EC Number   |
Reaction |
Reference |
|---|
   3.4.24.B17 | proteolytic degradation of proteins |
- |
- |
| 3.4.24.B17 | proteolytic degradation of proteins |
degenerate cleavage specificity, degradation of hydrophobic membrane-spanning segments of misfolded mitochodrial membrane proteins |
649814 |
| 3.4.24.B17 | proteolytic degradation of proteins |
degradation of membrane proteins |
652391 |
| 3.4.24.B17 | proteolytic degradation of proteins |
degradation of soluble and integral membrane proteins |
650082 |
| 3.4.24.B17 | proteolytic degradation of proteins |
enzyme is a AAA protease, highly conserved residues Phe228 and Gly230 lie in the central pore region of the hexamer and are important in proteolysis and coupling to ATP |
652491 |
| 3.4.24.B17 | proteolytic degradation of proteins |
essential for activity are residues Asn301, Asp307, Arg312, and Arg315, mechanism, ligand binding site at residues 144-398 |
653896 |
| 3.4.24.B17 | proteolytic degradation of proteins |
mechanism |
650184, 651704 |
| 3.4.24.B17 | proteolytic degradation of proteins |
mechanism, reaction only occurs with protein substrates of low intrinsic thermodynamic stability, sequential degradation from the tail |
653191 |
| 3.4.24.B17 | proteolytic degradation of proteins |
preference for positively charged and hydrophobic amino acid residues, large cytoplasmic domain contains ATPase and protease activities |
649856 |
| 3.4.24.B17 | proteolytic degradation of proteins |
soluble C-terminal domain harbors the ATPase and protease activity, the N-terminal domain permits the indispensible membrane integration of the enzyme, cleavage of small peptides from the C-terminal side of hydrophobic residues, overview |
-, 651768 |
