A Novel Polyamine Allosteric Site of SpeG from Vibrio cholerae Is Revealed by Its Dodecameric Structure.

Ekaterina V. Filippova; Misty L. Kuhn; Jerzy Osipiuk; Olga Kiryukhina; Andrzej Joachimiak; Miguel A. Ballicora; Wayne F. Anderson

doi:10.1016/j.jmb.2015.01.009

A Novel Polyamine Allosteric Site of SpeG from Vibrio cholerae Is Revealed by Its Dodecameric Structure.

Ekaterina V. Filippova, Misty L. Kuhn, Jerzy Osipiuk, Olga Kiryukhina, Andrzej Joachimiak, Miguel A. Ballicora, Wayne F. Anderson

Department of Chemistry and Biochemistry

Research output: Contribution to journal › Article › peer-review

Original language	American English
Journal	Journal of Molecular Biology
Volume	427
Issue number	6
DOIs	https://doi.org/10.1016/j.jmb.2015.01.009
State	Published - Jan 3 2015

Disciplines

Biology
Molecular Biology
Biochemistry

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@article{4b95461e5e604ae1bb8d544d4660e76c,

title = "A Novel Polyamine Allosteric Site of SpeG from Vibrio cholerae Is Revealed by Its Dodecameric Structure.",

author = "Filippova, {Ekaterina V.} and Kuhn, {Misty L.} and Jerzy Osipiuk and Olga Kiryukhina and Andrzej Joachimiak and Ballicora, {Miguel A.} and Anderson, {Wayne F.}",

note = "Spermidine N-acetyltransferase, encoded by the gene speG, catalyzes the initial step in the degradation of polyamines and is a critical enzyme for determining the polyamine concentrations in bacteria. In Escherichia coli, studies have shown that SpeG is the enzyme responsible for acetylating spermidine under stress conditions and for preventing spermidine toxicity.",

year = "2015",

month = jan,

day = "3",

doi = "10.1016/j.jmb.2015.01.009",

language = "American English",

volume = "427",

journal = "Journal of Molecular Biology",

number = "6",

}

TY - JOUR

T1 - A Novel Polyamine Allosteric Site of SpeG from Vibrio cholerae Is Revealed by Its Dodecameric Structure.

AU - Filippova, Ekaterina V.

AU - Kuhn, Misty L.

AU - Osipiuk, Jerzy

AU - Kiryukhina, Olga

AU - Joachimiak, Andrzej

AU - Ballicora, Miguel A.

AU - Anderson, Wayne F.

N1 - Spermidine N-acetyltransferase, encoded by the gene speG, catalyzes the initial step in the degradation of polyamines and is a critical enzyme for determining the polyamine concentrations in bacteria. In Escherichia coli, studies have shown that SpeG is the enzyme responsible for acetylating spermidine under stress conditions and for preventing spermidine toxicity.

PY - 2015/1/3

Y1 - 2015/1/3

UR - https://www.sciencedirect.com/science/article/pii/S0022283615000303

U2 - 10.1016/j.jmb.2015.01.009

DO - 10.1016/j.jmb.2015.01.009

M3 - Article

VL - 427

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 6

ER -

A Novel Polyamine Allosteric Site of SpeG from Vibrio cholerae Is Revealed by Its Dodecameric Structure.

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