scholarly journals Nucleotide-binding sites on Escherichia coli F1-ATPase. Specificity of noncatalytic sites and inhibition at catalytic sites by MgADP.

1994 ◽  
Vol 269 (46) ◽  
pp. 28871-28877 ◽  
Author(s):  
D.J. Hyndman ◽  
Y.M. Milgrom ◽  
E.A. Bramhall ◽  
R.L. Cross
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Nucleotide Binding ◽  
F1 Atpase ◽  
Nucleotide Binding Sites ◽  
Catalytic Sites

scholarly journals Observation of Asymmetry amongst Nucleotide Binding Sites of F1-ATPase of Escherichia coli by31P NMR Spectroscopy

2011 ◽  
Vol 32 (2) ◽  
pp. 531-535 ◽  
Author(s):  
Nam-Kung Jun ◽  
Joon-Hyung Sohn ◽  
Byung-Il Yeh ◽  
Jong-Whan Choi ◽  
Hyun-Won Kim
Keyword(s):  
Escherichia Coli ◽  
Nmr Spectroscopy ◽  
Binding Sites ◽  
Nucleotide Binding ◽  
F1 Atpase ◽  
Nucleotide Binding Sites

scholarly journals Properties of F1-ATPase from the uncD412 mutant of Escherichia coli

1983 ◽  
Vol 215 (2) ◽  
pp. 343-350 ◽  
Author(s):  
J G Wise ◽  
T M Duncan ◽  
L R Latchney ◽  
D N Cox ◽  
A E Senior
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Adenine Nucleotide ◽  
Hydrolysis Rate ◽  
Binding Affinities ◽  
Subunit Interaction ◽  
E Coli ◽  
F1 Atpase ◽  
Nucleotide Binding Sites ◽  
Catalytic Sites

Properties of purified F1-ATPase from Escherichia coli mutant strain AN484 (uncD412) have been studied in an attempt to understand why the amino acid substitution in the beta-subunit of this enzyme causes a tenfold reduction from normal MgATP hydrolysis rate. In most properties that were studied, uncD412 F1-ATPase resembled normal E. coli F1-ATPase. Both enzymes were found to contain a total of six adenine-nucleotide-binding sites, of which three were found to be non-exchangeable and three were exchangeable (catalytic) sites. Binding of the non-hydrolysable substrate analogue adenosine 5′-[beta gamma-imido]triphosphate (p[NH]ppA) to the three exchangeable sites showed apparent negative co-operativity. The binding affinities for p[NH]ppA, and also ADP, at the exchangeable sites were similar in the two enzymes. Both enzymes were inhibited by efrapeptin, aurovertin and p[NH]ppA, and were inactivated by dicyclohexylcarbodi-imide, 4-chloro-7-nitrobenzofurazan and p-fluorosulphonyl-benzoyl-5′-adenosine. Km values for CaATP and MgATP were similar in the two enzymes. uncD412 F1-ATPase was abnormally unstable at high pH, and dissociated into subunits readily with consequent loss of activity. The reason for the impairment of catalysis in uncD412 F1-ATPase cannot be stated with certainty from these studies. However we discuss the possibility that the mutation interrupts subunit interaction, thereby causing a partial impairment in the site-site co-operativity which is required for ‘promotion’ of catalysis in this enzyme.

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