Biology:Plus-end-directed kinesin ATPase
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Short description: Class of enzymes
| Plus-end-directed kinesin ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] ADP + phosphate
This enzyme also hydrolyses GTP.
See also
- Kinesin
References
- ↑ "Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility". Cell 42 (1): 39–50. August 1985. doi:10.1016/S0092-8674(85)80099-4. PMID 3926325.
- ↑ "Molecular motors: structural adaptations to cellular functions". Nature 389 (6651): 561–7. October 1997. doi:10.1038/39247. PMID 9335494. Bibcode: 1997Natur.389..561H.
- ↑ "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. September 1997. doi:10.1073/pnas.94.18.9654. PMID 9275178. Bibcode: 1997PNAS...94.9654N.
External links
- Plus-end-directed+kinesin+ATPase at the US National Library of Medicine Medical Subject Headings (MeSH)
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