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Literature summary extracted from

  • Nicholas, M.P.; Berger, F.; Rao, L.; Brenner, S.; Cho, C.; Gennerich, A.
    Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains (2015), Proc. Natl. Acad. Sci. USA, 112, 6371-6376 .
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.6.1.2 cytoplasm
-
 Saccharomyces cerevisiae 5737
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.6.1.2 ATP + H2O + a dynein associated with a microtubule at position n Saccharomyces cerevisiae
-
 ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
-
 ?
5.6.1.2 ATP + H2O + a dynein associated with a microtubule at position n Saccharomyces cerevisiae ATCC 204508
-
 ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.6.1.2 Saccharomyces cerevisiae P36022
-
-
5.6.1.2 Saccharomyces cerevisiae ATCC 204508 P36022
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.1.2 ATP + H2O + a dynein associated with a microtubule at position n
-
 Saccharomyces cerevisiae ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
-
 ?
5.6.1.2 ATP + H2O + a dynein associated with a microtubule at position n dynein is responsible for most microtubule minus-end-directed motility. Dynein contains four AAA+ ATPases per motor domain (AAA1-4). The main site of ATP hydrolysis is AAA1. ATP binding to AAA1 induces microtubule release only if AAA3 is in the posthydrolysis state Saccharomyces cerevisiae ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
-
 ?
5.6.1.2 ATP + H2O + a dynein associated with a microtubule at position n
-
 Saccharomyces cerevisiae ATCC 204508 ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
-
 ?
5.6.1.2 ATP + H2O + a dynein associated with a microtubule at position n dynein is responsible for most microtubule minus-end-directed motility. Dynein contains four AAA+ ATPases per motor domain (AAA1-4). The main site of ATP hydrolysis is AAA1. ATP binding to AAA1 induces microtubule release only if AAA3 is in the posthydrolysis state Saccharomyces cerevisiae ATCC 204508 ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
-
 ?

Subunits

EC Number Subunits Comment Organism
5.6.1.2 homodimer
-
 Saccharomyces cerevisiae