Sandbox Reserved 1677
From Proteopedia
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== Function of your protein == | == Function of your protein == | ||
- | Aldehyde dehydrogenase serves as a metabolic housekeeping enzyme due to its ability to detoxify aldehydes, which are highly reactive compounds generated through cellular. It can also scavenge aldehyde from lipid peroxidation and convert them to a less chemically reactive carboxylic acid. Aldc additionally plays an important role in ethanol metabolism via oxidation of acetaldehyde into acetate, metabolism of polyamine, and plant cell wall ester biogenesis. After testing different types of Aldehyde substrates, it turns out that the 8 carbon carbon substrate is the preferred aliphatic aldehyde substrate in this case Octanal, which is surrounded by aromatic rings. Octanal has the lowest Km and highest Vmax values. as you can be by the really amazing ligand that is bound to it. | + | <scene name='87/873239/Image_of_ligand/1'>Aldehyde dehydrogenase</scene> serves as a metabolic housekeeping enzyme due to its ability to detoxify aldehydes, which are highly reactive compounds generated through cellular. It can also scavenge aldehyde from lipid peroxidation and convert them to a less chemically reactive carboxylic acid. Aldc additionally plays an important role in ethanol metabolism via oxidation of acetaldehyde into acetate, metabolism of polyamine, and plant cell wall ester biogenesis. After testing different types of Aldehyde substrates, it turns out that the 8 carbon carbon substrate is the preferred aliphatic aldehyde substrate in this case Octanal, which is surrounded by aromatic rings. Octanal has the lowest Km and highest Vmax values. as you can be by the really amazing ligand that is bound to it. |
Revision as of 20:53, 18 April 2021
This Sandbox is Reserved from 01/25/2021 through 04/30/2021 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1665 through Sandbox Reserved 1682. |
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644