Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
protein L-Arg + H2O | Oryctolagus cuniculus | the ureido group on the citrulline formed by the peptidylarginine deiminase modification functions to unfold proteins due to decrease in net charge, loss of potential ionic bonds, and interference with H bonds | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | skeletal muscle | Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
filaggrin + H2O | deimination of protein-bound Arg residues to citrulline, the substrate has little structural order, the reaction proceeds rapidly to about 95% completion und results in loss of the organized structure | Oryctolagus cuniculus | ? + NH3 | - |
? | |
protein L-Arg + H2O | the ureido group on the citrulline formed by the peptidylarginine deiminase modification functions to unfold proteins due to decrease in net charge, loss of potential ionic bonds, and interference with H bonds | Oryctolagus cuniculus | ? | - |
? | |
trichohyalin + H2O | deimination of protein-bound Arg residues to citrulline, the substrate has a highly alpha-helical structure, the reaction proceeds slowly to about 25% and can be forced to a maximum of about 65% | Oryctolagus cuniculus | ? + NH3 | - |
? |