Sandbox Reserved 1670: Difference between revisions
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== Function of your protein == | == Function of your protein == | ||
This protein can be found in the plant pathogenic microbe Pseudomonas syringae strain PtoDC3000. The p. syringae mutautes its host, which in this case is tomato. The p. syringae produces a toxin that cause the tomato to not be able to fight off, there for causing diseases in the tomato. The research focuses on aldehyde dehydrogenases specifically aldC. aldehyde dehydrogenases are known for its capability to detoxing aldehydes, this is important because aldehydes are very reactive, so for an example from the article they can be turned into carboxylic acids which are not as reactive, which I believe slows down the mutation. The substrate of the AldC PtoDC3000 shows that this enzyme functions as a long-chain aliphatic aldehyde dehydrogenase. This article states that they ran tests to find the best substrate for this enzyme, which they found multiple substrate such as aliphatic aldehydes of 5–9-carbon length, as well as hydrocinnamaldehyde and 4-pyridinecarboxyaldehyde but it shows that octanal has the highest activity. | This protein can be found in the plant pathogenic microbe Pseudomonas syringae strain PtoDC3000. The p. syringae mutautes its host, which in this case is tomato. The p. syringae produces a toxin that cause the tomato to not be able to fight off, there for causing diseases in the tomato. The research focuses on aldehyde dehydrogenases specifically aldC. aldehyde dehydrogenases are known for its capability to detoxing aldehydes, this is important because aldehydes are very reactive, so for an example from the article they can be turned into carboxylic acids which are not as reactive, which I believe slows down the mutation. The substrate of the AldC PtoDC3000 shows that this enzyme functions as a long-chain aliphatic aldehyde dehydrogenase. This article states that they ran tests to find the best substrate for this enzyme, which they found multiple substrate such as aliphatic aldehydes of 5–9-carbon length, as well as hydrocinnamaldehyde and 4-pyridinecarboxyaldehyde but it shows that octanal has the highest activity. | ||
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4 catalytic amino acids known as the <scene name='87/873232/Catalytic_residues/4'>Catalytic Tetrad</scene> consisting of Asn159, Glu257, Gly288, and Cys291. Cys291 can be found to be mutated to an Ala <scene name='87/873232/Mutated_catalytic_tetrad/3'>Mutated Catalytic Tetrad</scene> | 4 catalytic amino acids known as the <scene name='87/873232/Catalytic_residues/4'>Catalytic Tetrad</scene> consisting of Asn159, Glu257, Gly288, and Cys291. Cys291 can be found to be mutated to an Ala <scene name='87/873232/Mutated_catalytic_tetrad/3'>Mutated Catalytic Tetrad</scene> | ||
There are two ligands in each of the chains in the homodimer <scene name='87/873232/Ligands/2'>NAD and Octanal</scene> | |||
The mutation of C291A can be found in the middle of the two ligands affecting the binding efficiency of the structure. | |||
