94781-50-7Relevant articles and documents
Selective oxidation of alcohol-d1to aldehyde-d1using MnO2
Kitsuwa, Kohei,Kumadaki, Katsushi,Nakayama, Atsushi,Okamura, Hironori,Ozawa, Keita,Shinada, Tetsuro,Tamura, Yusaku,Yamamoto, Yuki,Yasuno, Yoko
, p. 28530 - 28534 (2021/09/22)
The selective oxidation of alcohol-d1to prepare aldehyde-d1was newly developed by means of NaBD4reduction/activated MnO2oxidation. Various aldehyde-d1derivatives including aromatic and unsaturated ald
Phenylalanine ammonia lyase catalyzed synthesis of amino acids by an MIO-cofactor independent pathway
Lovelock, Sarah L.,Lloyd, Richard C.,Turner, Nicholas J.
supporting information, p. 4652 - 4656 (2014/05/20)
Phenylalanine ammonia lyases (PALs) belong to a family of 4-methylideneimidazole-5-one (MIO) cofactor dependent enzymes which are responsible for the conversion of L-phenylalanine into trans-cinnamic acid in eukaryotic and prokaryotic organisms. Under conditions of high ammonia concentration, this deamination reaction is reversible and hence there is considerable interest in the development of PALs as biocatalysts for the enantioselective synthesis of non-natural amino acids. Herein the discovery of a previously unobserved competing MIO-independent reaction pathway, which proceeds in a non-stereoselective manner and results in the generation of both L- and D-phenylalanine derivatives, is described. The mechanism of the MIO-independent pathway is explored through isotopic-labeling studies and mutagenesis of key active-site residues. The results obtained are consistent with amino acid deamination occurring by a stepwise E1cB elimination mechanism. All manner of things: A competing MIO-independent (MIO=4-methylideneimidazole-5-one) reaction pathway has been identified for phenylalanine ammonia lyases (PALs), which proceeds in a non-stereoselective manner, resulting in the generation of D-phenylalanine derivatives. The mechanism of D-amino acid formation is explored through isotopic-labeling studies and mutagenesis of key active-site residues.
A new interpretation of the Baylis-Hillman mechanism
Price, Kristin E.,Broadwater, Steven J.,Walker, Brian J.,McQuade, D. Tyler
, p. 3980 - 3987 (2007/10/03)
On the basis of reaction rate data, we have proposed a new mechanism for the Baylis-Hillman reaction involving the formation of a hemiacetal intermediate. We have determined that the rate-determining step is second order in aldehyde and first order in DAB