Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 7.1.2.2 extracted from

  • Komoriya, Y.; Ariga, T.; Iino, R.; Imamura, H.; Okuno, D.; Noji, H.
    Principal role of the arginine finger in rotary catalysis of F1-ATPase (2012), J. Biol. Chem., 287, 15134-15142.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged enzyme mutants R364K, C193S, and C193S/R364K and of His-tagged hybrid mutants in Escherichia coli Bacillus sp. (in: Bacteria)

Protein Variants

Protein Variants Comment Organism
C193S alpha(His6 at N terminus/C193S)3beta(His10 at N terminus)3gamma(S108C/I211C) mutant subcomplex of F1 Bacillus sp. (in: Bacteria)
C193S/R364K alpha(His6 at N terminus/C193S/R364K)3beta(His10 at N terminus)3gamma(S108C/I211C) mutant subcomplex of F1 Bacillus sp. (in: Bacteria)
additional information preparation of hybrid F1, alpha(C193S)3beta3gamma(S108C/I211C) subcomplex, of a hybrid F1 that carries a single alpha(R364K) subunit and 2 wild-type alpha subunits: F1(1 x alphaR364K), and of monomer alpha(His6 at N terminus/C193S/R364K) and of hybrid F1 containing one alpha(R364K), alpha(His6 at N terminus/C193S/R364K)alpha(C193S)2beta3gamma(S108C/I211C), termed F1(1xalphaR364K), the mutants are affected in rotation and hydrolysis activities, phenotypes, overview Bacillus sp. (in: Bacteria)
R364K alpha-subunit catalytic arginine finger mutant, the mutant shows a 350fold longer catalytic pause than the wild-type enzyme, but highly unidirectional rotation with a coupling ratio of 3 ATPs/turn, the same as wild-type, suggesting that cooperative torque generation by the 3 beta-subunits is not impaired. The alphaR364K mutation causes severe ADP inhibition of TF1 Bacillus sp. (in: Bacteria)

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics of rotation Bacillus sp. (in: Bacteria)

Organism

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

Subunits

Subunits Comment Organism
More F1-ATPase is an ATP-driven rotary motor wherein the gamma-subunit rotates against the surrounding alpha3beta3 stator ring. The three catalytic sites of F1-ATPase reside on the interface of the alpha and beta subunits of the alpha3beta3 ring. While the catalytic residues predominantly reside on the beta subunit, the alpha subunit has one catalytically critical arginine, termed the arginine finger Bacillus sp. (in: Bacteria)

Synonyms

Synonyms Comment Organism
F1-ATPase
-
Bacillus sp. (in: Bacteria)

General Information

General Information Comment Organism
malfunction lysine substitution of the alpha subunit catalytically critical Arg364 residue causes frequent pauses because of severe ADP inhibition, and a slight decrease in ATP binding rate Bacillus sp. (in: Bacteria)
additional information F1-ATPase is a water-soluble portion of the FoF1-ATP synthase and an ATP-driven rotary motor wherein the gamma-subunit rotates against the surrounding alpha3beta3 stator ring. The three catalytic sites of F1-ATPase reside on the interface of the alpha and beta subunits of the alpha3beta3 ring. While the catalytic residues predominantly reside on the beta subunit, the alpha subunit has one catalytically critical arginine at position 364, termed the arginine finger, with stereogeometric similarities with the arginine finger of G-protein-activating proteins. The principal role of the arginine finger is not to mediate cooperativity among the catalytic sites, but to enhance the rate of the ATP cleavage by stabilizing the transition state of ATP hydrolysis Bacillus sp. (in: Bacteria)