| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1981856 | FEBS Open Bio | 2012 | 14 Pages |
Abstract
⸠Focus is on a thermophilic (CtIDH) and cold active (DpIDH) isocitrate dehydrogenase. ⸠Biochemical characterization and three new IDH crystal structures are presented. ⸠CtIDH has many ionic interactions and hydrogen bonds, which explain the Tm of 68 °C. ⸠Prokaryotic IDH subfamily II seems to have a unique locking mechanism. ⸠The large domain is locked to the small domain and NADP+ is also directed correctly.
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Biochemistry
Authors
Hanna-Kirsti S. Leiros, Anita-Elin Fedøy, Ingar Leiros, Ida Helene Steen,