Gelatinase B
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.24 Metalloendopeptidases > 3.4.24.35 gelatinase B
Leishmanolysin is a membrane-bound zinc metalloendopeptidase on the promastigote of various Leishmania species, the type example of peptidase family M8. It contains a zinc-binding consensus sequence and is strongly inhibited by Z-Tyr-Leu-NHOH; it can auto-activate its proenzyme by cleavage of the Val100-/-Val bond and shows acid pH optimum with certain protein substrates. It prefers hydrophobic residues at P1 and P1' and basic residues at P2' and P3', cleaving a model nonapeptide at -Ala-Tyr-/-Leu-Lys-Lys-. On the parasite surface it degrades host complement, extracellular matrix and immune proteins. It features a zinc catalytic ectodomain anchored in the parasite membrane.
Leishmanolysin is a membrane-bound zinc metalloendopeptidase on the promastigote of various Leishmania species, the type example of peptidase family M8. It contains a zinc-binding consensus sequence and is strongly inhibited by Z-Tyr-Leu-NHOH; it can auto-activate its proenzyme by cleavage of the Val100-/-Val bond and shows acid pH optimum with certain protein substrates. It prefers hydrophobic residues at P1 and P1' and basic residues at P2' and P3', cleaving a model nonapeptide at -Ala-Tyr-/-Leu-Lys-Lys-. On the parasite surface it degrades host complement, extracellular matrix and immune proteins. It features a zinc catalytic ectodomain anchored in the parasite membrane.
References:
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