21017-05-0Relevant articles and documents
Studies of phosphorylation. II. Reaction of 2',3'-O-isopropylideneinosine and -guanosine with phosphoryl chloride.
Kusashio,Yoshikawa
, p. 142 - 149 (1968)
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S-Adenosyl Methionine Cofactor Modifications Enhance the Biocatalytic Repertoire of Small Molecule C-Alkylation
McKean, Iain J. W.,Sadler, Joanna C.,Cuetos, Anibal,Frese, Amina,Humphreys, Luke D.,Grogan, Gideon,Hoskisson, Paul A.,Burley, Glenn A.
supporting information, p. 17583 - 17588 (2019/11/11)
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.
The fluorinase from Streptomyces cattleya is also a chlorinase
Deng, Hai,Cobb, Steven L.,McEwan, Andrew R.,McGlinchey, Ryan P.,Naismith, James H.,O'Hagan, David,Robinson, David A.,Spencer, Jonathan B.
, p. 759 - 762 (2007/10/03)
(Chemical Equation Presented) Choices choices: The fluorinase enzyme from Streptomyces cattleya (catalyzes the formation of a C-F bond from fluoride ions) also has the capacity to utilize a chloride ion although it has a clear preference for the fluoride ion. The enzyme mediates a nucleophilic chlorination reaction, which is an unusual mechanism for enzymatic chlorination.