PMID: 6107127Sep 9, 1980Paper

DNA-dependent ATPase II from Bacillus cereus

Biochimica Et Biophysica Acta
G BánfalviA Ohlbaum

Abstract

A new DNA-dependent ATPase been purified close to homogeneity from soluble extracts of Bacillus cereus. This enzyme, called ATPase II catalyses the hydrolysis of ATP in the presence of Mg2+ or Ca2+ and DNA. Single-stranded linear DNA is a cofactor about 3-fold more effective than double-stranded DNA. The enzyme catalyses the strand separation of duplex DNA in the presence of ATP. However, at concentrations higher than 0.5 mM, phosphohydrolysis can occur without concomitant DNA unwinding. The enzyme has a molecular weight of 84 000 according to SDS-polyacrylamide gel electrophoresis. ATPase II is inhibited by adenosine 5'-(beta, gamma-imido)-diphosphate, actinomycin D and ethidium bromide, but not by nalidixic acid.

References

Sep 15, 1977·European Journal of Biochemistry·M Abdel-MonemH Hoffmann-Berling
Mar 15, 1977·Journal of Molecular Biology·M Abdel-MonemH Hoffmann-Berling
Apr 28, 1973·Biochimica Et Biophysica Acta·R LamedM Wilchek
Jan 1, 1966·Journal of Molecular Biology·C C Richardson
Jan 1, 1964·Biochemistry·P H VONHIPPEL, G FELSENFELD
Jan 1, 1967·Annual Review of Biochemistry·I R Lehman

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Citations

Apr 23, 2003·International Journal of Food Microbiology·Maarten J NautaFrédéric Carlin
Dec 1, 1992·Cell Biochemistry and Function·I H HigutiA J Nascimento
Oct 1, 1990·Biulleten' eksperimental'noĭ biologii i meditsiny·N V BubnovI I Botrin
Oct 21, 2016·Frontiers in Microbiology·Catherine DuportPhilippe Schmitt

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