Microbial metalloproteinases
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.24 Metalloendopeptidases > 3.4.24.4 microbial metalloproteinases
Serralysin is a ~50-kDa extracellular zinc metalloendopeptidase from Pseudomonas aeruginosa, Escherichia freundii, Serratia marcescens and Erwinia chrysanthemi, in peptidase family M10, formerly in EC 3.4.24.4. It shows broad specificity on the insulin B chain with some species variation, digests various proteins at pH optimum 9-10, and preferentially cleaves bonds with hydrophobic residues at P1'. In pathogenic bacteria it degrades host tissues and immune proteins. It features an M10-family zinc catalytic domain with a C-terminal repeat-like domain.
Serralysin is a ~50-kDa extracellular zinc metalloendopeptidase from Pseudomonas aeruginosa, Escherichia freundii, Serratia marcescens and Erwinia chrysanthemi, in peptidase family M10, formerly in EC 3.4.24.4. It shows broad specificity on the insulin B chain with some species variation, digests various proteins at pH optimum 9-10, and preferentially cleaves bonds with hydrophobic residues at P1'. In pathogenic bacteria it degrades host tissues and immune proteins. It features an M10-family zinc catalytic domain with a C-terminal repeat-like domain.
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