Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.3.15 extracted from

  • Tarcsa, E.; Marekov, L.N.; Mei, G.; Melino, G.; Lee, S.C.; Steinert, P.M.
    Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin (1996), J. Biol. Chem., 271, 30709-30716.
    View publication on PubMed
Search for more literature for 3.5.3.15

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle skeletal muscle Oryctolagus cuniculus
-

Substrates and Products (Substrate)

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
-
 ?