Plus-end-directed kinesin ATPase
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| Plus-end-directed kinesin ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.4.4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Plus-end-directed kinesin ATPase (EC 3.6.4.4, kinesin) is an enzyme with systematic name kinesin ATP phosphohydrolase (plus-end-directed).[1][2][3] This enzyme catalyses the following chemical reaction
- ATP + H2O ADP + phosphate
This enzyme also hydrolyses GTP.
See also[edit]
References[edit]
- ^ Vale RD, Reese TS, Sheetz MP (August 1985). "Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility". Cell. 42 (1): 39–50. doi:10.1016/S0092-8674(85)80099-4. PMC 2851632. PMID 3926325.
- ^ Howard J (October 1997). "Molecular motors: structural adaptations to cellular functions". Nature. 389 (6651): 561–7. Bibcode:1997Natur.389..561H. doi:10.1038/39247. PMID 9335494. S2CID 4421625.
- ^ Nakagawa T, Tanaka Y, Matsuoka E, Kondo S, Okada Y, Noda Y, Kanai Y, Hirokawa N (September 1997). "Identification and classification of 16 new kinesin superfamily (KIF) proteins in mouse genome". Proceedings of the National Academy of Sciences of the United States of America. 94 (18): 9654–9. Bibcode:1997PNAS...94.9654N. doi:10.1073/pnas.94.18.9654. PMC 23244. PMID 9275178.
External links[edit]
- Plus-end-directed+kinesin+ATPase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
