On November 21, 2013, Teufel, Robin; Miyanaga, Akimasa; Michaudel, Quentin; Stull, Frederick; Louie, Gordon; Noel, Joseph P.; Baran, Phil S.; Palfey, Bruce; Moore, Bradley S. published an article.Category: esters-buliding-blocks The title of the article was Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement. And the article contained the following:
Flavoproteins catalyze a diversity of fundamental redox reactions and are one of the most studied enzyme families. As monooxygenases, they are universally thought to control oxygenation by means of a peroxyflavin species that transfers a single atom of mol. oxygen to an organic substrate. Here it is reported that the bacterial flavoenzyme EncM catalyzes the peroxyflavin-independent oxygenation-dehydrogenation dual oxidation of a highly reactive poly(β-carbonyl). The crystal structure of EncM with bound substrate mimics and isotope labeling studies reveal previously unknown flavin redox biochem. It is shown that EncM maintains an unexpected stable flavin-oxygenating species, proposed to be a flavin-N5-oxide, to promote substrate oxidation and trigger a rare Favorskii-type rearrangement that is central to the biosynthesis of the antibiotic enterocin. This work provides new insight into the fine-tuning of the flavin cofactor in off-setting the innate reactivity of a polyketide substrate to direct its efficient electrocyclization. The experimental process involved the reaction of (R)-Methyl 3-hydroxybutanoate(cas: 3976-69-0).Category: esters-buliding-blocks
The Article related to flavin dependent oxidation encm enzymic favorskii rearrangement mechanism, crystal structure flavin dependent monooxygenase encm substrate analog complex, Enzymes: Kinetics-Mechanism-Enzyme and Coenzyme Models and other aspects.Category: esters-buliding-blocks
Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics