Biology:Dynein ATPase
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Short description: Class of enzymes
| Dynein ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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 [math]\displaystyle{ \rightleftharpoons }[/math] ADP + phosphate
This enzyme is a multisubunit protein complex associated with microtubules.
See also
- Dynein
References
- ↑ "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. December 1971. doi:10.1073/pnas.68.12.3092. PMID 5289252. Bibcode: 1971PNAS...68.3092S.
- ↑ "Dynein ATPases as microtubule motors". The Journal of Biological Chemistry 263 (31): 15837–40. November 1988. doi:10.1016/S0021-9258(18)37521-5. PMID 2972702.
- ↑ "The role of the dynein stalk in cytoplasmic and flagellar motility". European Biophysics Journal 27 (5): 466–73. 1998. doi:10.1007/s002490050157. PMID 9760728.
External links
- Dynein+ATPase at the US National Library of Medicine Medical Subject Headings (MeSH)
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