Sandbox Reserved 1677
From Proteopedia
(Difference between revisions)
| Line 8: | Line 8: | ||
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. | 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. | ||
| - | |||
| - | == Biological relevance and broader implications == | ||
| - | |||
| - | == Important amino acids== | ||
| - | |||
| - | == Structural highlights == | ||
| - | |||
| - | == Other important features == | ||
| - | |||
| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
| - | |||
| - | </StructureSection> | ||
| - | == References == | ||
| - | <references/> | ||
| - | |||
| - | |||
| - | |||
| - | <scene name='87/873239/Cartoon_view/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 <scene name='87/873239/Protein_view_2/3'>really amazing ligand that is bound to it</scene>. | ||
== Biological relevance and broader implications == | == 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. | 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== | == Important amino acids== | ||
| - | <scene name='87/873239/4_catalytic_residue/1'>4 Catalytic residues</scene> | ||
There are <scene name='87/873239/4_catalytic_residue/1'>four catalytic amino acids</scene> in AldC. Asn 159, Glu 257, Gly 288, Cys 291 | There are <scene name='87/873239/4_catalytic_residue/1'>four catalytic amino acids</scene> in AldC. Asn 159, Glu 257, Gly 288, Cys 291 | ||
19 NAD+ Residues (binding site) | 19 NAD+ Residues (binding site) | ||
| Line 38: | Line 18: | ||
Octanol Lingand (binding site) | Octanol Lingand (binding site) | ||
Trp 160 Tyr 163, Trp 450, Phe 456, Tyr 458, met 114, leu 118 | Trp 160 Tyr 163, Trp 450, Phe 456, Tyr 458, met 114, leu 118 | ||
| - | |||
== Structural highlights == | == 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. | 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 == | == Other important features == | ||
| + | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
</StructureSection> | </StructureSection> | ||
| - | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 22:08, 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. |
To get started:
More help: Help:Editing |
Your Heading Here (maybe something like 'Structure')
| |||||||||||
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
