6RYZ
SalL with S-adenosyl methionine
Summary for 6RYZ
| Entry DOI | 10.2210/pdb6ryz/pdb |
| Descriptor | Adenosyl-chloride synthase, S-ADENOSYLMETHIONINE, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | sall, s-adenosyl methionine, chlorinase, transferase |
| Biological source | Salinispora tropica CNB-440 |
| Total number of polymer chains | 3 |
| Total formula weight | 91951.57 |
| Authors | McKean, I.,Frese, A.,Cuetos, A.,Burley, G.,Grogan, G. (deposition date: 2019-06-12, release date: 2020-04-15, Last modification date: 2024-01-24) |
| Primary citation | McKean, I.J.W.,Sadler, J.C.,Cuetos, A.,Frese, A.,Humphreys, L.D.,Grogan, G.,Hoskisson, P.A.,Burley, G.A. S-Adenosyl Methionine Cofactor Modifications Enhance the Biocatalytic Repertoire of Small Molecule C-Alkylation. Angew.Chem.Int.Ed.Engl., 58:17583-17588, 2019 Cited by PubMed Abstract: A tandem enzymatic strategy to enhance the scope of C-alkylation of small molecules via the in situ formation of S-adenosyl methionine (SAM) cofactor analogues is described. A solvent-exposed channel present in the SAM-forming enzyme SalL tolerates 5'-chloro-5'-deoxyadenosine (ClDA) analogues modified at the 2-position of the adenine nucleobase. Coupling SalL-catalyzed cofactor production with C-(m)ethyl transfer to coumarin substrates catalyzed by the methyltransferase (MTase) NovO forms C-(m)ethylated coumarins in superior yield and greater substrate scope relative to that obtained using cofactors lacking nucleobase modifications. Establishing the molecular determinants that influence C-alkylation provides the basis to develop a late-stage enzymatic platform for the preparation of high value small molecules. PubMed: 31573135DOI: 10.1002/anie.201908681 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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