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Function of your protein

The enzyme is from a tomato plant. Ald-C is an aldehyde dehydrogenase which are known to preform many biological functions. This enzyme also functions as a long-chain aliphatic aldehyde dehydrogenase. It can detoxify highly reactive compounds such as aldehydes. In a plant they also help with cell wall ester biogenesis, and help plant when they feel "stress" such as dehydration or environmental changes. Ald-c is also linked to many biochemical processes such as ethanol metabolism by oxidation of acetyl aldehyde into acetate (removing aldehyde), and polyamine metabolism. On the other hand, AldC has also been linked to the synthesis of indol-3-acetic acid which is the primary plant hormone for P.Syringae.

Biological relevance and broader implications

The Pseudomonas syringae plant pathogen effects crops, it is relevant because farmers and people that work in the agriculture industry need to know of all the ways that their crops can get infected. Pseudomonas syringae makes the plants defenses against pathogens weak and it is more susceptible to get sick, by producing many different virulence factors such as parahormones, which are chemicals that are similar to the plants natural hormones but are not. Pseudomonas syringae can destroy many different plants in different environments and temperatures, it can also survive and spread through the leaves. IAA (Indole-3-Acetic Acid) is a main plant hormone that is produced in the apical bud of and young leaves of plants and is known to be an inducer of cell division and elongation. IAA is often used in horticulture to promote adventitious root growth and are used commercially to create root stem cuttings and to promote uniform fruit and flowering growth

This research is relevant to more areas in science because if someone want to make a defense chemical for Pseudomonas syringae they can use the chemistry in this paper to do so. There is a lost of valuable information that shows the chemistry, such as binding affinity. If someone is thinking about making a cure against Pseudomonas syringae they will need to know the characteristics of all the things that will bind well to it. This research paper also is useful in identifying superfamilies among different plant pathogens.

Important amino acids

There are which are essential for catalyzing the reactions and if one of them is mutated it can cause a huge effect in any enzyme. They are the ones that can preform acid base chemistry and catalyze the reaction which help it to make reactions happen appropriately. there are which are NAD and OYA (octantal). Cystine is an important amino acid but it was mutated to an alanine, which has possibly prevented the formation of a disulfide bridge.

The mutation was caused in the 291 position which is also one go the 4 catalytic residues. It was mutated to an alanine.

there are also other residues that are important for NAD binding.

Structural highlights

The octantal was the best substrate with the lowest Km and the highest affinity out of all 23 substrates. Ald-C is also a homodimer. The central beta sheets are surrounded by alpha helices to form the NAD(H) binding site. The C terminal region has a mixture of both alpha and betta domain, which includes the catalytic cysteine residue and forms the aldehyde – binding site.Due to the mutated cystine to an alanine there may have been a disturbance in a potential disulfides bridge that happens between 2 cysteines and are essential for stability (). In this space fill scene you can see where the hydrogen bonds are. For the of Ald-C the alpha helices and beta sheets are shown

Other important features

Alanine substitutions of Glu 257 and Glu 391 severely disrupted AldC activity, showing that alanine had serious effects on other amino acids found along Ald-C. In contrast to the NAD(H)-binding site, apolar interactions dominate the octanal binding in the substrate- binding pocket.

A cluster of aromatic residues and two apolar residues provide the hydrophobic environment that accommodates octanal and other aliphatic aldehydes. As described for other aldehyde dehydrogenase, the substrate-binding site forms an  for adaptable apolar ligand interaction.

two apolar residues provide the hydrophobic environment that accommodates octanal and other aliphatic alde- hydes.