77977-73-2Relevant academic research and scientific papers
Oxalyl-CoA Decarboxylase Enables Nucleophilic One-Carbon Extension of Aldehydes to Chiral α-Hydroxy Acids
Burgener, Simon,Cortina, Ni?a Socorro,Erb, Tobias J.
supporting information, p. 5526 - 5530 (2020/02/20)
The synthesis of complex molecules from simple, renewable carbon units is the goal of a sustainable economy. Here we explored the biocatalytic potential of the thiamine-diphosphate-dependent (ThDP) oxalyl-CoA decarboxylase (OXC)/2-hydroxyacyl-CoA lyase (HACL) superfamily that naturally catalyzes the shortening of acyl-CoA thioester substrates through the release of the C1-unit formyl-CoA. We show that the OXC/HACL superfamily contains promiscuous members that can be reversed to perform nucleophilic C1-extensions of various aldehydes to yield the corresponding 2-hydroxyacyl-CoA thioesters. We improved the catalytic properties of Methylorubrum extorquens OXC by rational enzyme engineering and combined it with two newly described enzymes—a specific oxalyl-CoA synthetase and a 2-hydroxyacyl-CoA thioesterase. This enzymatic cascade enabled continuous conversion of oxalate and aromatic aldehydes into valuable (S)-α-hydroxy acids with enantiomeric excess up to 99 %.
Semisynthetic cephalosporins. Synthesis and structure activity relationships of 7 mandelamido 3 cephem 4 carboxylic acids
Hoover,Dunn,Jakas,Lam,Taggart,Guarini,Phillips
, p. 34 - 41 (2007/10/06)
The synthesis, microbiological profile, and in vivo effectiveness in laboratory animals of a broad spectrum cephalosporin, 7(R) mandelamidocephalosporanic acid (1), are described. A number of derivatives and analogs of 1 were prepared and their structure activity relationships are discussed.
