EC Number   |
Natural Substrates |
|---|
   3.4.24.B17 | 3-deoxy-D-manno-octulosonate transferase + H2O |
3-deoxy-D-manno-octulosonate transferase carries out the attachment of two KDO residues to the lipid A precursor (lipid IVA) to form the minimal essential structure of the lipopolysaccharide (KDO2-lipid A). Thus, FtsH regulates the concentration of the lipid moiety of LPS (lipid A) as well as the sugar moiety (KDO-based core oligosaccharides), ensuring a balanced synthesis of lipopolysaccharide |
| 3.4.24.B17 | colicin D + H2O |
- |
| 3.4.24.B17 | colicin E3 + H2O |
- |
| 3.4.24.B17 | doxorubicin resistance protein B + H2O |
- |
| 3.4.24.B17 | F0a protein + H2O |
- |
| 3.4.24.B17 | FeoB protein + H2O |
- |
| 3.4.24.B17 | lambda Xis + H2O |
protein substrate is required for site-specific excision of phage lambda from the bacterial chromosome |
| 3.4.24.B17 | LpxC + H2O |
ATP-dependent. Essentiality of FtsH lies in its function to keep the proper LPS/phospholipid ratio by degrading LpxC |
| 3.4.24.B17 | LpxC protein + H2O |
efficient substrate |
| 3.4.24.B17 | more |
dislocation of membrane proteins mediated by the enzyme, periplasmic segments can also be degraded by the enzyme |
