User:Sharwat Jahan/Sandbox1 Desaturase
From Proteopedia
(New page: == Abstract == 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 diversifi...) |
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| - | == Abstract == | + | <applet load='2put' size='300' frame='true' align='right' caption='Insert caption here' />== Abstract == |
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 diiron active site with its six ligands and an 18:0 fatty acid substrate. The diiron active site is represented as orange in color embedded within a core 4-helix bundle labeled light blue within a hydrophobic cavity. Non-helical portions of the helical bundle are shown in white. Positioned adjacent to this diiron active site, the 18:0 fatty acid substrate is designated in CPK color scheme. There are six ligands in the active site surrounding the substrate and diiron center: two histidines – His146 and His232, and four glutamic acids – Glu105, Glu143, Glu196, and Glu229. These amino acid residues (indicated in CPK color scheme) help coordinate the active site and the correct positioning of the ligands are important for the reactivity of the diiron center. Two monitor lines connect the two iron (Fe) ions to Glu229 and Glu143 where these two residues bridge the two Fe ions. Each glutamic acid interacts with both irons. Although there are other ligand interactions that coordinate the diiron active site, this particular model focuses only on the two glutamic acid residues. 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. | 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 diiron active site with its six ligands and an 18:0 fatty acid substrate. The diiron active site is represented as orange in color embedded within a core 4-helix bundle labeled light blue within a hydrophobic cavity. Non-helical portions of the helical bundle are shown in white. Positioned adjacent to this diiron active site, the 18:0 fatty acid substrate is designated in CPK color scheme. There are six ligands in the active site surrounding the substrate and diiron center: two histidines – His146 and His232, and four glutamic acids – Glu105, Glu143, Glu196, and Glu229. These amino acid residues (indicated in CPK color scheme) help coordinate the active site and the correct positioning of the ligands are important for the reactivity of the diiron center. Two monitor lines connect the two iron (Fe) ions to Glu229 and Glu143 where these two residues bridge the two Fe ions. Each glutamic acid interacts with both irons. Although there are other ligand interactions that coordinate the diiron active site, this particular model focuses only on the two glutamic acid residues. 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. | ||
Revision as of 00:46, 1 December 2009
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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 diiron active site with its six ligands and an 18:0 fatty acid substrate. The diiron active site is represented as orange in color embedded within a core 4-helix bundle labeled light blue within a hydrophobic cavity. Non-helical portions of the helical bundle are shown in white. Positioned adjacent to this diiron active site, the 18:0 fatty acid substrate is designated in CPK color scheme. There are six ligands in the active site surrounding the substrate and diiron center: two histidines – His146 and His232, and four glutamic acids – Glu105, Glu143, Glu196, and Glu229. These amino acid residues (indicated in CPK color scheme) help coordinate the active site and the correct positioning of the ligands are important for the reactivity of the diiron center. Two monitor lines connect the two iron (Fe) ions to Glu229 and Glu143 where these two residues bridge the two Fe ions. Each glutamic acid interacts with both irons. Although there are other ligand interactions that coordinate the diiron active site, this particular model focuses only on the two glutamic acid residues. 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.
