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Literature summary for 7.1.2.2 extracted from

  • Imashimizu, M.; Bernat, G.; Sunamura, E.; Broekmans, M.; Konno, H.; Isato, K.; Roegner, M.; Hisabori, T.
    Regulation of F0F1-ATPase from Synechocystis sp. PCC 6803 by gamma and epsilon subunits is significant for light/dark adaptation (2011), J. Biol. Chem., 286, 26595-26602.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information deletion of the extra amino acid segment of FoF1 ATPase gamma subunit results in a high ATP hydrolysis activity Synechocystis sp.

Protein Variants

Protein Variants Comment Organism
additional information construction of mutant strains with a C-terminally truncated epsilon subunit, i.e. epsilonDELTAC, or with a gamma subunit lacking the inserted sequence of residues 198-222, i.e. gammaDELTA198-222, or a double mutant of both. All mutant strains show a lower intracellular ATP level and lower cell viability under prolonged dark incubation compared with the wild-type. Thylakoid membranes from the epsilonDELTAC strain showed higher ATP hydrolysis and lower ATP synthesis activities than those of the wild-type, but no significant difference is observed in growth rate and in intracellular ATP level both under light conditions and during light-dark cycles. The maximal ATPase activity of the epsilonDELTAC mutant is 2fold or more higher than for the wild-type, both show a similar drop in activity after transfer to the dark, phenotypes, overview Synechocystis sp.

Inhibitors

Inhibitors Comment Organism Structure
additional information the FoF1 ATPase epsilon subunit strongly inhibits ATP hydrolysis activity Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.12
-
ATP pH 8.0, 30°C, recombinant mutant epsilonDELTAC, ATP hydrolysis Synechocystis sp.
0.14
-
ATP pH 8.0, 30°C, recombinant wild-type enzyme, ATP hydrolysis Synechocystis sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
thylakoid membrane
-
Synechocystis sp. 42651
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Synechocystis sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Synechocystis sp.
-
ADP + phosphate + H+/out
-
?

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
Synechocystis sp. ADP + phosphate + H+/out
-
?

Synonyms

Synonyms Comment Organism
F0F1-ATPase
-
Synechocystis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
ATP hydrolysis assay at Synechocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
ATP hydrolysis assay at Synechocystis sp.

General Information

General Information Comment Organism
malfunction lethal phenotype of the epsilon knock-out mutant Synechocystis sp.
metabolism internal inhibition of ATP hydrolysis activity of F0F1-ATP synthase is very important for cyanobacteria that are exposed to prolonged dark adaptation and, in general, for the survival of photosynthetic organisms in an ever-changing environment Synechocystis sp.