PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 3574596-2 1987 Cathepsin L and cathepsin H were assayed in the presence of dithiothreitol and Na2EDTA (2 mM each) with Z-Phe-Arg-NHMec (pH 5.5) and Lys-NNa (pH 6.5) respectively. Z-Phe-Arg 104-113 cathepsin L Homo sapiens 0-11 2751313-12 1989 The enzymatic activity toward Z-Phe-Arg-NHMec at pH 5.5 increased during the conversion, indicating that active cathepsin L was formed from an inactive precursor molecule. Z-Phe-Arg 30-39 cathepsin L Rattus norvegicus 112-123 3574596-2 1987 Cathepsin L and cathepsin H were assayed in the presence of dithiothreitol and Na2EDTA (2 mM each) with Z-Phe-Arg-NHMec (pH 5.5) and Lys-NNa (pH 6.5) respectively. Z-Phe-Arg 104-113 cathepsin H Homo sapiens 16-27 3574596-6 1987 Z-Phe-Arg-NHMec is the best substrate for cathepsin L (KM = 5 microM, Kcat = 21 s-1), Arg-NNa--for cathepsin H (KM = 0.1 mM, Kcat = 1.93 s-1), being endoaminopeptidase cathepsin H also hydrolyses Bz-Arg-NNa (KM = 0.7 mM, Kcat = 1.3 s-1). Z-Phe-Arg 0-9 cathepsin L Homo sapiens 42-53 3574596-6 1987 Z-Phe-Arg-NHMec is the best substrate for cathepsin L (KM = 5 microM, Kcat = 21 s-1), Arg-NNa--for cathepsin H (KM = 0.1 mM, Kcat = 1.93 s-1), being endoaminopeptidase cathepsin H also hydrolyses Bz-Arg-NNa (KM = 0.7 mM, Kcat = 1.3 s-1). Z-Phe-Arg 0-9 cathepsin H Homo sapiens 99-110 3574596-6 1987 Z-Phe-Arg-NHMec is the best substrate for cathepsin L (KM = 5 microM, Kcat = 21 s-1), Arg-NNa--for cathepsin H (KM = 0.1 mM, Kcat = 1.93 s-1), being endoaminopeptidase cathepsin H also hydrolyses Bz-Arg-NNa (KM = 0.7 mM, Kcat = 1.3 s-1). Z-Phe-Arg 0-9 cathepsin H Homo sapiens 168-179 6421281-8 1984 One major difference between these two enzymes was in their Michaelis constants for Z-Phe-Arg-NMec; cathepsin B had Km 75 microM whereas that of cathepsin L was 0.7 microM. Z-Phe-Arg 84-93 cathepsin B Oryctolagus cuniculus 100-111 6421281-8 1984 One major difference between these two enzymes was in their Michaelis constants for Z-Phe-Arg-NMec; cathepsin B had Km 75 microM whereas that of cathepsin L was 0.7 microM. Z-Phe-Arg 84-93 cathepsin L1 Oryctolagus cuniculus 145-156 22210546-11 2012 Active CTSS had the ability to catalyze Z-Phe-Arg-AMC substrates in acidic conditions (pH 5.0) and weak alkaline environments (pH 7.5); this activity could be blocked by the cysteine protease inhibitor E-64. Z-Phe-Arg 40-49 cathepsin S Homo sapiens 7-11 6282022-3 1981 Some kinetic constants are given for the three synthetic substrates of cathepsin L which are known so far: Bz-Arg-NH2, Z-Lys-OPhNO2 and Z-Phe-Arg-NMec. Z-Phe-Arg 136-145 cathepsin L Homo sapiens 71-82 1540624-8 1992 The kinetics of hydrolysis using Z-Phe-Arg-NHMec and Bz-Phe-Val-Arg-NHMec as substrates resulted in values within the range expected for cathepsin B. Z-Phe-Arg 33-42 cathepsin B Homo sapiens 137-148 19910310-2 2010 The coefficient of inhibition (K(i)) was determined towards rabbit cathepsin L using Z-Phe-Arg-MCA as the substrate. Z-Phe-Arg 85-94 cathepsin L1 Oryctolagus cuniculus 67-78 12072215-4 2002 At the optimum pH of 5.5, hydrolysis of Z-Phe-Arg-NHMec was three-fold greater than that of Z-Arg-Arg-NHMec suggesting that the proteolytic specificities of the ESP are more like those of papain or cathepsin L, rather than cathepsin B. Z-Phe-Arg 40-49 cathepsin L Homo sapiens 198-209 12072215-4 2002 At the optimum pH of 5.5, hydrolysis of Z-Phe-Arg-NHMec was three-fold greater than that of Z-Arg-Arg-NHMec suggesting that the proteolytic specificities of the ESP are more like those of papain or cathepsin L, rather than cathepsin B. Z-Phe-Arg 40-49 cathepsin B Homo sapiens 223-234 8282126-5 1993 The complex has significantly enhanced stability at neutral and slightly alkaline pH, and reduced proteolytic activity against the synthetic substrate Z-Phe-Arg-MCA compared to free cathepsin L. Z-Phe-Arg 151-160 cathepsin L Homo sapiens 182-193 8922036-3 1996 Cathepsin B activity was estimated in serum using Z-Phe-Arg-NMec, and in tumor tissue using Z-Arg-Arg-pNA . Z-Phe-Arg 50-59 cathepsin B Homo sapiens 0-11 7487106-11 1995 Additionally, the mature (single-chain) form of cathepsin L displayed Km and kcat values on Z-Phe-Arg-NMec that yielded an exceptionally high catalytic coefficient (11,600 s-1 mM-1) compared to values reported for two-chain forms of cathepsin L. Z-Phe-Arg 92-101 cathepsin L Homo sapiens 48-59 1894742-2 1991 The activities of cathepsin B- and L-like proteinases in homogenised gingival tissue from control and periodontitis patients were measured biochemically using the selective peptide substrate Z-Phe-Arg-AFC and the selective cathepsin L inhibitor Z-Phe-Phe-CHN2. Z-Phe-Arg 191-200 cathepsin B Homo sapiens 18-29 2232482-6 1990 The pH optimum for cathepsin B (substrate: Z-Arg-Arg-HNMec) and L (substrate: Z-Phe-Arg-HNMec in the presence of Z-Phe-Phe-CHN2) was approximately pH 6.0 for both glomeruli and renal cortex; while that for cathepsin H (substrate: Arg-HNMec) was approximately 6.5. Z-Phe-Arg 78-87 cathepsin B Rattus norvegicus 19-30 2232482-6 1990 The pH optimum for cathepsin B (substrate: Z-Arg-Arg-HNMec) and L (substrate: Z-Phe-Arg-HNMec in the presence of Z-Phe-Phe-CHN2) was approximately pH 6.0 for both glomeruli and renal cortex; while that for cathepsin H (substrate: Arg-HNMec) was approximately 6.5. Z-Phe-Arg 78-87 chimerin 2 Rattus norvegicus 123-127 2232482-6 1990 The pH optimum for cathepsin B (substrate: Z-Arg-Arg-HNMec) and L (substrate: Z-Phe-Arg-HNMec in the presence of Z-Phe-Phe-CHN2) was approximately pH 6.0 for both glomeruli and renal cortex; while that for cathepsin H (substrate: Arg-HNMec) was approximately 6.5. Z-Phe-Arg 78-87 cathepsin H Rattus norvegicus 206-217