Crystal Structures of a Hyperthermophilic Archaeal Homoserine Dehydrogenase Suggest a Novel Cofactor Binding Mode for Oxidoreductases

Crystal Structures of a Hyperthermophilic Archaeal Homoserine Dehydrogenase Suggest a Novel Cofactor Binding Mode for Oxidoreductases

NAD(P)-dependent dehydrogenases differ according to their coenzyme preference: some prefer NAD, others NADP, and still others exhibit dual cofactor specificity. The structure of a newly identified archaeal homoserine dehydrogenase showed this enzyme to have a strong preference for NADP. However, NAD...

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Bibliographic Details
Main Authors: Hayashi, Junji, Inoue, Shota, Kim, Kwang, Yoneda, Kazunari, Kawarabayasi, Yutaka, Ohshima, Toshihisa, Sakuraba, Haruhiko
Format: Online
Language:English
Published: Nature Publishing Group 2015
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4495429/

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https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4495429/

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