Sandbox Reserved 1096: Difference between revisions
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== Citrullination of Arginine residues == | == Citrullination of Arginine residues == | ||
In humans, PAD2 is involved in a type of post-translational modification called citrullination. Indeed, this calcium-dependent enzyme catalyzes a deimination reaction : PAD2 uses one molecule of water to replace the terminal nitrogen of Arginine by an oxygen and a ketone group is formed in place of a ketimine one <ref name="ART1" />. | In humans, PAD2 is involved in a type of post-translational modification called citrullination. Indeed, this calcium-dependent enzyme catalyzes a deimination reaction : PAD2 uses one molecule of water to replace the terminal nitrogen of Arginine by an oxygen and a ketone group is formed in place of a ketimine one <ref name="ART1" />. | ||
[[Image:Citrullination.png|300px|left|thumb| Deimination of Arginine into Citrulline]] | |||
The transformation of arginyl residues ([https://fr.wikipedia.org/wiki/Arginine Arginine]), which are positively charged at a neutral pH, into citrullyl residues, which are neutral, leads to the '''''modification of the global charge''''' of the targeted protein. These residue modifications are the result of hydrolysation of guanidinium groups in side chains whose catalysis has been explained previously. As a result, the deimination reaction catalyzed by PAD2 may produce '''''important conformational changes''''' in proteins by increasing the hydrophobicity. | The transformation of arginyl residues ([https://fr.wikipedia.org/wiki/Arginine Arginine]), which are positively charged at a neutral pH, into citrullyl residues, which are neutral, leads to the '''''modification of the global charge''''' of the targeted protein. These residue modifications are the result of hydrolysation of guanidinium groups in side chains whose catalysis has been explained previously. As a result, the deimination reaction catalyzed by PAD2 may produce '''''important conformational changes''''' in proteins by increasing the hydrophobicity. | ||
