EC Number |
General Information |
Reference |
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3.4.22.B5 | more |
recombinant enzyme mutant CPB2.8DEKTACTE structure homology modeling using 1.75 A resolution crystal structure of cruzain complexed with the irreversible fluoromethyl ketone inhibitor Mor-Leu-Hpq was used as a template, PDB ID 1EWP, overview |
732753 |
3.4.22.B5 | physiological function |
amastigotes and promastigotes release the C-terminal fragment Cyspep into the extracellular environment, but only promastigotes release this polypeptide as Pro-CPB |
-, 754984 |
3.4.22.B5 | physiological function |
CPB is an important virulence factor, it inhibits lymphocytes Th1 and/or promotes Th2 responses either through proteolytic activity or through epitopes derived from its COOH-terminal extension. Some peptides from the CPB COOH-terminal extension influence host immune responses in the murine infection, thus helping Leishmania survival |
-, 717441 |
3.4.22.B5 | physiological function |
in a CPB-deficient mutant, both SNARE proteins VAMP3 and VAMP8 are down-modulated in a CPB-dependent manner. Expression of the virulence-associated GPI-anchored metalloprotease GP63 is inhibited in the absence of CPB. Expression of GP63 in the CPB-deficient mutant is sufficient to down-modulate VAMP3 and VAMP8. Episomal expression of GP63 enables the CPB-deficient mutant to establish infection in macrophages |
-, 755206 |
3.4.22.B5 | physiological function |
The proteolytic activity of Cbp proteins exhibits a gradual increase during the parasite's differentiation with low levels in samples of logarithmic promastigotes phase (3.2 mmol per min and mg protein) to a peak of activity after 72 h of incubation at 32°C (4.2 mmol per min and mg protein) followed by a subsequent decrease of 68 % of peak activity levels after 96 h of incubation at 32°C (2.8 mmol per min and mg protein) |
-, 752856 |
3.4.22.B5 | physiological function |
upon processing from its zymogen form, a release of the immunomodulatory CPB C-terminal extension (cyspep) into the cytoplasm of the macrophage takes place. Molecular models show a prevalence of beta-sheets in the cyspep protein. The formation of new strands, along with a rapid disruption of helical content, is observed |
754450 |