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The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs

Ali, Janid A., Jackson, Andrew P., Howells, Alison J., Maxwell, Anthony·1993·Biochemistry

Abstract

We have cloned and overexpressed a gene encoding a 43-kDa protein corresponding to the N-terminal fragment of the DNA gyrase B subunit. We show that this protein hydrolyzes ATP and binds coumarin drugs. The hydrolysis of ATP shows distinctly non-Michaelis-Menten kinetics and is consistent with a scheme in which the active form of the protein is a dimer, a conclusion supported by molecular weight studies. The coumarin drugs bind very tightly to the 43-kDa fragment, with novobiocin binding to the protein monomer and coumermycin A1 apparently inducing the formation of a dimer. The implications of these results with respect to the mechanism of supercoiling by DNA gyrase and the inhibition of gyrase by coumarin drugs are discussed.

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Metadata

Authors
Ali, J. A., Jackson, A. P., Howells, A. J., & Maxwell, A.
Venue
Biochemistry
Published
1993-03-16
Volume
32
Issue
10
Pages
2717-2724
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2068435780
Cited by
303
References
0
FWCI
3.37
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs. https://app.cochat.ai/papers/10.1021/bi00061a033
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Ali, J. A., Jackson, A. P., Howells, A. J., & Maxwell, A. (1993). The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs. Biochemistry. https://doi.org/10.1021/bi00061a033

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