Specific potassium binding stabilizes pI258 arsenate reductase from Staphylococcus aureus (Q73229420)

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2 November 2019

title

Specific potassium binding stabilizes pI258 arsenate reductase from Staphylococcus aureus (English)

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2 November 2019

main subject

Staphylococcus aureus

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Nina Lah

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2 November 2019

Jurij Lah

series ordinal

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2 November 2019

Ingrid Zegers

series ordinal

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2 November 2019

language of work or name

English

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publication date

7 April 2003

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Journal of Biological Chemistry

2 November 2019

published in

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2 November 2019

volume

278

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2 November 2019

issue

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2 November 2019

page(s)

24673-24679

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THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS

2 November 2019

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Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty

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Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases

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Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme

21 January 2018

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Purification and characterization of ACR2p, the Saccharomyces cerevisiae arsenate reductase.

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All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade

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21 January 2018

Identifiers

DOI

10.1074/JBC.M303194200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12682056%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

1 reference

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