4TSK
Ketol-acid reductoisomerase from Alicyclobacillus acidocaldarius
Summary for 4TSK
| Entry DOI | 10.2210/pdb4tsk/pdb |
| Descriptor | Ketol-acid reductoisomerase, MAGNESIUM ION, L(+)-TARTARIC ACID, ... (5 entities in total) |
| Functional Keywords | ketol-acid reductoisomerase, rossmann fold, nadph-binding, oxidoreductase, isomerase |
| Biological source | Alicyclobacillus acidocaldarius subsp. acidocaldarius |
| Total number of polymer chains | 1 |
| Total formula weight | 39753.53 |
| Authors | Cahn, J.K.B.,Brinkmann-Chen, S.,Arnold, F.H. (deposition date: 2014-06-18, release date: 2014-07-09, Last modification date: 2023-09-27) |
| Primary citation | Brinkmann-Chen, S.,Cahn, J.K.,Arnold, F.H. Uncovering rare NADH-preferring ketol-acid reductoisomerases. Metab. Eng., 26C:17-22, 2014 Cited by PubMed Abstract: All members of the ketol-acid reductoisomerase (KARI) enzyme family characterized to date have been shown to prefer the nicotinamide adenine dinucleotide phosphate hydride (NADPH) cofactor to nicotinamide adenine dinucleotide hydride (NADH). However, KARIs with the reversed cofactor preference are desirable for industrial applications, including anaerobic fermentation to produce branched-chain amino acids. By applying insights gained from structural and engineering studies of this enzyme family to a comprehensive multiple sequence alignment of KARIs, we identified putative NADH-utilizing KARIs and characterized eight whose catalytic efficiencies using NADH were equal to or greater than NADPH. These are the first naturally NADH-preferring KARIs reported and demonstrate that this property has evolved independently multiple times, using strategies unlike those used previously in the laboratory to engineer a KARI cofactor switch. PubMed: 25172159DOI: 10.1016/j.ymben.2014.08.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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