Signal-recognition-particle GTPase
| Signal-recognition-particle GTPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.5.4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Signal-recognition-particle GTPase (EC 3.6.5.4) is an enzyme with systematic name GTP phosphohydrolase (protein-synthesis-assisting).[1][2][3][4] This enzyme catalyses the following chemical reaction
- GTP + H2O GDP + phosphate
Enzyme activity is associated with the signal-recognition particle.
References
- ^ Connolly, T.; Gilmore, R. (1989). "The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide". Cell. 57 (4): 599–610. doi:10.1016/0092-8674(89)90129-3. PMID 2541918.
- ^ Connolly, T.; Rapiejko, P.J.; Gilmore, R. (1991). "Requirement of GTP hydrolysis for dissociation of the signal recognition particle from its receptor". Science. 252 (5009): 1171–1173. doi:10.1126/science.252.5009.1171. PMID 1851576.
- ^ Miller, J.D.; Wilhelm, H.; Gierasch, L.; Gilmore, R.; Walter, P. (1993). "GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation". Nature. 366 (6453): 351–354. doi:10.1038/366351a0. PMID 8247130.
- ^ Freymann, D.M.; Keenan, R.J.; Stroud, R.M.; Walter, P. (1997). "Structure of the conserved GTPase domain of the signal recognition particle". Nature. 385 (6614): 361–364. doi:10.1038/385361a0. PMID 9002524.
See also
External links
- Signal-recognition-particle+GTPase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)