6KQB
A long chain secondary alcohol dehydrogenase of Micrococcus luteus
Summary for 6KQB
| Entry DOI | 10.2210/pdb6kqb/pdb |
| Related | 6KQ9 |
| Descriptor | 3-hydroxybutyryl-CoA dehydrogenase (2 entities in total) |
| Functional Keywords | alcohol dehydrogenase, oxidoreductase |
| Biological source | Micrococcus luteus |
| Total number of polymer chains | 2 |
| Total formula weight | 73715.62 |
| Authors | |
| Primary citation | Seo, E.J.,Kim, H.J.,Kim, M.J.,Kim, J.S.,Park, J.B. Cofactor specificity engineering of a long-chain secondary alcohol dehydrogenase from Micrococcus luteus for redox-neutral biotransformation of fatty acids. Chem.Commun.(Camb.), 55:14462-14465, 2019 Cited by PubMed Abstract: Structure-based engineering of a NAD+-dependent secondary alcohol dehydrogenase from Micrococcus luteus led to a 1800-fold increase in catalytic efficiency for NADP+. Furthermore, the engineered enzymes (e.g., D37S/A38R/V39S/T15I) were successfully coupled to a NADPH-dependent Baeyer-Villiger monooxygenase from Pseudomonas putida KT2440 for redox-neutral biotransformations of C18 fatty acids into C9 chemicals. PubMed: 31728457DOI: 10.1039/c9cc06447h PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.261 Å) |
Structure validation
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