| 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.
See also
References
- ^ Summers KE, Gibbons IR (December 1971). "Adenosine triphosphate-induced sliding of tubules in trypsin-treated flagella of sea-urchin sperm". Proceedings of the National Academy of Sciences of the United States of America. 68 (12): 3092–6. Bibcode: 1971PNAS...68.3092S. doi: 10.1073/pnas.68.12.3092. PMC 389597. PMID 5289252.
- ^ Gibbons IR (November 1988). "Dynein ATPases as microtubule motors". The Journal of Biological Chemistry. 263 (31): 15837–40. doi: 10.1016/S0021-9258(18)37521-5. PMID 2972702.
- ^ Gee M, Vallee R (1998). "The role of the dynein stalk in cytoplasmic and flagellar motility". European Biophysics Journal. 27 (5): 466–73. doi: 10.1007/s002490050157. PMID 9760728. S2CID 21477926.
External links
- Dynein+ATPase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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