Kinetic properties of soluble adenosine triphosphatase of escherichia coli

1977 ◽  
Vol 15 (2) ◽  
pp. 145-148 ◽  
Author(s):  
Jan Ahlers
Keyword(s):  
Escherichia Coli ◽  
Adenosine Triphosphatase ◽  
Kinetic Properties

Kinetic properties of rrn promoters in Escherichia coli

Biochimie ◽  
2002 ◽  
Vol 84 (10) ◽  
pp. 981-996 ◽  
Author(s):  
X Zhang ◽  
P Dennis ◽  
M Ehrenberg ◽  
H Bremer
Keyword(s):  
Escherichia Coli ◽  
Kinetic Properties

Genetics of the Adenosine Triphosphatase Complex of Escherichia coli

1982 ◽  
pp. 453-457
Author(s):  
J. Allan Downie ◽  
Frank Gibson ◽  
Graeme B. Cox
Keyword(s):  
Escherichia Coli ◽  
Adenosine Triphosphatase

scholarly journals A mutation affecting a second component of the F0 portion of the magnesium ion-stimulated adenosine triphosphatase of Escherichia coli K12. The uncC424 allele

1977 ◽  
Vol 164 (1) ◽  
pp. 193-198 ◽  
Author(s):  
F Gibson ◽  
G B Cox ◽  
J A Downie ◽  
J Radik
Keyword(s):  
Escherichia Coli ◽  
Electron Transport ◽  
Fluorescence Quenching ◽  
Mutant Strain ◽  
Mutant Allele ◽  
Adenosine Triphosphatase ◽  
Magnesium Ion ◽  
New Mutation ◽  
Similar Phenotype

A new mutant strain of Escherichia coli in which phosphorylation is uncoupled from electron transport was isolated. The new mutant strain has a similar phenotype to the uncB mutant described previously; results from reconstitution experiments in vitro indicate that the new mutation also affects a component of the F0 portion of the Mg2+-stimulated adenosine triphosphatase. A method was developed to incorporate mutant unc alleles into plasmids. Partial diploid strains were prepared in which the uncB402 allele was incorporated into the plasmid and the new unc mutation into the chromosome, or vice versa. Complementation between the mutant unc alleles was indicated by growth on succinate, growth yields on glucose, ATP-dependent transhydrogenase activities, ATP-induced atebrin-fluorescence quenching and oxidative-phosphorylation measurements. The gene in which the new mutation occurs is therefore distinct from the uncB gene, and the mutant allele was designated uncC424.

scholarly journals Characterization of cuckoo-pint (Arum maculatum) mitochondrial adenosine triphosphatases

1986 ◽  
Vol 233 (3) ◽  
pp. 839-844 ◽  
Author(s):  
P P J Dunn ◽  
A R Slabas ◽  
A L Moore
Keyword(s):  
Adenosine Triphosphatase ◽  
Kinetic Properties ◽  
Ph Profile ◽  
Enzyme Preparations ◽  
Adenosine Triphosphatases ◽  
Membrane Bound ◽  
Cold Stability ◽  
Arum Maculatum ◽  
Guanosine Triphosphatase ◽  
Soluble Enzymes

The catalytic properties of cuckoo-pint (Arum maculatum) mitochondrial adenosine triphosphatase have been analysed. The pH profile, effect of inhibitors, cold-stability and substrate specificity are characteristic of mitochondrial adenosine triphosphatases, although a high guanosine triphosphatase activity does appear to be restricted to plant mitochondrial adenosine triphosphatases. The kinetic properties of nucleoside 5′-triphosphate hydrolysis by membrane-bound and soluble enzymes have been studied by means of double-reciprocal plots. These plots were linear in the absence of an activating anion, which may indicate that the catalytic and/or regulatory mechanism of Arum maculatum adenosine triphosphatase is different from that of other enzyme preparations. It is suggested that the differences in subunit composition of plant and mammalian adenosine triphosphatases reported previously [Dunn, Slabas & Moore (1985) Biochem. J. 225, 821-824] are structurally, rather than functionally, significant.

pH dependence of the kinetic properties of allosteric phosphofructokinase from Escherichia coli

Biochemistry ◽  
1991 ◽  
Vol 30 (23) ◽  
pp. 5750-5754 ◽  
Author(s):  
Dominique Deville-Bonne ◽  
Florence Bourgain ◽  
Jean Renaud Garel
Keyword(s):  
Escherichia Coli ◽  
Ph Dependence ◽  
Kinetic Properties
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