A widely-used, very stable one of these enzymes was extracted from the fungus Engyodontium album; that one is inactivated at 65 C for 10 minutes and is designated by the letter "K".
A widely-used, very stable one of these enzymes was extracted from the fungus Engyodontium album; that one is inactivated at 65 C for 10 minutes and is designated by the letter "K". Research-grade formulations of another one of these enzymes are made stable by reductive methylation and treated with TPCK to increase specificity; that example of these enzymes is commonly used "in-gel" before a tandem mass spec and to detach adherent cells.  AEBSF, PLAAC and PMSF are commonly used to inhibit these enzymes. One class of these proteins stabilizes its tetrahedral intermediate using an oxyanion hole and holds its (*) substrate using a hydrophobic specificity pocket. In that enzyme's mechanism a proton shuttle containing Asp102 and His57 deprotonates Ser195, which nucleophilically attacks a substrate carbonyl.. That catalytic triad is in the active site of chymotrypsin. For 10 points, name these enzymes that break down proteins.
A widely-used, very stable one of these enzymes was extracted from the fungus Engyodontium album; that one is inactivated at 65 C for 10 minutes and is designated by the letter "K".
proteases [or proteinases or peptidases, accept "cysteine proteases" or "serine proteases" or "aspartyl proteases"; accept "trypsin"]