Sandbox Reserved 1096: Difference between revisions

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==='''Catalysis of deimination'''===

PAD2 is a calcium-dependent enzyme which catalyzes the deimination of [https://en.wikipedia.org/wiki/Arginine Arginine] residues. This reaction occurs only if calcium ions bind to specific sites of PAD2 but they do not directly participate in catalysis : they act as cofactors. Once Calcium bonding is accomplished, a '''''catalytic cysteine residue in position 647''''' in the peptide chain changes its position to carry out a [https://en.wikipedia.org/wiki/Nucleophilic_substitution nucleophilic attack] on guanidium groups of arginine residues. In terms of specific catalysis at the active site of PAD2, four residues are essential for the progress of citrullination: D351, H471, D473 and C647<ref name="ART1" /><ref name="ARTC">DOI:10.1007/s00214-012-1293-9</ref>. These arginine residues that are substrates in this reaction can bind to PAD2 because calcium binding engenders a move out of the active site for an arginin in position 347 and a move in for a tryptophan in position 348, in order to form a pocket for the substrate<ref name="ART1" />.

PAD2 is a calcium-dependent enzyme which catalyzes the deimination of [https://en.wikipedia.org/wiki/Arginine Arginine] residues. This reaction occurs only if calcium ions bind to specific sites of PAD2 but they do not directly participate in catalysis : they act as cofactors. Once Calcium bonding is accomplished, a '''''catalytic cysteine residue in position 647''''' in the peptide chain changes its position to carry out a [https://en.wikipedia.org/wiki/Nucleophilic_substitution nucleophilic attack] on guanidium groups of arginine residues. In terms of specific catalysis at the active site of PAD2, four residues are essential for the progress of citrullination: D351, H471, D473 and C647<ref name="ART1" /><ref name="ARTC">McCoy, R.S., Braun-Sand, S.B. Semimicroscopic investigation of active site pK a values in peptidylarginine deiminase 4. Theor Chem Acc 131, 1293 (2012) [https://doi.org/10.1007/s00214-012-1293-9 DOI:10.1007/s00214-012-1293-9]</ref>. These arginine residues that are substrates in this reaction can bind to PAD2 because calcium binding engenders a move out of the active site for an arginin in position 347 and a move in for a tryptophan in position 348, in order to form a pocket for the substrate<ref name="ART1" />.

== Citrullination of Arginine residues ==

Sandbox Reserved 1096: Difference between revisions

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@@ Line 22: / Line 22: @@
 ==='''Catalysis of deimination'''===
-PAD2 is a calcium-dependent enzyme which catalyzes the deimination of [https://en.wikipedia.org/wiki/Arginine Arginine] residues. This reaction occurs only if calcium ions bind to specific sites of PAD2 but they do not directly participate in catalysis : they act as cofactors. Once Calcium bonding is accomplished, a '''''catalytic cysteine residue in position 647''''' in the peptide chain changes its position to carry out a [https://en.wikipedia.org/wiki/Nucleophilic_substitution nucleophilic attack] on guanidium groups of arginine residues. In terms of specific catalysis at the active site of PAD2, four residues are essential for the progress of citrullination: D351, H471, D473 and C647<ref name="ART1" /><ref name="ARTC">DOI:10.1007/s00214-012-1293-9</ref>.  These arginine residues that are substrates in this reaction can bind to PAD2 because calcium binding engenders a move out of the active site for an arginin in position 347 and a move in for a tryptophan in position 348, in order to form a pocket for the substrate<ref name="ART1" />.
+PAD2 is a calcium-dependent enzyme which catalyzes the deimination of [https://en.wikipedia.org/wiki/Arginine Arginine] residues. This reaction occurs only if calcium ions bind to specific sites of PAD2 but they do not directly participate in catalysis : they act as cofactors. Once Calcium bonding is accomplished, a '''''catalytic cysteine residue in position 647''''' in the peptide chain changes its position to carry out a [https://en.wikipedia.org/wiki/Nucleophilic_substitution nucleophilic attack] on guanidium groups of arginine residues. In terms of specific catalysis at the active site of PAD2, four residues are essential for the progress of citrullination: D351, H471, D473 and C647<ref name="ART1" /><ref name="ARTC">McCoy, R.S., Braun-Sand, S.B. Semimicroscopic investigation of active site pK a values in peptidylarginine deiminase 4. Theor Chem Acc 131, 1293 (2012) [https://doi.org/10.1007/s00214-012-1293-9 DOI:10.1007/s00214-012-1293-9]</ref>.  These arginine residues that are substrates in this reaction can bind to PAD2 because calcium binding engenders a move out of the active site for an arginin in position 347 and a move in for a tryptophan in position 348, in order to form a pocket for the substrate<ref name="ART1" />.
 == Citrullination of Arginine residues ==