126434-65-9Relevant articles and documents
Spontaneous Nanobelt Formation by Self-Assembly of β-Benzyl GABA
Jeon, Aram,Gong, Jintaek,Oh, Jun Kyun,Kwon, Sunbum,Lee, Wonchul,Kim, Sang Ouk,Cho, Sung June,Lee, Hee-Seung
, p. 1945 - 1948 (2019)
We present the formation of a nanobelt by self-assembly of β-benzyl GABA (γ-aminobutyric acid). This simple γ-amino acid building block self-assembled to form a well-defined nanobelt in chloroform. The nanobelt showed distinct optical properties due to π–π interactions. This new-generation self-assembled single amino acid may serve as a template for functional nanomaterials.
Type II flavin-containing monooxygenases: A new class of biocatalysts that harbors baeyer-villiger monooxygenases with a relaxed coenzyme specificity
Riebel, Anette,Fink, Michael J.,Mihovilovic, Marko D.,Fraaije, Marco W.
, p. 1112 - 1117 (2014/05/06)
Within a newly identified set of flavin-containing monooxygenases (FMOs) from Rhodococcus jostii RHA1, we have identified three monooxygenases (FMO-E, FMO-F, and FMO-G) that are effective in catalyzing Baeyer-Villiger oxidations. These type II FMOs display relaxed coenzyme specificity by accepting both NADPH (reduced form of nicotinamide adenine dinucleotide phosphate) and NADH (reduced form of nicotinamide adenine dinucleotide), as a coenzyme, which is a novel and attractive feature among biocatalysts capable of conducting Baeyer-Villiger oxidations. We purified FMO-E and determined that the Michaelis constants for both coenzymes were in the micromolar range, whereas the activity was highest for NADH. By using the stopped-flow technique, formation of a peroxyflavin-enzyme intermediate was observed, which indicated that type II FMOs follow a catalytic mechanism similar to that of other class B flavoprotein monooxygenases. A set of cyclobutanones and cyclohexanones were used to probe the regio- and enantioselectivity of all three recombinant monooxygenases. The biocatalysts readily accepted small cyclic ketones, which enabled the conversion of previously poorly accepted substrates by other monooxygenases (especially norcamphor), and exhibited excellent and unique regio- and enantioselectivities. Sequence analysis revealed that type II FMOs that act as Baeyer-Villiger monooxygenases contain a unique N-terminal domain. Sequence conservation in this protein domain can be used to identify new NADH-dependent Baeyer-Villiger monooxygenases, which would facilitate future biocatalyst discovery efforts. New kid on the block: Members of a newly recognized group of sequence-related flavin-containing monooxygenases can perform Baeyer-Villiger oxidations. Their coenzyme indifference and unique specificity make them attractive biocatalysts.
Peptide catalyzed asymmetric conjugate addition reactions of aldehydes to nitroethylene - A convenient entry into γ2-amino acids
Wiesner, Markus,Revell, Jefferson D.,Tonazzi, Sandro,Wennemers, Helma
, p. 5610 - 5611 (2008/12/22)
The peptide H-d-Pro-Pro-Glu-NH2 is a highly effective catalyst for conjugate addition reactions between aldehydes and nitroethylene. Only 1 mol % of H-d-Pro-Pro-Glu-NH2 and a 1.5-fold excess of aldehyde with respect to nitroethylene suffice to obtain γ-nitroaldehydes and, after reduction, monosubstituted γ-nitroalcohols in excellent yields and optical purities. The products can be readily converted into γ2-amino acids, thereby opening an effective direct entry into this important class of compounds. Copyright
