Choline Oxidase
AbstractAbstract
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Choline oxidase is the enzyme that catalyzes the reaction between choline and betaine glycine. Betaine glycine is an osmoprotectant and instrumental in helping plants and bacteria survive dry conditions. Studying the choline oxidase may help in the development of controlling populations of beneficial plants or pathogenic bacteria. The data was analyzed using the BLAST and Rasmol programs. The structure of choline oxidase from Arthrobacter globiformis (bacteria) was compared with the structure of the complimentary protein in Mus musculus (mice), carnitine acetyltransferase (Altschul et al., 2005). There are seven amino acids evolutionarily preserved within the vicinity of the flavin group (between amino acids 460 to 483 of each subunit). Of these seven, three are within 9 Å of the flavin group while the other four are farther away. These three are threonine 463, valine 464, and histadine 466. They are colored blue and are connected with the ligand via white monitor lines. The other four conserved residues are colored cyan, but are too far to really interact with the flavin group (colored cpk). Beta sheets are colored yellow to showcase the secondary structure of the entire subunit. Evolutionary preservation of the Thr463, may signify an importance in aiding the function of the flavin group as it relates to the activity of the enzyme. Previous studies indicate that His466 is indeed important in the function of choline oxidase (Quaye, Lountos, Fan, Orville, & Gadda, 2008).
Works CitedWorks Cited
Altschul SF, Wootton JC, Gertz EM, Agarwala R, Morgulis A, Schäffer AA, and Yu YK (2005). Protein database searches using compositionally adjusted substitution matrices. FEBS J. 272, 5101-5109.
Quaye, O., Lountos, G., Fan, F., Orville, A., & Gadda, G. (2008). Role of Glu312 in Binding and Positioning of the Substrate for the Hydride. Biochemistry , 47, 243-256.