| IED ID | IndEnz0002006242 |
| Enzyme Type ID | protease006242 |
| Protein Name |
Cruzipain EC 3.4.22.51 Cruzaine Major cysteine proteinase |
| Gene Name | |
| Organism | Trypanosoma cruzi |
| Taxonomic Lineage | cellular organisms Eukaryota Discoba Euglenozoa Kinetoplastea (kinetoplasts) Metakinetoplastina Trypanosomatida Trypanosomatidae Trypanosoma Schizotrypanum Trypanosoma cruzi |
| Enzyme Sequence | MSGWARALLLAAVLVVMACLVPAATASLHAEETLTSQFAEFKQKHGRVYESAAEEAFRLSVFRENLFLARLHAAANPHATFGVTPFSDLTREEFRSRYHNGAAHFAAAQERARVPVKVEVVGAPAAVDWRARGAVTAVKDQGQCGSCWAFSAIGNVECQWFLAGHPLTNLSEQMLVSCDKTDSGCSGGLMNNAFEWIVQENNGAVYTEDSYPYASGEGISPPCTTSGHTVGATITGHVELPQDEAQIAAWLAVNGPVAVAVDASSWMTYTGGVMTSCVSEQLDHGVLLVGYNDSAAVPYWIIKNSWTTQWGEEGYIRIAKGSNQCLVKEEASSAVVGGPGPTPEPTTTTTTSAPGPSPSYFVQMSCTDAACIVGCENVTLPTGQCLLTTSGVSAIVTCGAETLTEEVFLTSTHCSGPSVRSSVPLNKCNRLLRGSVEFFCGSSSSGRLADVDRQRRHQPYHSRHRRL |
| Enzyme Length | 467 |
| Uniprot Accession Number | P25779 |
| Absorption | |
| Active Site | ACT_SITE 147; ACT_SITE 284; ACT_SITE 304 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by E-64 (L-trans-epoxysuccinylleucylamido(4-guanidino)butane), Leupeptin, and N-alpha-p-tosyl-L-lysine chloromethyl ketone. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity similar to that of cathepsin L.; EC=3.4.22.51; |
| DNA Binding | |
| EC Number | 3.4.22.51 |
| Enzyme Function | FUNCTION: Hydrolyzes chromogenic peptides at the carboxyl Arg or Lys; requires at least one more amino acid, preferably Arg, Phe, Val or Leu, between the terminal Arg or Lys and the amino-blocking group.; FUNCTION: The cysteine protease may play an important role in the development and differentiation of the parasites at several stages of their life cycle. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (13); Chain (1); Disulfide bond (3); Glycosylation (3); Helix (9); Natural variant (23); Propeptide (1); Region (1); Sequence conflict (1); Signal peptide (1); Site (1); Turn (2) |
| Keywords | 3D-structure;Autocatalytic cleavage;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000305 |
| Structure 3D | X-ray crystallography (29) |
| Cross Reference PDB | 1AIM; 1EWL; 1EWM; 1EWO; 1EWP; 1F29; 1F2A; 1F2B; 1F2C; 1ME3; 1ME4; 1U9Q; 2AIM; 2OZ2; 3HD3; 3I06; 3IUT; 3KKU; 3LXS; 4KLB; 4PI3; 4QH6; 4W5B; 4W5C; 4XUI; 6N3S; 6O2X; 6UX6; 7JUJ; |
| Mapped Pubmed ID | 10997902; 12467703; 15727867; 19620707; 19773167; 19908842; 20088534; 20540517; 20856868; 23991231; 26173110; 26819670; 31204688; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,836 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.51; |