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3.4.22.51: cruzipain

This is an abbreviated version!
For detailed information about cruzipain, go to the full flat file.

Word Map on EC 3.4.22.51

Reaction

broad endopeptidase specificity similar to that of cathepsin L =

Synonyms

brucipain, cathepsin L-like cysteine protease, cathepsin L-like protease, CatL-like protease, congopain, CP, cruzain, cruzipain, cruzipain 2, CTE-truncated recombinant protease, cz, CZP, evansain, family C1 cysteine peptidase, GP57/51, kinin-releasing cysteine proteases, lysosomal-like cysteine protease, major cysteine proteinase, major cysteine-protease, NACrI, proteinase, Trypanosoma congolese cysteine, proteinase, Trypanosoma cruzi cysteine, proteinase, Trypanosoma cysteine, rhodesain, TCI, TCII, trypanopain, Trypanosoma congolese cysteine protease, Trypanosoma cruzi cysteine protease, Trypanosoma cysteine protease

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.51 cruzipain

Engineering

Engineering on EC 3.4.22.51 - cruzipain

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C25A
enzyme is inactive
E208A
the mutant enzyme recognizes benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin less effectively than wild-type cruzain does, turnover of the substrate is comparable, suggesting that once bound, mutant cruzain processes benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarinat rates similar to that of the wild-type enzyme. Diminutions by 300fold and 200fold in the kcat/Km values of benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin and benzyloxycarbonyl-Arg-Ala-7-amido-4-methylcoumarin, respectively, are observed for the E208A mutant cruzain compared to that of the wild type, suggesting that ion pairing between Glu208 and P2 Arg is essential for recognition of these substrates. This is also reflected in values of Km, which are increased for benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin (10fold) and benzyloxycarbonyl-Arg-Ala-7-amido-4-methylcoumarin (4fold)
E219P
variant with altered cleavage recognition site
additional information