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Literature summary for 3.4.22.51 extracted from

  • Gillmor, S.A.; Craik, C.S.; Fletterick, R.J.
    Structural determinants of specificity in the cysteine protease cruzain (1997), Protein Sci., 6, 1603-1611.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.51

Crystallization (Commentary)

Crystallization (Comment) Organism
bound to benzoyl-Arg-Ala-fluoromethyl ketone and benzoyl-Tyr-Ala-fluoromethyl ketone, hanging drop vapor diffusion method Trypanosoma cruzi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.001
-
 benzoyl-Tyr-Arg-7-amido-4-methylcoumarin
-
 Trypanosoma cruzi
0.01 0.015 benzoyl-Phe-Arg-7-amido-4-methylcoumarin
-
 Trypanosoma cruzi

Organism

Organism UniProt Comment Textmining
Trypanosoma cruzi Q598P5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
-
 Trypanosoma cruzi benzoyl-Phe-Arg + 7-amino-4-methylcoumarin
-
 ?
benzoyl-Tyr-Arg-7-amido-4-methylcoumarin + H2O
-
 Trypanosoma cruzi benzoyl-Tyr-Arg + 7-amino-4-methylcoumarin
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 substrates placing hydrophobic residues in the specificity pocket are cleaved at a broader pH range than hydrophilic substrates Trypanosoma cruzi

pH Range

pH Minimum pH Maximum Comment Organism
4.5 7.4 hydrophobic substrates reach 50% activity at pH 4.5 and maintain full activity above pH 7.5, more hydrophilic side chains only reach 50% activity at pH 5.5-6 Trypanosoma cruzi