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Results 1 - 10 of 29 > >>
EC Number Metals/Ions Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.21Br- 2 mM, activation 137216
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.21Ca2+ activation 137216
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.21Ca2+ even a slight disruption of the Ca2+-binding site destabilizes the three-dimensional fold of glutamate carboxypeptidase II and is associated with impaired secretion, a high propensity to form nonphysiological oligomers, and an inability to bind active site-targeted ligands. Additionally, the Ca2+-binding site is critical for maintenance of the native homodimeric quaternary arrangement of GCPII, which is indispensable for its enzymatic activity 755336
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.21Ca2+ positively regulates enzyme expression 669595
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.21Cl- 2 mM, activation 137216
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.21Co2+ activation 137216
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.21Co2+ stimulates the metallopeptidase 669923
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.21F- 100 mM, 20% of the activity compared to Cl- 137216
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.21I- 2 mM, activation 137216
Display the word mapDisplay the reaction diagram Show all sequences 3.4.17.21K+ extracellularly applied K+ increases the enzyme activity in vivo in glial cells and the ventral nerve cord 669932
Results 1 - 10 of 29 > >>