This chapter covers the structural chemistry and the biological aspects of β-lytic metalloendopeptidase. β-lytic metalloendopeptidase, formerly β-lytic protease, was discovered over three decades ago in the culture filtrate of Myxobacter 495, a soil bacterium initially defined as Sorangium sp. and currently classified as Lysobacter enzymogenes. This organism has a remarkable ability to lyse other bacteria and some soil nematodes, a property by which it was originally selected. The trivial name β-lytic protease stems from the enzyme's ability to cause lysis of bacterial cell walls and differentiates it from α-lytic protease. L. enzymogenes β-lytic metalloendopeptidase lyses Arthrobacter globiformis and Micrococcus luteus (previously M. lysodeikticus) cells. Lysis of the former is more efficient. The enzyme is likely to also lyse Staphylococcus aureus cells. L. enzymogenes β-lytic metalloendopeptidase is a basic 19.1 kDa protein. The enzyme (178 amino acid residues) contains two disulfide bonds between residues 65–111 and 155–168, and one zinc atom per mol that is essential for activity. It does not contain the consensus zinc-binding site HEXXH but has a conserved HXH sequence that is implicated in zinc binding.
|Title of host publication||Handbook of Proteolytic Enzymes, Second Edition|
|Subtitle of host publication||Volume 1: Aspartic and Metallo Peptidases|
|Number of pages||3|
|State||Published - 1 Jan 2004|