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Function of your protein

serve as a metabolic housekeeping enzyme due to their ability to detoxify aldehydes, which are highly reactive compounds generated through cellular. They can also scavenge aldehyde from lipid peroxidation and convert them to a less chemically reactive carboxylic acid. Aldc additionally play an important role in ethanol metabolism via oxidation of acetaldehyde into acetate, metabolism of polyamine, and plant cell wall ester biogenesis. The bacterial pathogen Pseudomonas syringae is the organism that is causing mutation in the host. It turns out that 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 and NAD+ is the cofactor.

Biological relevance and broader implications

The bacterial pathogen peudomanas syringae is used as a model for understanding microbial evolution, how host and pathogens interact and bacterial virulence mechanisms. P.syringae utilizes several strategies to manipulate hormone signaling in its host plants. These interactions help agriculturalists to detect diseases in plants and how to protect crops from being invaded by these harmful pathogens. In order to suppress host defenses and promote disease development, P. syringae produces a wide variety of virulence factors including auxin Indole-3-acetic acid (IAA) synthesis, whose production is implicated in pathogen virulence. PtoDC3000 synthesizes IAA using an uncharacterized pathway that requires indole-3-acetaldehyde dehydrogenase.

Important amino acids

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.

There are  in AldC.  Asn 159, Glu 257, Gly 288, Cys 291

(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 ==

, add more details here

Structural highlights

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.

New cartoon View: tertiary/ Quaternary features

shows how amino acids interacts with one another inside the protein.

Other important features

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