[1]
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NUCLEOTIDE SEQUENCE.
STRAIN=Tulahuen;
PubMed=1559982 [NCBI, ExPASy, EBI, Israel, Japan]
Eakin A.E.,
Mills A.A.,
Harth G.,
McKerrow J.H.,
Craik C.S.;
"The sequence, organization, and expression of the major cysteine protease (cruzain) from Trypanosoma cruzi.";
J. Biol. Chem. 267:7411-7420(1992).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONES 1800-2 AND 1800-4).
STRAIN=Tulahuen 2;
DOI=10.1016/0166-6851(92)90219-A; PubMed=1311053 [NCBI, ExPASy, EBI, Israel, Japan]
Campetella O.,
Henriksson J.,
Aaslund L.,
Frasch A.C.C.,
Pettersson U.,
Cazzulo J.J.;
"The major cysteine proteinase (cruzipain) from Trypanosoma cruzi is encoded by multiple polymorphic tandemly organized genes located on different chromosomes.";
Mol. Biochem. Parasitol. 50:225-234(1992).
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-306.
STRAIN=RA;
DOI=10.1016/0166-6851(90)90002-4; PubMed=2406590 [NCBI, ExPASy, EBI, Israel, Japan]
Eakin A.E.,
Bouvier J.,
Sakanari J.A.,
Craik C.S.,
McKerrow J.H.;
"Amplification and sequencing of genomic DNA fragments encoding cysteine proteases from protozoan parasites.";
Mol. Biochem. Parasitol. 39:1-8(1990).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] OF 295-467.
STRAIN=Tulahuen 2;
DOI=10.1016/0166-6851(91)90103-D; PubMed=2038364 [NCBI, ExPASy, EBI, Israel, Japan]
Aaslund L.,
Henriksson J.,
Campetella O.,
Frasch A.C.C.,
Pettersson U.,
Cazzulo J.J.;
"The C-terminal extension of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi.";
Mol. Biochem. Parasitol. 45:345-348(1991).
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[5]
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AUTOCATALYSIS OF C-TERMINAL.
STRAIN=Tulahuen 2;
DOI=10.1016/0166-6851(91)90216-S; PubMed=2011151 [NCBI, ExPASy, EBI, Israel, Japan]
Hellman U.,
Wernstedt C.,
Cazzulo J.J.;
"Self-proteolysis of the cysteine proteinase, cruzipain, from Trypanosoma cruzi gives a major fragment corresponding to its carboxy-terminal domain.";
Mol. Biochem. Parasitol. 44:15-21(1991).
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[6]
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SPECIFICITY.
STRAIN=Tulahuen 2;
DOI=10.1016/0167-4838(90)90166-D; PubMed=2407295 [NCBI, ExPASy, EBI, Israel, Japan]
Cazzulo J.J.,
Cazzulo-Franke M.C.,
Martinez J.,
Franke de Cazzulo B.M.;
"Some kinetic properties of a cysteine proteinase (cruzipain) from Trypanosoma cruzi.";
Biochim. Biophys. Acta 1037:186-191(1990).
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[7]
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PROTEIN SEQUENCE OF 123-146 AND 304-317.
DOI=10.1016/0166-6851(89)90039-X; PubMed=2651912 [NCBI, ExPASy, EBI, Israel, Japan]
Cazzulo J.J.,
Couso R.,
Raimondi A.,
Wernstedt C.,
Hellman U.;
"Further characterization and partial amino acid sequence of a cysteine proteinase from Trypanosoma cruzi.";
Mol. Biochem. Parasitol. 33:33-42(1989).
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[8]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 123-337.
PubMed=9260273 [NCBI, ExPASy, EBI, Israel, Japan]
Gillmor S.A.,
Craik C.S.,
Fletterick R.J.;
"Structural determinants of specificity in the cysteine protease cruzain.";
Protein Sci. 6:1603-1611(1997).
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- 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.
- CATALYTIC ACTIVITY: Broad endopeptidase specificity similar to that of cathepsin L.
- ENZYME REGULATION: Strongly inhibited by E-64 (L-trans-epoxysuccinylleucylamido(4-guanidino)butane), Leupeptin, and N-alpha-p-tosyl-L-lysine chloromethyl ketone.
- DEVELOPMENTAL STAGE: Present in all developmental stages.
- MISCELLANEOUS: Purified cruzipain is able to degrade itself, yielding a complex mixture of small peptides, and a major 25 kDa fragment.
- SIMILARITY: Belongs to the peptidase C1 family [view classification].
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