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. | ||
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== Biological relevance and broader implications == | == Biological relevance and broader implications == | ||
Revision as of 22:05, 17 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
Function of your protein
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 .
Biological relevance and broader implications
In order to suppress host defenses and promote disease development, Pseudomonas syringae produces a wide variety of virulence factors which includes phytohormones, to manipulate hormone signaling in its host. P.syringae also synthesizes auxin Indole-3-acetic acid (IAA), whose production is implicated in pathogen virulence. Bioinformatic analysis of ptoDC3000 shows a set of aldehyde dehydrogenase sharing approximately 30-40% amino acid identity with each other.
Important amino acids
There are in AldC. Asn 159, Glu 257, Gly 288, Cys 291
19 NAD+ Residues (binding site)
Ile 155, Asn 159, Lys 182, Gly 219, Ile 233, Ser 236, Ala 239, leu 242, Glu 257, leu 258, Gly 259, Cys 291, Glu 391, Phe 393
Octanol Lingand (binding site)
Trp 160 Tyr 163, Trp 450, Phe 456, Tyr 458, met 114, leu 118
Structural highlights
Aldc's secondary structure has two domains, hydrophobic and hydrophilic regions. The N-terminus of Aldc contains a central beta sheet surrounded by alpha helices which forms the NAD(H)-binding site. Additionally, around the C-terminus there is a mixture of alpha and beta domains which the cysteine residue and forms the aldehyde binding site. A small three stranded beta sheet domain facilitates aligomerization. There is an interdomain linker region that connects the N and C terminal domains of Aldc.
Other important features
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. </StructureSection>
