EC Number |
Cofactor |
Reference |
---|
3.4.21.53 | ADP |
results in 72% activity with substrate alpha-casein, and 64% with peptide substrate glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide compared to ATP in presence of Mg2+ |
752612 |
3.4.21.53 | AMPPNP |
5'-adenylyl imidodiphosphate, results in 80% activity with substrate alpha-casein, and 92% with peptide substrate glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide compared to ATP in presence of Mg2+ |
752612 |
3.4.21.53 | AMPPNP |
adenylylimidodiphosphate, is not as effective as ATP, slight activation |
755563 |
3.4.21.53 | ATP |
- |
29357, 29362, 29363, 29364, 650090, 651853, 651889, 677574, 677704, 677854, 678789, 678943, 680501, 680779, 681850, 681937, 682726, 754600, 755340, 755478 |
3.4.21.53 | ATP |
a ofmitochondrial ATP-dependent protease |
732470 |
3.4.21.53 | ATP |
activates |
755563 |
3.4.21.53 | ATP |
activates, the ATP-binding site is situated at the interface between the alpha/beta-subdomain and the alpha-subdomain. Motifs for ATP hydrolysis and nucleotide sensing are well conserved at the interface. Structure, detailed overview |
754406 |
3.4.21.53 | ATP |
activation only in the presence of Mg2+ |
29339, 29340, 29341, 29342, 29343 |
3.4.21.53 | ATP |
ADP bound to the ATPase region stabilizes the enzyme |
731835 |
3.4.21.53 | ATP |
ADP remains on the enzyme |
29350 |