Cruzipain

Details

Name
Cruzipain
Synonyms
  • 3.4.22.51
  • Cruzaine
  • Major cysteine proteinase
Gene Name
Not Available
Organism
Trypanosoma cruzi
Amino acid sequence
>lcl|BSEQ0010901|Cruzipain
MSGWARALLLAAVLVVMACLVPAATASLHAEETLTSQFAEFKQKHGRVYESAAEEAFRLS
VFRENLFLARLHAAANPHATFGVTPFSDLTREEFRSRYHNGAAHFAAAQERARVPVKVEV
VGAPAAVDWRARGAVTAVKDQGQCGSCWAFSAIGNVECQWFLAGHPLTNLSEQMLVSCDK
TDSGCSGGLMNNAFEWIVQENNGAVYTEDSYPYASGEGISPPCTTSGHTVGATITGHVEL
PQDEAQIAAWLAVNGPVAVAVDASSWMTYTGGVMTSCVSEQLDHGVLLVGYNDSAAVPYW
IIKNSWTTQWGEEGYIRIAKGSNQCLVKEEASSAVVGGPGPTPEPTTTTTTSAPGPSPSY
FVQMSCTDAACIVGCENVTLPTGQCLLTTSGVSAIVTCGAETLTEEVFLTSTHCSGPSVR
SSVPLNKCNRLLRGSVEFFCGSSSSGRLADVDRQRRHQPYHSRHRRL
Number of residues
467
Molecular Weight
49835.59
Theoretical pI
6.01
GO Classification
Functions
cysteine-type endopeptidase activity
General Function
Cysteine-type endopeptidase activity
Specific 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.The cysteine protease may play an important role in the development and differentiation of the parasites at several stages of their life cycle.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0002568|1404 bp
ATGTCTGGCTGGGCGCGTGCGCTGTTGCTCGCGGCCGTCCTGGTCGTCATGGCGTGCCTC
GTCCCCGCGGCGACGGCGAGCCTGCATGCGGAGGAGACGCTGACGTCGCAATTCGCAGAA
TTCAAGCAGAAGCATGGCAGGGTGTACGAGAGCGCCGCGGAGGAGGCGTTCCGCCTGAGC
GTGTTCAGGGAGAACCTGTTTCTTGCGAGGCTGCACGCCGCGGCAAACCCACACGCGACC
TTCGGCGTCACGCCCTTCTCGGACCTCACGCGCGAGGAATTCCGGTCCCGCTACCACAAC
GGCGCGGCGCACTTTGCGGCGGCGCAGGAGCGCGCGAGAGTGCCGGTGAAGGTGGAGGTA
GTTGGCGCGCCCGCGGCAGTGGATTGGCGTGCGAGAGGCGCCGTGACAGCCGTCAAGGAC
CAGGGCCAATGCGGTTCGTGCTGGGCCTTCTCCGCCATTGGCAACGTTGAGTGCCAGTGG
TTTCTTGCCGGCCACCCGCTGACGAACCTGTCGGAGCAGATGCTCGTGTCGTGCGACAAA
ACGGACTCTGGCTGCAGTGGTGGCCTGATGAACAACGCCTTTGAGTGGATTGTGCAGGAG
AATAACGGCGCCGTGTACACGGAGGACAGCTACCCTTATGCGTCGGGCGAGGGGATATCG
CCGCCGTGCACGACGTCAGGCCACACGGTGGGTGCCACGATTACCGGTCACGTTGAATTA
CCTCAGGACGAGGCCCAAATAGCCGCATGGCTTGCAGTCAATGGCCCGGTTGCCGTTGCC
GTCGACGCCAGCAGCTGGATGACCTACACGGGCGGCGTTATGACGAGCTGCGTCTCCGAG
CAGCTGGATCACGGCGTTCTTCTCGTCGGCTACAATGACAGCGCCGCAGTGCCGTACTGG
ATCATCAAGAACTCGTGGACCACGCAGTGGGGCGAGGAAGGCTACATCCGCATTGCAAAG
GGCTCGAACCAGTGCCTTGTCAAGGAGGAGGCGAGCTCCGCGGTGGTCGGTGGTCCCGGA
CCCACTCCCGAGCCAACCACCACGACAACCACAAGTGCCCCAGGACCGTCCCCATCGTAC
TTTGTGCAGATGTCCTGCACTGACGCTGCGTGCATTGTCGGGTGCGAGAACGTGACGTTA
CCGACCGGTCAGTGTCTCCTGACCACCAGCGGCGTCTCTGCCATTGTCACGTGCGGTGCT
GAGACTCTCACAGAAGAAGTCTTCCTTACGAGTACGCACTGCAGCGGCCCATCGGTGAGG
TCCTCTGTTCCTCTCAACAAATGCAACCGGCTTTTAAGAGGCTCCGTTGAGTTCTTCTGC
GGCTCCAGCTCCAGTGGCCGACTGGCCGACGTGGACAGGCAGCGTCGCCATCAGCCATAC
CACAGCCGTCATCGCCGCCTCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP25779
UniProtKB Entry NameCYSP_TRYCR
GenBank Protein ID162048
GenBank Gene IDM84342
General References
  1. Eakin AE, Mills AA, Harth G, McKerrow JH, Craik CS: The sequence, organization, and expression of the major cysteine protease (cruzain) from Trypanosoma cruzi. J Biol Chem. 1992 Apr 15;267(11):7411-20. [Article]
  2. Campetella O, Henriksson J, Aslund L, Frasch AC, Pettersson U, Cazzulo JJ: The major cysteine proteinase (cruzipain) from Trypanosoma cruzi is encoded by multiple polymorphic tandemly organized genes located on different chromosomes. Mol Biochem Parasitol. 1992 Feb;50(2):225-34. [Article]
  3. Eakin AE, Bouvier J, Sakanari JA, Craik CS, McKerrow JH: Amplification and sequencing of genomic DNA fragments encoding cysteine proteases from protozoan parasites. Mol Biochem Parasitol. 1990 Feb;39(1):1-8. [Article]
  4. Aslund L, Henriksson J, Campetella O, Frasch AC, Pettersson U, Cazzulo JJ: The C-terminal extension of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi. Mol Biochem Parasitol. 1991 Apr;45(2):345-7. [Article]
  5. Hellman U, Wernstedt C, Cazzulo JJ: Self-proteolysis of the cysteine proteinase, cruzipain, from Trypanosoma cruzi gives a major fragment corresponding to its carboxy-terminal domain. Mol Biochem Parasitol. 1991 Jan;44(1):15-21. [Article]
  6. Cazzulo JJ, Cazzulo Franke MC, Martinez J, Franke de Cazzulo BM: Some kinetic properties of a cysteine proteinase (cruzipain) from Trypanosoma cruzi. Biochim Biophys Acta. 1990 Feb 9;1037(2):186-91. [Article]
  7. Cazzulo JJ, 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. 1989 Feb;33(1):33-41. [Article]
  8. Gillmor SA, Craik CS, Fletterick RJ: Structural determinants of specificity in the cysteine protease cruzain. Protein Sci. 1997 Aug;6(8):1603-11. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01810[1-(1-Methyl-4,5-Dioxo-Pent-2-Enylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl EsterexperimentalunknownDetails
DB01871[1-(1-Benzyl-3-Hydroxy-2-Oxo-Propylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl EsterexperimentalunknownDetails
DB020514-Nitrophenyl (3S)-3-({N-[(benzyloxy)carbonyl]-L-phenylalanyl}amino)-5-phenyl-1-pentanesulfonateexperimentalunknownDetails
DB02128[1-(3-hydroxy-2-oxo-1-phenethyl-propylcarbamoyl)2-phenyl-ethyl]-carbamic acid pyridin-4-ylmethyl esterexperimentalunknownDetails
DB022003-[N-[benzyloxycarbonyl]-phenylalaninyl-amino]-5-phenyl-pentane-1-sulfonylmethylbenzeneexperimentalunknownDetails
DB03536Benzyl N-[(2S)-5-(diaminomethylamino)-1-[[(2S)-4-fluoro-3-oxobutan-2-yl]amino]-1-oxopentan-2-yl]carbamateexperimentalunknownDetails
DB03573WRR-99experimentalunknownDetails
DB03691WRR-112experimentalunknownDetails
DB04427N-{(3S)-1-[(Benzyloxy)sulfamoyl]-5-phenyl-3-pentanyl}-Nα-[(4-methyl-1-piperazinyl)carbonyl]-L-phenylalaninamideexperimentalunknownDetails
DB04502WRR-204experimentalunknownDetails