Choriolysin H
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.24 Metalloendopeptidases > 3.4.24.67 choriolysin H
Tentoxilysin is a zinc metalloendopeptidase produced by Clostridium tetani, the type example of peptidase family M27 (tentoxilysin family). The 150-kDa proenzyme is processed to disulfide-linked 100- and 50-kDa subunits, the latter carrying the endopeptidase activity; it is weakly inhibited by captopril and phosphoramidon. It hydrolyzes the -Gln76-/-Phe- bond in synaptobrevin (VAMP), disabling neuroexocytosis. Acting at spinal inhibitory interneurons, it blocks inhibitory neurotransmitter release and causes spastic paralysis; clostridial neurotoxins are among the most toxic substances known. It features an M27-family zinc catalytic light chain bound to a ganglioside-binding heavy chain.
Tentoxilysin is a zinc metalloendopeptidase produced by Clostridium tetani, the type example of peptidase family M27 (tentoxilysin family). The 150-kDa proenzyme is processed to disulfide-linked 100- and 50-kDa subunits, the latter carrying the endopeptidase activity; it is weakly inhibited by captopril and phosphoramidon. It hydrolyzes the -Gln76-/-Phe- bond in synaptobrevin (VAMP), disabling neuroexocytosis. Acting at spinal inhibitory interneurons, it blocks inhibitory neurotransmitter release and causes spastic paralysis; clostridial neurotoxins are among the most toxic substances known. It features an M27-family zinc catalytic light chain bound to a ganglioside-binding heavy chain.
References:
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