Sandbox Reserved 1475: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 40: | Line 40: | ||
In [[Figure 5]] it is visible to see that acetaldehyde and benzaldehyde both have really high Km values, 645uM and 305uM respectfully, and relatively low Vmax values, 139nmol/min/mg and 200nmol/min/mg respectfully. Octantal and decanal both have really low Km values, 5uM and 3uM respectfully, and relatively high Vmax values, 152nmol/min/mg and 214nmol/min/mg respectfully. Acetaldehyde and benzaldehyde are both short chained aldehydes compared to octantal and decanal aldehydes. It is easier to compare the ratio of Vmax/Km. An energetically favorable substrate would display a ratio of Vmax/Km that has a large magnitude. As seen in [[Figure 5]], both the long chained octantal and decanal aldehydes had large Vmax/Km values, 152 AND 214 respectfully. The substrate that RalDH2 uses to actually convert Vitamin A (Retinol) to retinoic acid is retinal in its "all-trans" form. As seen in [[Figure 5]] the Km value for the this substrate is the smallest out all that were tested, and the Vmax values was comparatively high. The Vmax/Km was also pretty large at a value of 49± 6. | In [[Figure 5]] it is visible to see that acetaldehyde and benzaldehyde both have really high Km values, 645uM and 305uM respectfully, and relatively low Vmax values, 139nmol/min/mg and 200nmol/min/mg respectfully.<ref name="Km value chart">Wang, Xianshu. Penzes, Peter., Napoli, Joseph L., Cloning of a cDNA Encoding an Aldehyde Dehydrogenase and Its Expression in ''Escherichia coli'' RECOGNITION OF RETINAL AS SUBSTRATE. J. Biol. Chem. (1996) 271:16288-16293. doi:10.1074/jbc.271.27.16288 </ref> Octantal and decanal both have really low Km values, 5uM and 3uM respectfully, and relatively high Vmax values, 152nmol/min/mg and 214nmol/min/mg respectfully.<ref name="Km value chart" /> Acetaldehyde and benzaldehyde are both short chained aldehydes compared to octantal and decanal aldehydes. It is easier to compare the ratio of Vmax/Km. An energetically favorable substrate would display a ratio of Vmax/Km that has a large magnitude. As seen in [[Figure 5]], both the long chained octantal and decanal aldehydes had large Vmax/Km values, 152 AND 214 respectfully.<ref name="Km value chart" /> The substrate that RalDH2 uses to actually convert Vitamin A (Retinol) to retinoic acid is retinal in its "all-trans" form. As seen in [[Figure 5]] the Km value for the this substrate is the smallest out all that were tested, and the Vmax values was comparatively high. The Vmax/Km was also pretty large at a value of 49± 6.<ref name="Km value chart" /> | ||
== Disease == | == Disease == | ||