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Literature summary for 3.6.4.6 extracted from

  • Hill, C.P.; Babst, M.
    Structure and function of the membrane deformation AAA ATPase Vps4 (2012), Biochim. Biophys. Acta, 1823, 172-181.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.6

Activating Compound

Activating Compound Comment Organism Structure
additional information Ist1, Did2, Vta1 and Vps60 function as a regulatory system that ensures proper recruitment and assembly of ATPase Vps4 on the ESCRT-III protein complex. Directly or indirectly these factors affect ATPase activity of Vps4, suggesting that they also regulate the Vps4 ESCRT-III disassembly activity Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E233Q a mutant protein with very low ATPase activity. In the presence of ADP recombinant mutant enzyme forms dimers. In contrast, the addition of ATP results in the formation of a large complex with at least ten subunits Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Saccharomyces cerevisiae Vps4 disassembles the ESCRT-III protein polymer, thereby changing the morphology of the underlying membrane. The disassembly reaction causes the ESCRT-III subunits to regain the monomeric conformational state, which is the high-energy state that is poised to reassemble again into the ESCRT-III oligomer for subsequent rounds of membrane scission. When assembled, Vps4 progresses through many ATP hydrolysis cycles without dissociation ADP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O = ADP + phosphate Vps4 disassembles the ESCRT-III protein polymer, thereby changing the morphology of the underlying membrane Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O Vps4 disassembles the ESCRT-III protein polymer, thereby changing the morphology of the underlying membrane. The disassembly reaction causes the ESCRT-III subunits to regain the monomeric conformational state, which is the high-energy state that is poised to reassemble again into the ESCRT-III oligomer for subsequent rounds of membrane scission. When assembled, Vps4 progresses through many ATP hydrolysis cycles without dissociation Saccharomyces cerevisiae ADP + phosphate
-
 ?
ATP + H2O Vps4 disassembles the ESCRT-III protein polymer, thereby changing the morphology of the underlying membrane Saccharomyces cerevisiae ADP + phosphate
-
 ?

Subunits

Subunits Comment Organism
More Vps4 exhibits a dynamic structure that is regulated by the nucleotide-binding state. Oligomerization of the enzyme occurs at protein concentrations above 0.0005 mM in vitro whereas the concentration of Vps4 in vivo is 0.0002 mM. In the cytoplasm the enzyme is dimeric and exhibits no ATPase activity. It is recruited to membrane-associated ESCRT-III where it oligomerizes into the active enzyme Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
membrane deformation AAA ATPase
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.85
-
 ATP higher order oligomer of the enzyme, pH and temperature not specified in the publication Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function Vps4 functions together with the protein complex ESCRT-III in membrane fission Saccharomyces cerevisiae