Site-directed Blog Posting

If you're wondering why I haven't been posting....you can see below for why. I will get to writing new posts and stuff soon, I promise. (Below is the abstract for "Site-Directed Mutagenesis of His392 with Non-Canonical Amino Acids To Analyze The Structure and Activity of Escherichia Coli HPII Catalase’s Heme Active Site," which I am writing for a class.)

A site-directed mutagenesis investigating the structure and activity of HPII catalase was performed. Two distinct varieties of HPII catalase were made by incorporating aminophenylalanine and O-methyl-L tyrosine respectively at site 392. The oxygen generation rate was measured as a function of initial hydrogen peroxide concentration for wildtype catalase and translated into catalytic constants using Michaelis-Menten kinetics. The catalytic constant  was 6.25 s^-1 whereas the Michaelis-Menten constant  was 28.7 mM, which displays strong disagreement with literature values (  and   = 100800 s^-1).  Though these results appear inconsistent with literature, they may still provide valuable insight into the relative change in activity observed with the mutant catalase (OMT392 and AF392). Experimental conclusions that answer our hypothesis cannot yet be made due to inconclusive results.