AI Article Synopsis
- The study analyzed the aminopeptidase activities of snake venoms from multiple species, finding that all tested venoms contained aminopeptidase A (APA) and related enzymes.
- The venom from Gloydius blomhoffi brevicaudus displayed the strongest APA activity, which had similar characteristics to mammalian enzymes, including its sensitivity to metallopeptidase inhibitors.
- Molecular cloning revealed that the identified APA from G. blomhoffi brevicaudus is a type II integral membrane protein, closely related to mammalian APAs, marking its first documented structure in reptiles.
Article Abstract
The aminopeptidase activities of snake venoms from Gloydius blomhoffi brevicaudus, Gloydius halys blomhoffii, Trimeresurus flavoviridis, Bothrops jararaca and Crotalus atrox were investigated. Aminopeptidase A (APA), aminopeptidase B and aminopeptidase N activities were present in all snake venoms. The strongest APA activity was found in venom from G. blomhoffi brevicaudus. The susceptibility to metallopeptidase inhibitors and the pH optimum of the partially purified enzyme from G. blomhoffi brevicaudus venom were similar to those of known APAs from mammals. A G. blomhoffi brevicaudus venom gland cDNA library was screened to isolate cDNA clones using probes based on highly conserved amino acid sequences in known APAs. Molecular cloning of APA from G. blomhoffi brevicaudus venom predicted that it was a type II integral membrane protein containing 958 amino acid residues with 17 potential N-linked glycosylation sites. It possessed a His-Glu-Xaa-Xaa-His-(Xaa)(18)-Glu zinc binding motif that allowed the classification of this protein as a member of the M1 family of zinc-metallopeptidases, or gluzincins. The deduced amino acid sequence shows approximately 60% sequence identity to mammalian APA sequences. This is the first study to report the primary structure of APA from a reptile.
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| http://dx.doi.org/10.1016/j.toxicon.2007.02.012 | DOI Listing |
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Article Synopsis
- The study analyzed the aminopeptidase activities of snake venoms from multiple species, finding that all tested venoms contained aminopeptidase A (APA) and related enzymes.
- The venom from Gloydius blomhoffi brevicaudus displayed the strongest APA activity, which had similar characteristics to mammalian enzymes, including its sensitivity to metallopeptidase inhibitors.
- Molecular cloning revealed that the identified APA from G. blomhoffi brevicaudus is a type II integral membrane protein, closely related to mammalian APAs, marking its first documented structure in reptiles.
Characterization and cDNA cloning of dipeptidyl peptidase IV from the venom of Gloydius blomhoffi brevicaudus.
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Dipeptidyl peptidase activity was investigated in snake venoms from Gloydius blomhoffi brevicaudus, Gloydius halys blomhoffii, Trimeresurus flavoviridis and Crotalus atrox. The strongest dipeptidyl peptidase IV (DPP IV) activity was found in venom from G. blomhoffi brevicaudus.
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