Cloned (Comment) | Organism |
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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 | Comment | Organism |
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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 Maximum [mM] | Substrate | Comment | Organism | Structure |
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additional information | - |
additional information | Michaelis-Menten kinetics of rotation | Bacillus sp. (in: Bacteria) |
Organism | UniProt | Comment | Textmining |
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Bacillus sp. (in: Bacteria) | - |
- |
- |
Bacillus sp. (in: Bacteria) PS3 | - |
- |
- |
Subunits | Comment | Organism |
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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 | Comment | Organism |
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F1-ATPase | - |
Bacillus sp. (in: Bacteria) |
General Information | Comment | Organism |
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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) |