Glutamyl Endopeptidase I

Stennicke, Henning R.; Breddam, Klaus

doi:10.1016/b978-0-12-382219-2.00561-5

Cited by 2 publications

(2 citation statements)

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“…The derived amino acid sequence of GluNS was predicted that contains some special domains by bioinformatics analysis, such as streptogrisin prodomain and peptidase S1. As mentioned in the relevant literatures, the glutamic endopeptidases are divided into three groups according to the origin of the bacterial species (Stennicke & Breddam, 2013): Staphylococcal group (Ohara‐Nemoto et al., 2002), Bacillus group (Kakudo et al., 1992; Sloma et al., 1990) and Streptomyces group (Kitadokoro et al., 1993; Suzuki et al., 1994). Several reports have shown that on account of the degradation of neutrophil defensins, IgG and α‐1‐antichymotrypsin, a Staphylococcal glutamyl endopeptidase, V8 proteinase (GluV8), is considered to play an important role in septicaemia in human staphylococcal infections (Potempa et al., 1986; Selsted et al., 1993).…”

Section: Discussionmentioning

confidence: 99%

“…Relevant studies have shown that the immunological response to GluV8 could be an important host‐defence mechanism (Calander et al., 2008). Functionally, glutamyl endopeptidase family members specifically cleave the carboxyl side of the peptide bond of negatively charged residue, such as glutamic acid and aspartic acid (Stennicke & Breddam, 2013).…”

Section: Introductionmentioning

confidence: 99%

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Characterization and function study of a glutamyl endopeptidase homolog from Nocardia seriolae

Hou

Chen

et al. 2020

Journal of Fish Diseases

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Glutamic endopeptidases (Glu), belonging to the class of serine proteases, are a subfamily of chymotrypsin‐like proteolytic enzymes, which are regarded as important virulence factors in bacteria. However, the roles of glutamic endopeptidases of Nocardia seriolae in pathogenic process still remain uncertain. Here, a glutamic endopeptidase homolog from N. seriolae (GluNS) was cloned and its function was elucidated. GluNS encoded a 414‐aa protein which shared 93% identity to N. concava. In the phylogenetic tree, the glutamic endopeptidases of genus Nocardia clustered together firstly and then clustered with Streptomyces species. Moreover, GluNS was identified to be a secreted protein of N. seriolae and localized in the mitochondria of FHM cells. The transient overexpression of GluNS significantly induced increase in caspase‐3 activity and decrease in ΔΨm values in FHM cells. The number of apoptotic bodies was remarkably higher than that in control group. Taken together, GluNS overexpression induced apoptotic characteristics in FHM cells. This study provided new insights into the function of glutamic endopeptidase from N. seriolae.

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