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Literature summary for 5.6.1.3 extracted from

  • Arellano-Santoyo, H.; Geyer, E.A.; Stokasimov, E.; Chen, G.Y.; Su, X.; Hancock, W.; Rice, L.M.; Pellman, D.
    A tubulin binding switch underlies Kip3/Kinesin-8 depolymerase activity (2017), Dev. Cell, 42, 37-51.e8 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.3

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + a kinesin associated with a microtubule at position n Saccharomyces cerevisiae
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 ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P53086
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a kinesin associated with a microtubule at position n
-
 Saccharomyces cerevisiae ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
 ?
ATP + H2O + a kinesin associated with a microtubule at position n kinesin-8/Kip3 uses ATP hydrolysis for stepping on the microtubule lattice, but at the plus-end, Kip3 undergoes a switch. Its ATPase activity is suppressed when it binds tightly to the curved conformation of tubulin. This prolongs plus-end binding, stabilizes protofilament curvature, and ultimately promotes microtubule disassembly Saccharomyces cerevisiae ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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 ?

Synonyms

Synonyms Comment Organism
kinesin-8
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 Saccharomyces cerevisiae
Kip3
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 Saccharomyces cerevisiae