true1992-05-012024-03-27144CYSP_TRYCRThe sequence, organization, and expression of the major cysteine protease (cruzain) from Trypanosoma cruzi.Eakin A.E.Mills A.A.Harth G.McKerrow J.H.Craik C.S.doi:10.1016/s0021-9258(18)42533-11992J. Biol. Chem.2677411-7420NUCLEOTIDE SEQUENCETulahuenThe major cysteine proteinase (cruzipain) from Trypanosoma cruzi is encoded by multiple polymorphic tandemly organized genes located on different chromosomes.Campetella O.Henriksson J.Aaslund L.Frasch A.C.C.Pettersson U.Cazzulo J.J.doi:10.1016/0166-6851(92)90219-a1992Mol. Biochem. Parasitol.50225-234NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONES 1800-2 AND 1800-4)Tulahuen 2Amplification and sequencing of genomic DNA fragments encoding cysteine proteases from protozoan parasites.Eakin A.E.Bouvier J.Sakanari J.A.Craik C.S.McKerrow J.H.doi:10.1016/0166-6851(90)90002-41990Mol. Biochem. Parasitol.391-8NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-306RAThe C-terminal extension of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi.Aaslund L.Henriksson J.Campetella O.Frasch A.C.C.Pettersson U.Cazzulo J.J.doi:10.1016/0166-6851(91)90103-d1991Mol. Biochem. Parasitol.45345-348NUCLEOTIDE SEQUENCE [MRNA] OF 295-467Self-proteolysis of the cysteine proteinase, cruzipain, from Trypanosoma cruzi gives a major fragment corresponding to its carboxy-terminal domain.Hellman U.Wernstedt C.Cazzulo J.J.doi:10.1016/0166-6851(91)90216-s1991Mol. Biochem. Parasitol.4415-21AUTOCATALYSIS OF C-TERMINALSome kinetic properties of a cysteine proteinase (cruzipain) from Trypanosoma cruzi.Cazzulo J.J.Cazzulo-Franke M.C.Martinez J.Franke de Cazzulo B.M.doi:10.1016/0167-4838(90)90166-d1990Biochim. Biophys. Acta1037186-191SPECIFICITYFurther characterization and partial amino acid sequence of a cysteine proteinase from Trypanosoma cruzi.Cazzulo J.J.Couso R.Raimondi A.Wernstedt C.Hellman U.doi:10.1016/0166-6851(89)90039-x1989Mol. Biochem. Parasitol.3333-42PROTEIN SEQUENCE OF 123-146 AND 304-317Structural determinants of specificity in the cysteine protease cruzain.Gillmor S.A.Craik C.S.Fletterick R.J.doi:10.1002/pro.55600608011997Protein Sci.61603-1611X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 123-3372.00A=123-3372.00A=123-3372.00A=123-3372.10A=123-3371.75A=123-3372.15A/B/C=123-3371.60A=123-3371.80A=123-3372.00A=123-3371.20A=123-3371.20A=123-3372.30X=123-3372.20A=123-3371.95A/C=123-3371.75A/B=123-3371.10A=123-3371.20A=123-3371.28A=123-3371.50A/C=123-3372.62A/B/C/D/E=123-3371.27A/B=122-3373.13A/B/C/D/E=123-3372.70A/B/C=123-3373.27A/B/C/D/E=122-3372.51A/B/C=122-3371.19A/B=123-3371.19A/B=123-3371.94A=123-3372.20A/B/C/D/E/F=123-3372.14A=123-3372.08A=123-3373-[N-[benzyloxycarbonyl]-phenylalaninyl-amino]-5-phenyl-pentane-1-sulfonylmethylbenzene4-Methyl-N-[(2S)-1-oxo-3-phenyl-1-[[(3S)-1-phenyl-5-(phenylmethoxysulfamoyl)pentan-3-yl]amino]propan-2-yl]piperazine-1-carboxamide4-Nitrophenyl (3S)-3-({N-[(benzyloxy)carbonyl]-L-phenylalanyl}amino)-5-phenyl-1-pentanesulfonate[1-(1-Benzyl-3-Hydroxy-2-Oxo-Propylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl Ester[1-(1-Methyl-4,5-Dioxo-Pent-2-Enylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl Ester[1-(3-hydroxy-2-oxo-1-phenethyl-propylcarbamoyl)2-phenyl-ethyl]-carbamic acid pyridin-4-ylmethyl esterBenzyl N-[(2S)-5-(diaminomethylamino)-1-[[(2S)-4-fluoro-3-oxobutan-2-yl]amino]-1-oxopentan-2-yl]carbamateWRR-112WRR-204WRR-996524Peptidase_C1ACysteine proteinasesDUF3586Papain-like_cys_pep_sfPept_asp_ASPept_cys_ASPept_his_ASPeptidase_C1APeptidase_C1A_CPeptidase_C1A_papain-likeProt_inhib_I29CATHEPSIN OCYSTEINE PROTEASE FAMILY C1-RELATEDDUF3586Inhibitor_I29Peptidase_C1PAPAINInhibitor_I29Pept_C1Cysteine proteinasesTHIOL_PROTEASE_ASNTHIOL_PROTEASE_CYSTHIOL_PROTEASE_HISCruzipain3.4.22.51CruzaineMajor cysteine proteinaseHydrolyzes 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.The cysteine protease may play an important role in the development and differentiation of the parasites at several stages of their life cycle.Strongly inhibited by E-64 (L-trans-epoxysuccinylleucylamido(4-guanidino)butane), Leupeptin, and N-alpha-p-tosyl-L-lysine chloromethyl ketone.Present in all developmental stages.Purified cruzipain is able to degrade itself, yielding a complex mixture of small peptides, and a major 25 kDa fragment.Belongs to the peptidase C1 family.118Activation peptide19122Cruzipain36459123467Disordered333355147284304Cleavage; by autolysis337338N-linked (GlcNAc...) asparagine169N-linked (GlcNAc...) asparagine292N-linked (GlcNAc...) asparagine377144185178223277325In clone 1800-2.S9In clone 1800-2.A35In clone 1800-2.V39In clone 1800-4.N51In clone 1800-2.R56In clone 1800-4.G76In clone 1800-4.G109In clone 1800-2.N117G146In strain: RA.SG157158In clones 1800-2 and 1800-4.G186In strain: RA.G204In clones 1800-2 and 1800-4.CV250251In strain: RA.H261262In clone 1800-4.F286In strain: RA.LIn clone 1800-2.A308D313In clone 1800-2.F409In clone 1800-2.Q427In clone 1800-2.W430In clone 1800-2.Y457In clone 1800-2.Q461C3571251281291321431451621721801821841902002072082102162182252272302392442542572632652662682712742972993033073093153223243263293361992-05-011true498366e32d0bd89f39592ee9190e688af10d6MSGWARALLLAAVLVVMACLVPAATASLHAEETLTSQFAEFKQKHGRVYESAAEEAFRLSVFRENLFLARLHAAANPHATFGVTPFSDLTREEFRSRYHNGAAHFAAAQERARVPVKVEVVGAPAAVDWRARGAVTAVKDQGQCGSCWAFSAIGNVECQWFLAGHPLTNLSEQMLVSCDKTDSGCSGGLMNNAFEWIVQENNGAVYTEDSYPYASGEGISPPCTTSGHTVGATITGHVELPQDEAQIAAWLAVNGPVAVAVDASSWMTYTGGVMTSCVSEQLDHGVLLVGYNDSAAVPYWIIKNSWTTQWGEEGYIRIAKGSNQCLVKEEASSAVVGGPGPTPEPTTTTTTSAPGPSPSYFVQMSCTDAACIVGCENVTLPTGQCLLTTSGVSAIVTCGAETLTEEVFLTSTHCSGPSVRSSVPLNKCNRLLRGSVEFFCGSSSSGRLADVDRQRRHQPYHSRHRRLtruetruetruetruetruetruetrue