Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site (Q34436869)

2 August 2017

title

Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site (English)

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2 August 2017

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Kazuko Fujiwara

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2 August 2017

Sachiko Toma

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2 August 2017

Kazuko Okamura-Ikeda

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2 August 2017

Yutaro Motokawa

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2 August 2017

Atsushi Nakagawa

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2 August 2017

Hisaaki Taniguchi

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2 August 2017

language of work or name

English

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publication date

25 July 2005

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Journal of Biological Chemistry

2 August 2017

published in

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2 August 2017

volume

280

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2 August 2017

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2 August 2017

page(s)

33645-33651

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Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein

2 August 2017

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Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein

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A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria

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The Escherichia coli lipB gene encodes lipoyl (octanoyl)-acyl carrier protein:protein transferase

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Evidence for two protein-lipoylation activities inEscherichia coli

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Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains

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Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M505010200

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2 August 2017

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