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6RZ2

SalL with Chloroadenosine

Summary for 6RZ2
Entry DOI10.2210/pdb6rz2/pdb
DescriptorAdenosyl-chloride synthase, 5'-CHLORO-5'-DEOXYADENOSINE (3 entities in total)
Functional Keywordssall, chloroadenosine, chlorinase, transferase
Biological sourceSalinispora tropica CNB-440
Total number of polymer chains3
Total formula weight91382.83
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 citationMcKean, 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: 31573135
DOI: 10.1002/anie.201908681
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.77 Å)
Structure validation

243083

数据于2025-10-15公开中

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