A comparison of the enzymatic properties of the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi
Congopain and cruzipain, the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi, were compared for their activities towards a series of new, sensitive fluorogenic substrates of the papain family of cysteine proteinases and for their sensitivity to inhibition by cystatins an...
| Autores principales: | , , , , , |
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| Formato: | Journal Article |
| Lenguaje: | Inglés |
| Publicado: |
Elsevier
1997
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| Materias: | |
| Acceso en línea: | https://hdl.handle.net/10568/33058 |
| _version_ | 1855518521873661952 |
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| author | Chagas, J.R. Authié, Edith Servean, C. Lalmanach, G. Juliano, L. Gauthier, F. |
| author_browse | Authié, Edith Chagas, J.R. Gauthier, F. Juliano, L. Lalmanach, G. Servean, C. |
| author_facet | Chagas, J.R. Authié, Edith Servean, C. Lalmanach, G. Juliano, L. Gauthier, F. |
| author_sort | Chagas, J.R. |
| collection | Repository of Agricultural Research Outputs (CGSpace) |
| description | Congopain and cruzipain, the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi, were compared for their activities towards a series of new, sensitive fluorogenic substrates of the papain family of cysteine proteinases and for their sensitivity to inhibition by cystatins and related biotinylated peptidyl diazomethanes. Low K1 values, in the 10 pM range, were found for the interaction of both proteinases with natural cystatin inhibitors. The kinetic constants for the hydrolysis of cystatin-derived substrates, and the inhibition by related diazomethanes' were essentially identical. Unlike cathepsins B, and L, the related mammal papain family proteinases, congopain and cruzipain accomodate a prolyl residue in P2'. Substrates having the sequence VGGP from P2 to P2' were hydrolysed by both congopain and cruzipain with a K cat/Km greater than 4.10(3) mM-1 S-1. Irreversible diazomethane inhibitors, deduced from the unprime sequence of cystatin-derived substrates, inhibited the two parasite proteinases. N-terminal labelling of diazomethanes with a biotin group did not alter the rate of inhibitition significantly, which provides a useful tool for examining the distribution of these enzymes in the parasite and in the host. Despite their similar activities on cystatin-derived substrates, congopain and cruzipain had significantly different pH-activity profiles when assayed with a cystatin-derived substrate. They were correlated with structural differences, especially at the presumed S2 subsites. |
| format | Journal Article |
| id | CGSpace33058 |
| institution | CGIAR Consortium |
| language | Inglés |
| publishDate | 1997 |
| publishDateRange | 1997 |
| publishDateSort | 1997 |
| publisher | Elsevier |
| publisherStr | Elsevier |
| record_format | dspace |
| spelling | CGSpace330582024-05-01T08:15:47Z A comparison of the enzymatic properties of the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi Chagas, J.R. Authié, Edith Servean, C. Lalmanach, G. Juliano, L. Gauthier, F. trypanosoma congolense trypanosoma cruzi cysteine enzymes enzyme inhibitors molecular biology parasitology Congopain and cruzipain, the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi, were compared for their activities towards a series of new, sensitive fluorogenic substrates of the papain family of cysteine proteinases and for their sensitivity to inhibition by cystatins and related biotinylated peptidyl diazomethanes. Low K1 values, in the 10 pM range, were found for the interaction of both proteinases with natural cystatin inhibitors. The kinetic constants for the hydrolysis of cystatin-derived substrates, and the inhibition by related diazomethanes' were essentially identical. Unlike cathepsins B, and L, the related mammal papain family proteinases, congopain and cruzipain accomodate a prolyl residue in P2'. Substrates having the sequence VGGP from P2 to P2' were hydrolysed by both congopain and cruzipain with a K cat/Km greater than 4.10(3) mM-1 S-1. Irreversible diazomethane inhibitors, deduced from the unprime sequence of cystatin-derived substrates, inhibited the two parasite proteinases. N-terminal labelling of diazomethanes with a biotin group did not alter the rate of inhibitition significantly, which provides a useful tool for examining the distribution of these enzymes in the parasite and in the host. Despite their similar activities on cystatin-derived substrates, congopain and cruzipain had significantly different pH-activity profiles when assayed with a cystatin-derived substrate. They were correlated with structural differences, especially at the presumed S2 subsites. 1997-09 2013-07-03T05:26:00Z 2013-07-03T05:26:00Z Journal Article https://hdl.handle.net/10568/33058 en Limited Access Elsevier Molecular and Biochemical Parasitology;88: 85-94 |
| spellingShingle | trypanosoma congolense trypanosoma cruzi cysteine enzymes enzyme inhibitors molecular biology parasitology Chagas, J.R. Authié, Edith Servean, C. Lalmanach, G. Juliano, L. Gauthier, F. A comparison of the enzymatic properties of the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi |
| title | A comparison of the enzymatic properties of the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi |
| title_full | A comparison of the enzymatic properties of the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi |
| title_fullStr | A comparison of the enzymatic properties of the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi |
| title_full_unstemmed | A comparison of the enzymatic properties of the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi |
| title_short | A comparison of the enzymatic properties of the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi |
| title_sort | comparison of the enzymatic properties of the major cysteine proteinases from trypanosoma congolense and trypanosoma cruzi |
| topic | trypanosoma congolense trypanosoma cruzi cysteine enzymes enzyme inhibitors molecular biology parasitology |
| url | https://hdl.handle.net/10568/33058 |
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