Sandbox Reserved 895: Difference between revisions

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According to SCOP, the bovine RPE65 (PDB: ''4RSC'', SCOP: ''8051041''), belongs in the domain 8051041, the family 4007172 corresponding to retinoid isomerase RPE65-like, the superfamily 3002594 corresponding to RPE65-like, the fold 2001013 corresponding to 7-bladed beta-propeller and the class 100001 corresponding to all beta proteins. <ref> SCOP Databank 14 Apr 2020 Available from: http://scop.mrc-lmb.cam.ac.uk/term/8051041 </ref>

Using sequence homology, RPE65 belong to a family of proteins known as carotenoid cleavage oxygenase (CCO) enzymes. This class of enzymes often cleave β-carotene or apocarotenoids. However, what makes RPE65 unique ~~form~~ all the other enzymes in this family is that RPE65 catalyzes an ~~isomerhydrolase~~ reaction. Additionally, unlike the other enzymes in the CCO family, there is no obvious role for molecular oxygen in the RPE65 enzymology. All members of the CCO family contain four conserved histidine residues (His180, His241, His313 and His527) that bind to an ion (Fe2+) cofactor. <ref> DOI 19805034 </ref> <ref> DOI 10.1016/j.bbadis.2018.04.014 </ref>

Using sequence homology, RPE65 belong to a family of proteins known as carotenoid cleavage oxygenase (CCO) enzymes. This class of enzymes often cleave β-carotene or apocarotenoids. However, what makes RPE65 unique from all the other enzymes in this family is that RPE65 catalyzes an isomerohydrolase reaction. Additionally, unlike the other enzymes in the CCO family, there is no obvious role for molecular oxygen in the RPE65 enzymology. All members of the CCO family contain four conserved histidine residues (His180, His241, His313 and His527) that bind to an ion (Fe2+) cofactor. <ref> DOI 19805034 </ref> <ref> DOI 10.1016/j.bbadis.2018.04.014 </ref>

RPE65 can exist as both soluble and membrane bound forms which can undergo post-translational modifications (PTMs). At ~~cystine~~ residues Cys231, Cys239 and Cys330 the enzyme can be S-palmitoylated. S-palmitoylation of RPE65 was speculated to increase the ratio of membrane-bound to soluble RPE65 which can increase the enzymatic activity. <ref> DOI 15186777 </ref> However other studies have challenged this hypothesis and as such palmitoylation of RPE65 require further research to determine the activity. <ref> DOI 17504753 </ref>

RPE65 can exist as both soluble and membrane bound forms which can undergo post-translational modifications (PTMs). At cysteine residues Cys231, Cys239 and Cys330 the enzyme can be S-palmitoylated. S-palmitoylation of RPE65 was speculated to increase the ratio of membrane-bound to soluble RPE65 which can increase the enzymatic activity. <ref> DOI 15186777 </ref> However other studies have challenged this hypothesis and as such palmitoylation of RPE65 require further research to determine the activity. <ref> DOI 17504753 </ref>

=== '''[1.2.2] Structural Analysis of RPE65''' ===

Sandbox Reserved 895: Difference between revisions

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 According to SCOP, the bovine RPE65 (PDB: ''4RSC'', SCOP: ''8051041''), belongs in the domain 8051041, the family 4007172 corresponding to retinoid isomerase RPE65-like, the superfamily 3002594 corresponding to RPE65-like, the fold 2001013 corresponding to 7-bladed beta-propeller and the class 100001 corresponding to all beta proteins. <ref> SCOP Databank 14 Apr 2020 Available from: http://scop.mrc-lmb.cam.ac.uk/term/8051041 </ref>
-Using sequence homology, RPE65 belong to a family of proteins known as carotenoid cleavage oxygenase (CCO) enzymes. This class of enzymes often cleave β-carotene or apocarotenoids. However, what makes RPE65 unique form all the other enzymes in this family is that RPE65 catalyzes an isomerhydrolase reaction. Additionally, unlike the other enzymes in the CCO family, there is no obvious role for molecular oxygen in the RPE65 enzymology. All members of the CCO family contain four conserved histidine residues (His180, His241, His313 and His527) that bind to an ion (Fe2+) cofactor. <ref> DOI 19805034 </ref> <ref> DOI 10.1016/j.bbadis.2018.04.014 </ref>
+Using sequence homology, RPE65 belong to a family of proteins known as carotenoid cleavage oxygenase (CCO) enzymes. This class of enzymes often cleave β-carotene or apocarotenoids. However, what makes RPE65 unique from all the other enzymes in this family is that RPE65 catalyzes an isomerohydrolase reaction. Additionally, unlike the other enzymes in the CCO family, there is no obvious role for molecular oxygen in the RPE65 enzymology. All members of the CCO family contain four conserved histidine residues (His180, His241, His313 and His527) that bind to an ion (Fe2+) cofactor. <ref> DOI 19805034 </ref> <ref> DOI 10.1016/j.bbadis.2018.04.014 </ref>
-RPE65 can exist as both soluble and membrane bound forms which can undergo post-translational modifications (PTMs). At cystine residues Cys231, Cys239 and Cys330 the enzyme can be S-palmitoylated. S-palmitoylation of RPE65 was speculated to increase the ratio of membrane-bound to soluble RPE65 which can increase the enzymatic activity. <ref> DOI 15186777  </ref> However other studies have challenged this hypothesis and as such palmitoylation of RPE65 require further research to determine the activity. <ref> DOI 17504753 </ref>
+RPE65 can exist as both soluble and membrane bound forms which can undergo post-translational modifications (PTMs). At cysteine residues Cys231, Cys239 and Cys330 the enzyme can be S-palmitoylated. S-palmitoylation of RPE65 was speculated to increase the ratio of membrane-bound to soluble RPE65 which can increase the enzymatic activity. <ref> DOI 15186777  </ref> However other studies have challenged this hypothesis and as such palmitoylation of RPE65 require further research to determine the activity. <ref> DOI 17504753 </ref>
 === '''[1.2.2] Structural Analysis of RPE65''' ===