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Structural insights into the octamerization of glycerol dehydrogenase.
Park, Taein; Kang, Jung Youn; Jin, Minwoo; Yang, Jihyeong; Kim, Hyunwoo; Noh, Chaemin; Jung, Che-Hun; Eom, Soo Hyun.
Afiliación
  • Park T; Department of Chemistry, Gwangju Institute of Science and Technology (GIST), Gwangju, Republic of Korea.
  • Kang JY; School of Life Sciences, Gwangju Institute of Science and Technology (GIST), Gwangju, Republic of Korea.
  • Jin M; School of Life Sciences, Gwangju Institute of Science and Technology (GIST), Gwangju, Republic of Korea.
  • Yang J; School of Life Sciences, Gwangju Institute of Science and Technology (GIST), Gwangju, Republic of Korea.
  • Kim H; School of Life Sciences, Gwangju Institute of Science and Technology (GIST), Gwangju, Republic of Korea.
  • Noh C; School of Life Sciences, Gwangju Institute of Science and Technology (GIST), Gwangju, Republic of Korea.
  • Jung CH; Department of Molecular Medicine, Chonnam National University, Gwangju, Republic of Korea.
  • Eom SH; Department of Chemistry, Chonnam National University, Gwangju, Republic of Korea.
PLoS One ; 19(3): e0300541, 2024.
Article en En | MEDLINE | ID: mdl-38483875
ABSTRACT
Glycerol dehydrogenase (GDH) catalyzes glycerol oxidation to dihydroxyacetone in a NAD+-dependent manner. As an initiator of the oxidative pathway of glycerol metabolism, a variety of functional and structural studies of GDH have been conducted previously. Structural studies revealed intriguing features of GDH, like the flexible ß-hairpin and its significance. Another commonly reported structural feature is the enzyme's octameric oligomerization, though its structural details and functional significance remained unclear. Here, with a newly reported GDH structure, complexed with both NAD+ and glycerol, we analyzed the octamerization of GDH. Structural analyses revealed that octamerization reduces the structural dynamics of the N-domain, which contributes to more consistently maintaining a distance required for catalysis between the cofactor and substrate. This suggests that octamerization may play a key role in increasing the likelihood of the enzyme reaction by maintaining the ligands in an appropriate configuration for catalysis. These findings expand our understanding of the structure of GDH and its relation to the enzyme's activity.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Deshidrogenasas del Alcohol de Azúcar / NAD Idioma: En Revista: PLoS One Asunto de la revista: CIENCIA / MEDICINA Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Deshidrogenasas del Alcohol de Azúcar / NAD Idioma: En Revista: PLoS One Asunto de la revista: CIENCIA / MEDICINA Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos