@article{mbs:/content/journal/micro/10.1099/00221287-148-8-2427, author = "Valens, Michèle and Broutelle, Anne-Cécile and Lefebvre, Mélanie and Blight, Mark A.", title = "A zinc metalloprotease inhibitor, Inh, from the insect pathogen Photorhabdus luminescens", journal= "Microbiology", year = "2002", volume = "148", number = "8", pages = "2427-2437", doi = "https://doi.org/10.1099/00221287-148-8-2427", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-148-8-2427", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "entomopathogen", keywords = "APRin, alkaline protease inhibitor", keywords = "Inh, inhibitor protein", keywords = "protein purification", keywords = "protease inhibitor", keywords = "APR, alkaline protease", abstract = "The entomopathogen Photorhabdus luminescens secretes many proteins during the late stages of insect larvae infection and during in vitro laboratory culture. The authors have previously characterized and purified a 55 kDa zinc metalloprotease, PrtA, from culture supernatants of P. luminescens. PrtA is secreted via a classical type I secretory pathway and is encoded within the operon prtA–inh–prtBCD. The 405 bp inh gene encodes a 14·8 kDa pre-protein that is translocated to the periplasm by the classical signal-peptide-dependent sec pathway, yielding the mature 11·9 kDa inhibitor Inh. Inh is a specific inhibitor of the protease PrtA. This study describes the purification of Inh and the initial characterization of its in vitro protease inhibition properties.", }