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Literature summary for 7.1.2.2 extracted from

  • Kuruma, Y.; Suzuki, T.; Ono, S.; Yoshida, M.; Ueda, T.
    Functional analysis of membranous Fo-a subunit of F1Fo-ATP synthase by in vitro protein synthesis (2012), Biochem. J., 442, 631-638.
    View publication on PubMed
Search for more literature for 7.1.2.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of at subunit beta N-terminally His10-tagged wild-type and mutant F1Fo in Escherichia coli and by the in vitro protease-free protein synthesis, PURE, system Bacillus sp. (in: Bacteria)

Protein Variants

Protein Variants Comment Organism
D112A site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant shows reduced activity compared to the wild-type enzyme Bacillus sp. (in: Bacteria)
additional information construction of a F1Fo mutant lacking the alpha-subunit, F1FoDELTAa, the alpha-subunit produced by the in vitro protease-free protein synthesis system is integrated into a preformed Fo a-less F1Fo complex in Escherichia coli membrane vesicles and liposomes. The resulting F1Fo has a H+-coupled ATP synthesis/hydrolysis activity that is approximately half that of the native F1Fo Bacillus sp. (in: Bacteria)
N173A site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant retains full activity compared to the wild-type enzyme Bacillus sp. (in: Bacteria)
N90A site-directed mutagenesis, mutation of the alpha-subunit residue, inactive mutant Bacillus sp. (in: Bacteria)
Q217A site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant shows reduced activity compared to the wild-type enzyme Bacillus sp. (in: Bacteria)
R169A site-directed mutagenesis, mutation of the alpha-subunit residue, inactive mutant Bacillus sp. (in: Bacteria)

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Bacillus sp. (in: Bacteria) 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Bacillus sp. (in: Bacteria)

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Bacillus sp. (in: Bacteria)
-
 ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in Bacillus sp. (in: Bacteria) PS3
-
 ADP + phosphate + H+/out
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
 unc operon
-
Bacillus sp. (in: Bacteria) PS3
-
 unc operon
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His10-tagged wild-type and mutant F1Fo from Escherichia coli and the in vitro protease-free protein synthesis, PURE, system by nickel affinity chromatography Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Bacillus sp. (in: Bacteria) ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in
-
 Bacillus sp. (in: Bacteria) PS3 ADP + phosphate + H+/out
-
 ?

Synonyms

Synonyms Comment Organism
F1Fo
-
 Bacillus sp. (in: Bacteria)
F1FO-ATP synthase
-
 Bacillus sp. (in: Bacteria)

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 assay at Bacillus sp. (in: Bacteria)

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Bacillus sp. (in: Bacteria)

General Information

General Information Comment Organism
additional information Asn90 is located in the middle of putative second transmembrane helix and likely to play an important role in H+-translocation Bacillus sp. (in: Bacteria)