EC Number   |
Reaction |
Reference |
|---|
   3.4.21.105 | cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains |
- |
- |
| 3.4.21.105 | cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains |
active site structure and catalytic mechanism, structure-function realationship |
683913 |
| 3.4.21.105 | cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains |
catalytic mechanism, structure of the active site within the membrane, residues Ser201, His150, and Asn154 are important in catalysis, overview |
684010 |
| 3.4.21.105 | cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains |
rhomboid structure and catalytic mechanism, catalytic dyad id formed by S201 and H254, structure-function modeling |
683867 |
| 3.4.21.105 | cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains |
rhomboid structure and catalytic mechanism, structure-function modeling |
683867 |
| 3.4.21.105 | cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains |
ROM1 of Toxoplasma gondii contains a catalytic triad consisting of asparagine, histidine, and serine residues of in transmembrane domains 2, 6, and 4 |
683419 |
| 3.4.21.105 | cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains |
structure-function relationship, catalytic residues are Ser201 of transmembrane helix 4 and His254 of transmembrane helix 6 |
684012 |
| 3.4.21.105 | cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains |
the active site structure, with a Ser 201 and His 254 catalytic dyad, is accessible by substrate through a large V-shaped opening that faces laterally towards the lipid, but is blocked by a half-submerged loop structure, catalytically involved residues and water molecules, catalytic mechanism, overview |
683916 |
| 3.4.21.105 | cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains |
transmembrane helix 5 is the lateral substrate gate, the enzyme contains a catalytic serine recessed into the plane of the membrane, within a hydrophilic cavity that opens to the extracellular face, but protected laterally from membrane lipids by a ring of transmembrane segments, structure-function analysis, transmembrane helix 5 movement to gate lateral substrate entry is a rate-limiting step in intramembrane proteolysis |
684013 |
