β-Lytic metalloendopeptidase

Efrat Kessler*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

2 Scopus citations

Abstract

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.

Original languageEnglish
Title of host publicationHandbook of Proteolytic Enzymes, Second Edition
Subtitle of host publicationVolume 1: Aspartic and Metallo Peptidases
PublisherElsevier
Pages998-1000
Number of pages3
Volume1
ISBN (Electronic)9780120796113
ISBN (Print)9780124121058
DOIs
StatePublished - 1 Jan 2004

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