User:Jeremy Jovellanos
From Proteopedia
Abstract
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By facilitating the addition of double bonds at the expense of two hydrogen atoms, desaturase enzymes have proven to be significant in fatty acid functionality and diversification. Manipulating desaturases by filling in the active site would allow the position at which double bonds are formed on saturated fatty acids to be changed. As a result, the functionality of the unsaturated fatty acid product can be improved. Modifying the desaturase can also change the enzyme’s specificity to its substrate allowing it to bind a wider variety of fatty acid chain lengths. A desaturase that can bind to several fatty acids with different chain lengths would be more useful commercially. Through the use of Rasmol, a 3-D molecular visualization software, fatty acid 225 of the castor desaturase is modeled with its di-iron active site with its six ligands and an 18:0 fatty acid substrate. The di-iron active site is represented as orange in color embedded within a core helical bundle labeled light blue while the non-helical shown in white. Positioned adjacent to this di-iron active site, the 18:0 fatty acid substrate is designated in gray. There are six ligands in the active site surrounding the substrate and di-iron center (two histidines-His146 and His232, and four glutamic acids- Glu105, Glu143, Glu196, and Glu229). These amino acid residues help coordinate the active site and the correct positioning of the ligands are important for the reactivity of the di-iron center. His146, His232, Glu105, Glu143, Glu196, and Glu229 are all in the CPK color scheme. If manipulated successfully, this enzyme may be able to bind a 16:0 or a 14:0 fatty acid substrate rather than the just the normal 18:0, as well as place the double bond between two carbons other than the 9 and 10 carbons. This research on castor desaturase can use genetically altered plants with modified desaturase enzymes to serve as “green-factories” which can produce specific renewable resources as well as bioenergy sources. Consequently, this may help to meet the world’s rising demands on natural resources.
I am a 3rd year undergraduate student at Stony Brook University pursuing a bachelor of science degree in Biology with a concentration in Neuroscience and minor in Spanish Language and Literature. To become further involved in the scientific community and gain research experience in biological sciences, I am currently enrolled (Fall 2009) in the course BIO 487 - Research in Molecular Cellular and Developmental Biology. Under the supervision of Dr. Marvin O'Neal and Dr. Gisselle Medina, the primary focus of "P.R.E.P.A.R.E" (Protein Explorations in Preparation for Authentic Research Experiences)is to construct physical models of proteins while keeping in mind structure and function.
