6RYZ

SalL with S-adenosyl methionine

6RYZ の概要

• エントリーDOI: 10.2210/pdb6ryz/pdb
• 分子名称: Adenosyl-chloride synthase, S-ADENOSYLMETHIONINE, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: sall, s-adenosyl methionine, chlorinase, transferase
• 由来する生物種: Salinispora tropica CNB-440
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 91951.57

構造登録者

McKean, I.,Frese, A.,Cuetos, A.,Burley, G.,Grogan, G. (登録日: 2019-06-12, 公開日: 2020-04-15, 最終更新日: 2024-01-24)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.5 Å)