7POC
An Irreversible, Promiscuous and Highly Thermostable Claisen-Condensation Biocatalyst Drives the Synthesis of Substituted Pyrroles
Summary for 7POC
| Entry DOI | 10.2210/pdb7poc/pdb |
| Descriptor | 8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate coenzyme A ligase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total) |
| Functional Keywords | biocatalyst, cascade, chemo-enzymatic, thermophilic, promiscuous, alpha-oxoamine synthase, pyrrole, synthase |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 4 |
| Total formula weight | 187329.15 |
| Authors | Basle, A.,Ashley, B.,Campopiano, D.,Marles-Wright, J. (deposition date: 2021-09-08, release date: 2022-09-21, Last modification date: 2024-02-28) |
| Primary citation | Ashley, B.,Basle, A.,Sajjad, M.,El Ashram, A.,Kelis, P.,Marles-Wright, J.,Campopiano, D.J. Versatile Chemo-Biocatalytic Cascade Driven by a Thermophilic and Irreversible C-C Bond-Forming alpha-Oxoamine Synthase. Acs Sustain Chem Eng, 11:7997-8002, 2023 Cited by PubMed Abstract: We report a chemo-biocatalytic cascade for the synthesis of substituted pyrroles, driven by the action of an irreversible, thermostable, pyridoxal 5'-phosphate (PLP)-dependent, C-C bond-forming biocatalyst (AOS). The AOS catalyzes the Claisen-like condensation between various amino acids and acyl-CoA substrates to generate a range of α-aminoketones. These products are reacted with β-keto esters in an irreversible Knorr pyrrole reaction. The determination of the 1.6 Å resolution crystal structure of the PLP-bound form of AOS lays the foundation for future engineering and directed evolution. This report establishes the AOS family as useful and versatile C-C bond-forming biocatalysts. PubMed: 37266354DOI: 10.1021/acssuschemeng.3c00243 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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