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, NADP...

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Veröffentlicht in:	Scientific reports 2015-07, Vol.5 (1), p.11674-11674, Article 11674
Hauptverfasser:	Hayashi, Junji, Inoue, Shota, Kim, Kwang, Yoneda, Kazunari, Kawarabayasi, Yutaka, Ohshima, Toshihisa, Sakuraba, Haruhiko
Format:	Artikel
Sprache:	eng
Schlagworte:	101/58 631/45/173 631/45/607/1168 Amino Acid Sequence Archaea - genetics Archaea - metabolism Binding Sites Catalysis Dehydrogenase Dehydrogenases Enzymes Homoserine dehydrogenase Homoserine Dehydrogenase - chemistry Homoserine Dehydrogenase - genetics Homoserine Dehydrogenase - metabolism Humanities and Social Sciences Kinetics Models, Molecular Molecular Sequence Data multidisciplinary NAD NADP NADP - chemistry NADP - metabolism Oxidation Oxidoreductases - metabolism Protein Binding Protein Conformation Science Sequence Alignment Site-directed mutagenesis Structural analysis Substrate Specificity
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