Final answer:
In rattlesnake venom, enzymes such as phospholipase A2, metalloproteases, and serine proteases, along with three-finger toxins, would be most sensitive to proteases due to their protein structures that can be targeted and broken down.
Step-by-step explanation:
Rattlesnake venom contains a collection of different enzymes that are sensitive to proteases. Proteases, being protein-digesting enzymes, can degrade various proteins and peptides, which are found in the venom. For instance, the venom of cottonmouth snakes is mainly composed of protein families that include phospholipase A2 (PLA2), metalloproteases (SVMP), and serine proteases (SVSP). PLA2s lead to inflammation and pain, SVMPs cause hemorrhage, and SVSPs affect blood coagulation. As proteases target specific amino acids or have metal ions in their active site, they can break down these venom components. There are also neurotoxins like those from the eastern coral snake that would also be sensitive to certain protease activities. However, when considering overall sensitivity to proteases, the three-finger toxins (3FTx), which are a family of proteins including neurotoxins that attack nerve tissues, are particularly vulnerable due to their proteinaceous nature and specific cleavage sites for proteases.