5CPL
The crystal structure of Xenobiotic reductase A (XenA) from Pseudomonas putida in complex with a nicotinamide mimic (mNH2)
Summary for 5CPL
| Entry DOI | 10.2210/pdb5cpl/pdb |
| Descriptor | Xenobiotic reductase, 1-benzyl-1,4,5,6-tetrahydropyridine-3-carboxamide, 1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL, ... (5 entities in total) |
| Functional Keywords | reductase, nicotinamide mimic, biomimetic, oxidoreductase |
| Biological source | Pseudomonas putida |
| Total number of polymer chains | 2 |
| Total formula weight | 83317.53 |
| Authors | Knaus, T.,Paul, C.E.,Levy, C.W.,Mutti, F.G.,Hollmann, F.,Scrutton, N.S. (deposition date: 2015-07-21, release date: 2016-01-20, Last modification date: 2024-01-10) |
| Primary citation | Knaus, T.,Paul, C.E.,Levy, C.W.,de Vries, S.,Mutti, F.G.,Hollmann, F.,Scrutton, N.S. Better than Nature: Nicotinamide Biomimetics That Outperform Natural Coenzymes. J.Am.Chem.Soc., 138:1033-1039, 2016 Cited by PubMed Abstract: The search for affordable, green biocatalytic processes is a challenge for chemicals manufacture. Redox biotransformations are potentially attractive, but they rely on unstable and expensive nicotinamide coenzymes that have prevented their widespread exploitation. Stoichiometric use of natural coenzymes is not viable economically, and the instability of these molecules hinders catalytic processes that employ coenzyme recycling. Here, we investigate the efficiency of man-made synthetic biomimetics of the natural coenzymes NAD(P)H in redox biocatalysis. Extensive studies with a range of oxidoreductases belonging to the "ene" reductase family show that these biomimetics are excellent analogues of the natural coenzymes, revealed also in crystal structures of the ene reductase XenA with selected biomimetics. In selected cases, these biomimetics outperform the natural coenzymes. "Better-than-Nature" biomimetics should find widespread application in fine and specialty chemicals production by harnessing the power of high stereo-, regio-, and chemoselective redox biocatalysts and enabling reactions under mild conditions at low cost. PubMed: 26727612DOI: 10.1021/jacs.5b12252 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.57 Å) |
Structure validation
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