Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction

Homoserine dehydrogenase (HSD; 305 amino acid residues) catalyzes an NAD(P)-dependent reversible reaction between l-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway. HSD from the hyperthermophilic archaeon Sulfolobus tokodaii was markedly activated (2.5-fold) by the a...

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Autores principales: Tomonaga, Yoshihisa, Kaneko, Ryosuke, Goto, Masaru, Ohshima, Toshihisa, Yoshimune, Kazuaki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2015
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5668673/
https://www.ncbi.nlm.nih.gov/pubmed/29124164
http://dx.doi.org/10.1016/j.bbrep.2015.07.006
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author Tomonaga, Yoshihisa
Kaneko, Ryosuke
Goto, Masaru
Ohshima, Toshihisa
Yoshimune, Kazuaki
author_facet Tomonaga, Yoshihisa
Kaneko, Ryosuke
Goto, Masaru
Ohshima, Toshihisa
Yoshimune, Kazuaki
author_sort Tomonaga, Yoshihisa
collection PubMed
description Homoserine dehydrogenase (HSD; 305 amino acid residues) catalyzes an NAD(P)-dependent reversible reaction between l-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway. HSD from the hyperthermophilic archaeon Sulfolobus tokodaii was markedly activated (2.5-fold) by the addition of 0.8 mM dithiothreitol. The crystal structure of the homodimer indicated that the activation was caused by cleavage of the disulfide bond formed between two cysteine residues (C303) in the C-terminal regions of the two subunits.
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spelling pubmed-56686732017-11-09 Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction Tomonaga, Yoshihisa Kaneko, Ryosuke Goto, Masaru Ohshima, Toshihisa Yoshimune, Kazuaki Biochem Biophys Rep Research Article Homoserine dehydrogenase (HSD; 305 amino acid residues) catalyzes an NAD(P)-dependent reversible reaction between l-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway. HSD from the hyperthermophilic archaeon Sulfolobus tokodaii was markedly activated (2.5-fold) by the addition of 0.8 mM dithiothreitol. The crystal structure of the homodimer indicated that the activation was caused by cleavage of the disulfide bond formed between two cysteine residues (C303) in the C-terminal regions of the two subunits. Elsevier 2015-07-15 /pmc/articles/PMC5668673/ /pubmed/29124164 http://dx.doi.org/10.1016/j.bbrep.2015.07.006 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Research Article
Tomonaga, Yoshihisa
Kaneko, Ryosuke
Goto, Masaru
Ohshima, Toshihisa
Yoshimune, Kazuaki
Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction
title Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction
title_full Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction
title_fullStr Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction
title_full_unstemmed Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction
title_short Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction
title_sort structural insight into activation of homoserine dehydrogenase from the archaeon sulfolobus tokodaii via reduction
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5668673/
https://www.ncbi.nlm.nih.gov/pubmed/29124164
http://dx.doi.org/10.1016/j.bbrep.2015.07.006
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