Entry
Name
fragilysin;
Bacteroides fragilis (entero)toxin
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
Reaction(IUBMB)
Broad proteolytic specificity, bonds hydrolysed including -Gly!Leu-, -Met!Leu-, -Phe!Leu-, -Cys!Leu-, Leu!Gly
Comment
Thought to be a cause of diarrhoea in animals and humans. Hydrolyses extracellular matrix proteins, and disrupts tight junctions of intestinal epithelial cells. Also degrades intracellular, cytoskeletal proteins actin, myosin and others. In peptidase family M10 (interstitial collagenase family)
History
EC 3.4.24.74 created 1997
Orthology
Genes
BFB : VU15_14325 VU15_18690
Taxonomy
Reference
Authors
Moncrief JS, Obiso R Jr, Barroso LA, Kling JJ, Wright RL, Van Tassell RL, Lyerly DM, Wilkins TD.
Title
The enterotoxin of Bacteroides fragilis is a metalloprotease.
Journal
Reference
Authors
Obiso RJ Jr, Lyerly DM, Van Tassell RL, Wilkins TD.
Title
Proteolytic activity of the Bacteroides fragilis enterotoxin causes fluid secretion and intestinal damage in vivo.
Journal
Reference
Authors
Donelli G, Fabbri A, Fiorentini C.
Title
Bacteroides fragilis enterotoxin induces cytoskeletal changes and surface blebbing in HT-29 cells.
Journal
Reference
Authors
Koshy SS, Montrose MH, Sears CL.
Title
Human intestinal epithelial cells swell and demonstrate actin rearrangement in response to the metalloprotease toxin of Bacteroides fragilis.
Journal
Reference
Authors
Kling JJ, Wright RL, Moncrief JS, Wilkins TD
Title
Cloning and characterization of the gene for the metalloprotease enterotoxin of Bacteroides fragilis.
Journal
Sequence
Other DBs
ExPASy - ENZYME nomenclature database: 3.4.24.74