYVAL + H2O - Homo sapiens KYSSW + YVAL - ? 418733 3.4.23.1 KYSSWYVAL + H2O - Sus scrofa KYSSW + YVAL - ? 418733 3.4.23.1 L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu + H2O - Sus scrofa ? - ? 384999 3.4.23.1 lactoferrin + H2O - Bos taurus ? - ? 361048 3.4.23.1 Leu-Ser-Phe(NO2)-Nle-Ala-Leu + H2O - Sus scrofa ? - ? 37071 3.4.23.1 Leu-Ser-Phe(p-NO2)-Nle-Ala-Leu + H2O - Sus scrofa ? - ? 366909 3.4.23.1 LSF(NO2)-Nle-AL + H2O - Sus scrofa ? - ? 366918 3.4.23.1 Lys-Pro-Ala-Glu-Phe-Phe(4NO2)-Ala-Leu + H2O - Sus scrofa ? - ? 37061 3.4.23.1 Lys-Pro-Ala-Glu-Phe-Phe(4NO2)-Ala-Leu + H2O - Anas platyrhynchos ? - ? 37061 3.4.23.1 Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu + H2O - Sus scrofa ? - ? 414814 3.4.23.1 Lys-Pro-Ala-Glu-Phe-Phe(p-NO2)-Ala-Leu + H2O - Sus scrofa ? - ? 366908 3.4.23.1 Mca-KKPAEFFALK-Dnp + H2O this peptide is preferentially cleaved at Phe-Phe, with a second minor cleavage occurring at Phe-Ala Shewanella amazonensis Mca-KKPAEF + FFALK-Dnp - ? 418825 3.4.23.1 Mca-KLHPEVLFVLEK-Dnp + H2O the preferred cleavage site is between Leu-Phe, a minor cleavage site is between Phe-Ala Shewanella amazonensis Mca-KLHPEVL + FVLEK-Dnp - ? 418826 3.4.23.1 metmyoglobin + H2O - Sus scrofa ? treatment with pepsin at pH 4.0 results in lowering the (pseudo)peroxidase activity of metmyoglobin both at physiological pH and at meat pH, leading to strongly enhanced prooxidative effect of mildly proteolyzed metmyoglobin on lipid oxidation ? 385185 3.4.23.1 MOCAc-Ala-Pro-Ala-Lys-Phe-Phe-Arg-Leu-Lys(Dnp)-NH2 + H2O - Sus scrofa ? - ? 414878 3.4.23.1 additional information milk clotting activity Sus scrofa ? - ? 89 3.4.23.1 additional information milk clotting activity Coturnix japonica ? - ? 89 3.4.23.1 additional information preference for hydrophobic L-amino acid residues on both sides of X-Y bond in benzyloxycarbonyl-L-histidyl-X-Y-OR Sus scrofa ? - ? 89 3.4.23.1 additional information transpeptidation reactions Gallus gallus ? - ? 89 3.4.23.1 additional information transpeptidation reactions Sus scrofa ? - ? 89 3.4.23.1 additional information transpeptidation reactions salmon ? - ? 89 3.4.23.1 additional information transpeptidation reactions shark ? - ? 89 3.4.23.1 additional information transpeptidation reactions Scombridae gen. sp. ? - ? 89 3.4.23.1 additional information transpeptidation reactions dogfish ? - ? 89 3.4.23.1 additional information absolute requirement for L-enantiomer in both the X and Y position of substrate Gallus gallus ? - ? 89 3.4.23.1 additional information absolute requirement for L-enantiomer in both the X and Y position of substrate Sus scrofa ? - ? 89 3.4.23.1 additional information absolute requirement for L-enantiomer in both the X and Y position of substrate salmon ? - ? 89 3.4.23.1 additional information absolute requirement for L-enantiomer in both the X and Y position of substrate shark ? - ? 89 3.4.23.1 additional information absolute requirement for L-enantiomer in both the X and Y position of substrate Scombridae gen. sp. ? - ? 89 3.4.23.1 additional information absolute requirement for L-enantiomer in both the X and Y position of substrate dogfish ? - ? 89 3.4.23.1 additional information condensation reaction: pH 4, high substrate concentrations, oligopeptides converted to polymeric products Gallus gallus ? - ? 89 3.4.23.1 additional information condensation reaction: pH 4, high substrate concentrations, oligopeptides converted to polymeric products Sus scrofa ? - ? 89 3.4.23.1 additional information condensation reaction: pH 4, high substrate concentrations, oligopeptides converted to polymeric products salmon ? - ? 89 3.4.23.1 additional information condensation reaction: pH 4, high substrate concentrations, oligopeptides converted to polymeric products shark ? - ? 89 3.4.23.1 additional information condensation reaction: pH 4, high substrate concentrations, oligopeptides converted to polymeric products Scombridae gen. sp. ? - ? 89 3.4.23.1 additional information condensation reaction: pH 4, high substrate concentrations, oligopeptides converted to polymeric products dogfish ? - ? 89 3.4.23.1 additional information side chain specificity Gallus gallus ? - ? 89 3.4.23.1 additional information side chain specificity Sus scrofa ? - ? 89 3.4.23.1 additional information side chain specificity salmon ? - ? 89 3.4.23.1 additional information side chain specificity shark ? - ? 89 3.4.23.1 additional information side chain specificity Scombridae gen. sp. ? - ? 89 3.4.23.1 additional information side chain specificity dogfish ? - ? 89 3.4.23.1 additional information organic sulfites Gallus gallus ? - ? 89 3.4.23.1 additional information organic sulfites Sus scrofa ? - ? 89 3.4.23.1 additional information organic sulfites salmon ? - ? 89 3.4.23.1 additional information organic sulfites shark ? - ? 89 3.4.23.1 additional information organic sulfites Scombridae gen. sp. ? - ? 89 3.4.23.1 additional information organic sulfites dogfish ? - ? 89 3.4.23.1 additional information the active site of pepsin is formed in the intermediate conformation dominant at mildly acidic pH Sus scrofa ? - ? 89 3.4.23.1 additional information preference for hydrophobic and aromatic residues at P’1 site of substrate Homo sapiens ? - ? 89 3.4.23.1 additional information detailed study on the interaction of porcine pepsin A with derivatives of aromatic amino acids immobilized via a carboxyl or amino group to Sepharose activated with divinyl sulfone Sus scrofa ? - ? 89 3.4.23.1 additional information no digestion of Phe-Gly-His-Phe-(p-nitro-Phe)-Ala-Phe-OMe Trematomus bernacchii ? - ? 89 3.4.23.1 additional information digestibility of maize and sorghum proteins without and after heat-treatment Sus scrofa ? - ? 89 3.4.23.1 additional information solubilization of collagens from the skin of Priacanthus tayenus and Priacanthus macracanthus Sus scrofa ? - ? 89 3.4.23.1 additional information solubilization of collagens from the skin of Priacanthus tayenus and Priacanthus macracanthus Thunnus tonggol ? - ? 89 3.4.23.1 additional information the cleavage site of isoform PG1 to produce pepsin is clearly at the 41-42 bond of Phe-Ala Lateolabrax japonicus ? - ? 89 3.4.23.1 additional information Edans-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys-Dabcyl-Arg, Arg-Glu-Edans-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-Lys-Dabcyl-Arg, and Mca-Lys-Ser-Glu-Val-Asn-Leu-Asp-Ala-Glu-Phe-Lys-Dnp are not significantly processed by shewasin A Shewanella amazonensis ? - ? 89 3.4.23.1 additional information pepsin A strongly prefers a hydrophobic/aromatic residue at P1’ in any type of peptide Homo sapiens ? - ? 89 3.4.23.1 additional information pepsin A strongly prefers a hydrophobic/aromatic residue at P1’ in any type of peptide Sus scrofa ? - ? 89 3.4.23.1 additional information the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A1 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met Micropterus salmoides ? - ? 89 3.4.23.1 additional information the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A2 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met Micropterus salmoides ? - ? 89 3.4.23.1 additional information the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. The enzyme prefers some hydrophobic residues such as Leu, Val, Ala and Met Sus scrofa ? - ? 89 3.4.23.1 additional information amino acids set free by pepsin include tryptophan and phenylalanine. Aromatic amino acids are preferentially exposed and released by the enzyme Homo sapiens ? - ? 89 3.4.23.1 additional information binding study with procyanidin B3 Sus scrofa ? - ? 89 3.4.23.1 additional information no activity with ((7-methoxycoumarin-4-yl)acetyl)-Lys-Leu-His-Pro-Glu-Val-Leu-Phe-Val-Leu-Glu-Lys-(2,4-dinitrophenyl), Arg-Glu-(EDANS)-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys-(DABCYL)-Arg, ((7-methoxycoumarin-4-yl)acetyl)-Lys-Ser-Glu-Val-Asn-Leu-Asp-Ala-Glu-Phe-Lys-(2,4-dinitrophenyl), or ((7-methoxycoumarin-4-yl)acetyl)-Lys-Ala-Leu-Ile-Pro-Ser-Tyr-Lys-Trp-Ser-Lys-(2,4-dinitrophenyl) Shewanella denitrificans ? - ? 89 3.4.23.1 N,N-dimethyl-casein + H2O - Homo sapiens ? - ? 37052 3.4.23.1 N,N-dimethyl-casein + H2O - Ovis aries ? - ? 37052 3.4.23.1 N,N-dimethylcasein + H2O - Ovis aries ? - ? 453121 3.4.23.1 N,N-dimethylhemoglobin + H2O - Ovis aries ? - ? 37053 3.4.23.1 N-trifluoroacetyl aromatic L-amino acids + H2O - Sus scrofa ? - ? 37047 3.4.23.1 naphthalene-1-carbaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4S)-3,4-dihydroxy-4-(naphthalen-1-yl)butan-2-one - ? 450403 3.4.23.1 NT/NMN (142-151) + H2O - Homo sapiens KIPYIL + KRQL - ? 418974 3.4.23.1 NT/NMN (142-151) + H2O - Sus scrofa KIPYIL + KRQL - ? 418974 3.4.23.1 ovalbumin + H2O - Homo sapiens ? - ? 37064 3.4.23.1 ovine immunoglobulin G1 + H2O - Sus scrofa ? - ? 450425 3.4.23.1 ovine immunoglobulin G2 + H2O - Sus scrofa ? - ? 450426 3.4.23.1 oxidized insulin B chain + H2O two major cleavage sites are at Leu15-Tyr16 and Tyr16-Leu17 Shewanella amazonensis FVNQHLCGSHLVEAL + L-Tyr + LVCGERGFFYTPKA - ? 418985 3.4.23.1 oxidized insulin B chain + H2O the cleavage specificities clarified with oxidized insulin B chain are restricted to a few bonds consisting of hydrophobic/aromatic residues, such as the Leu15-Tyr16, Phe24-Phe25 and Phe25-Tyr26 bonds Micropterus salmoides FVNQHLCGSHLVEAL + YLVCGERGFFYTPKA - ? 450428 3.4.23.1 Oxidized insulin B-chain + H2O - Homo sapiens ? - ? 15443 3.4.23.1 Phe-Gly-His-(4-nitro)Phe-Phe-Ala-Phe-OMe + H2O - Sus scrofa ? - ? 37057 3.4.23.1 POMC (165-174) + H2O - Homo sapiens AFPLE + FKREL - ? 419000 3.4.23.1 POMC (165-174) + H2O - Sus scrofa AFPLE + FKREL - ? 419000 3.4.23.1 Pro-Thr-Glu-Lys-Phe(4-NO2)-Arg-Leu-NH2 + H2O - Sus scrofa ? - ? 37069 3.4.23.1 Pro-Thr-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O - Sus scrofa ? - ? 16335 3.4.23.1 Pro-Thr-Glu-Phe-(p-nitro-Phe)-Arg-Leu-OH + H2O - Trematomus bernacchii Pro-Thr-Glu-Phe + (p-nitro-Phe)-Arg-Leu-OH - ? 393334 3.4.23.1 Pro-Thr-Glu-Phe-Phe(4-NO2)-Arg-Leu + H2O - Sus scrofa ? - ? 37068 3.4.23.1 Proteins + H2O low specificity Sus scrofa ? - ? 369561 3.4.23.1 Proteins + H2O enzyme formed from pepsinogen A, agent of gastric digestion in mammals and birds Gallus gallus ? - ? 369561 3.4.23.1 Proteins + H2O preferential cleavage: Phe-, Leu- Gallus gallus ? - ? 369561 3.4.23.1 Proteins + H2O preferential cleavage: Phe-, Leu- Sus scrofa ? - ? 369561 3.4.23.1 Ribonuclease + H2O reduced and carboxymethylated ribonuclease A Homo sapiens ? - ? 16994 3.4.23.1 serum albumin + H2O - Homo sapiens ? - ? 37063 3.4.23.1 serum albumin + H2O - dogfish ? - ? 37063 3.4.23.1 SGGYDLSFLPQPPQE + H2O predominant cleavage of the peptide corresponding to the carboxy-terminal telopeptide region of bovine type I collagen alpha1 chain at Asp-Leu, Leu-Ser and Phe-Leu and at a significant lower rate at Ser-Phe Sus scrofa ? - ? 366910 3.4.23.1 Substance P + H2O RPKPQQFFGLM Micropterus salmoides ? - ? 17205 3.4.23.1 substance P + H2O - Homo sapiens RPKPQQF + FGLM - ? 419085 3.4.23.1 substance P + H2O - Sus scrofa RPKPQQF + FGLM - ? 419085 3.4.23.1 thiophene-2-carbaldehyde + 1-hydroxypropan-2-one in MeCN buffer, at 30°C Sus scrofa (3R,4R)-3,4-dihydroxy-4-(thiophen-2-yl)butan-2-one - ? 450753 3.4.23.1 trypsinogen + H2O - Castor fiber trypsin + peptide fragment - ? 383394 3.4.23.1 Z-GGFF-OP4P + H2O - Sus scrofa benzyloxycarbonyl-GGF + Phe 3-(4-pyridyl)propyl ester - ? 450838