Enzymatic effects of a lysine-to-glutamine mutation in the ATP-binding consensus sequence in the RecD subunit of the RecBCD enzyme from Escherichia coli (Q67841207)

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scientific article published on January 25, 1992

Enzymatic effects of a lysine-to-glutamine mutation in the ATP-binding consensus sequence in the RecD subunit of the RecBCD enzyme from Escherichia coli.

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English	Enzymatic effects of a lysine-to-glutamine mutation in the ATP-binding consensus sequence in the RecD subunit of the RecBCD enzyme from Escherichia coli	scientific article published on January 25, 1992	Enzymatic effects of a lysine-to-glutamine mutation in the ATP-binding consensus sequence in the RecD subunit of the RecBCD enzyme from Escherichia coli.

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18 September 2019

10.1016/s0021-9258(18)46007-3

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17 December 2022

Enzymatic effects of a lysine-to-glutamine mutation in the ATP-binding consensus sequence in the RecD subunit of the RecBCD enzyme from Escherichia coli (English)

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18 September 2019

Escherichia coli

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Escherichia coli proteins

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30 November 2023

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30 November 2023

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30 November 2023

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F. Korangy

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30 November 2023

D. A. Julin

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1 January 1992

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18 September 2019

January 1992

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10.1016/s0021-9258(18)46007-3

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17 December 2022

25 January 1992

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National Center for Biotechnology Information

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30 November 2023

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30 November 2023

http://intl.jbc.org/cgi/content/abstract/267/3/1733

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30 November 2023

https://api.elsevier.com/content/article/PII:S0021925818460073?httpAccept=text/xml

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10.1016/S0021-9258(18)46007-3

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30 November 2023

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30 November 2023

Journal of Biological Chemistry

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10.1016/s0021-9258(18)46007-3

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17 December 2022

267

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10.1016/s0021-9258(18)46007-3

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10.1016/s0021-9258(18)46007-3

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1733-1740

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18 September 2019

10.1016/s0021-9258(18)46007-3

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17 December 2022

recD: the gene for an essential third subunit of exonuclease V

1

1 reference

10.1016/S0021-9258(18)46007-3

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A new class of Escherichia coli recBC mutants: implications for the role of RecBC enzyme in homologous recombination

4

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Solubility and dialysis limits of DNA oligonucleotides

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Photoaffinity labeling of the recBCD enzyme of Escherichia coli with 8-azidoadenosine 5'-triphosphate.

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Alteration by site-directed mutagenesis of the conserved lysine residue in the ATP-binding consensus sequence of the RecD subunit of the Escherichia coli RecBCD enzyme.

12

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The recBC deoxyribonuclease of Escherichia coli: isolation and characterization of the subunit proteins and reconstitution of the enzyme

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Site-specific mutagenesis of conserved residues within Walker A and B sequences of Escherichia coli UvrA protein

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Biochemical and physical characterization of exonuclease V from Escherichia coli. Comparison of the catalytic activities of the RecBC and RecBCD enzymes.

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Directed mutations of the strongly conserved lysine 155 in the catalytic nucleotide-binding domain of beta-subunit of F1-ATPase from Escherichia coli.

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Characterization of the adenosinetriphosphatase activity of the Escherichia coli RecBCD enzyme: relationship of ATP hydrolysis to the unwinding of duplex DNA.

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10.1016/S0021-9258(18)46007-3

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10.1016/s0021-9258(18)46007-3

https://api.crossref.org/v1/works/https://doi.org/10.1016/s0021-9258(18)46007-3

17 December 2022

PubMed publication ID

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:1309793%20AND%20SRC:MED&resulttype=core&format=json

18 September 2019

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