Plus-end-directed kinesin ATPase
Plus-end-directed kinesin ATPase | |||||||||
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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 ADP + phosphate
This enzyme also hydrolyses GTP.
References
- ↑ Vale, R.D.; Reese, T.S.; Sheetz, M.P. (1985). "Identification of a novel force-generating protein, kinesin, in microtubule-based motility". Cell. 42: 39–50. doi:10.1016/S0092-8674(85)80099-4. PMC 2851632. PMID 3926325.
- ↑ Howard, J. (1997). "Molecular motors: structural adaptations to cellular functions". Nature. 389 (6651): 561–567. doi:10.1038/39247. PMID 9335494.
- ↑ Nakagawa, T.; Tanaka, Y.; Matsuoka, E.; Kondo, S.; Okada, Y.; Noda, F.; Kanai, Y.; Hirokawa, N. (1997). "Identification and classification of 16 new kinesin superfamily (KIF) proteins in mouse genome". Proc. Natl. Acad. Sci. USA. 94 (18): 9654–9659. doi:10.1073/pnas.94.18.9654. PMC 23244. PMID 9275178.
See also
External links
- Plus-end-directed kinesin ATPase at the US National Library of Medicine Medical Subject Headings (MeSH)
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