Dynein ATPase
| Dynein ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.4.2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Dynein ATPase (EC 3.6.4.2, dynein adenosine 5'-triphosphatase) is an enzyme with systematic name ATP phosphohydrolase (tubulin-translocating).[1][2][3] This enzyme catalyses the following chemical reaction
- ATP + H2O ADP + phosphate
This enzyme is a multisubunit protein complex associated with microtubules.
References
- ^ Summers, K.E.; Gibbons, I.R. (1971). "Adenosine triphosphate-induced sliding of tubules in trypsin-treated flagella of sea-urchin sperm". Proc. Natl. Acad. Sci. USA. 68: 3092–3096. doi:10.1073/pnas.68.12.3092. PMID 5289252.
- ^ Gibbons, I.R. (1988). "Dynein ATPases as microtubule motors". J. Biol. Chem. 263: 15837–15840. PMID 2972702.
- ^ Gee, M.; Vallee, R. (1998). "The role of the dynein stalk in cytoplasmic and flagellar motility". Eur. Biophys. J. 27: 466–473. doi:10.1007/s002490050157. PMID 9760728.
See also
External links
- Dynein+ATPase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)