Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-methyl-D-aspartate receptor NR2A subunit | Homo sapiens | plasmin cleaves the native NR2A amino-terminal domain, removing the functional high affinity Zn2+ binding site. Plasmin also cleaves recombinant NR2A amino-terminal domain at lysine 317, thereby producing a 40 kDa fragment, consistent with plasmin-induced NR2A cleavage fragmentsobserved in rat brain preparations. Zn2+ inhibition of agonist-evoked N-methyl-D-aspartate receptor currents of NR1/NR2A-transfected HEK 293 cells and cultured cortical neurons is significantly reduced by plasmin treatment. Mutating the plasmin cleavage site Lys317 on NR2A to alanine blocks plasmins effect on Zn2+ inhibition | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-methyl-D-aspartate receptor NR2A subunit | plasmin cleaves the native NR2A amino-terminal domain, removing the functional high affinity Zn2+ binding site. Plasmin also cleaves recombinant NR2A amino-terminal domain at lysine 317, thereby producing a 40 kDa fragment, consistent with plasmin-induced NR2A cleavage fragmentsobserved in rat brain preparations. Zn2+ inhibition of agonist-evoked N-methyl-D-aspartate receptor currents of NR1/NR2A-transfected HEK 293 cells and cultured cortical neurons is significantly reduced by plasmin treatment. Mutating the plasmin cleavage site Lys317 on NR2A to alanine blocks plasmins effect on Zn2+ inhibition | Homo sapiens | ? | - |
? |