When a brown powder of 2a was dissolved in acetonitrile, 2a was converted to 2b. Equilibrium was reached at a 74:26 molar ratio within 1 week at 303 K. The isomerization proceeds through a cubane-like transition state, in which recombination of a carbon-carbon bond occurs.
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http://dx.doi.org/10.1021/ja809540w | DOI Listing |
Acta Pharm
December 2024
University Ss Cyril and Methodius in Skopje Faculty of Pharmacy, Institute of Pharmaceutical Chemistry 1000 Skopje Republic of North Macedonia.
AKR1D1, a key enzyme in the aldo-keto reductase superfamily, plays a dual role in both steroid metabolism and bile acid synthesis by catalyzing the NADPH-dependent reduction of carbon-carbon double bonds, specifically converting 3-ketosteroid hormones into 5β-steroids. Positioned at the critical intersection of steroid hormone and bile acid metabolism, AKR1D1 has the potential to profoundly influence metabolic homeostasis and drug metabolism. Despite its importance, the enzyme's therapeutic implications and role in drug metabolism remain underexplored.
View Article and Find Full Text PDFMethods Enzymol
November 2024
Department of Inflammation and Immunity, Lerner Research Institute, Cleveland Clinic Lerner College of Medicine at CWRU, Cleveland, OH, United States.
The gamma-glutamyl carboxylase (GGCX) generates clusters of carboxylated glutamic acid residues in vitamin K-dependent (VKD) proteins, which is required for their diverse functions including hemostasis and regulation of calcification. The GGCX modifies a VKD protein using several substrates and cofactors, and has regulatory mechanisms like processivity that ensures full carboxylation of VKD proteins. The GGCX mechanism is incompletely understood.
View Article and Find Full Text PDFMethods Enzymol
November 2024
Department of Biological Sciences, Marquette University, Milwaukee, WI, United States.
Biotin-dependent carboxylases catalyze the MgATP- and bicarbonate-dependent carboxylation of various acceptor substrates through a two-step carboxylation reaction. Biotin-dependent carboxylases play an essential role in the metabolism of key biomolecules and, therefore, they are the subject of ongoing drug discovery efforts, as well as of studies seeking to better characterize their structure and function. It has been an ongoing challenge to obtain high yields of mammalian biotin-dependent carboxylases for in vitro experimentation; these enzymes have not been successfully purified when recombinantly expressed from a bacterial expression host and only low yields of these recombinant, vertebrate enzymes have been obtained through expression in cell culture systems.
View Article and Find Full Text PDFNanoscale
November 2024
Department of Chemical and Biomolecular Engineering, KAIST Institute for the Nanocentury, Energy and Environmental Research Center (EERC), Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Korea.
Achieving high selectivity towards hydrobenzoin (HB) from photocatalytic carbon-carbon (C-C) coupling reaction of benzyl alcohol (BzOH) remains a challenge due to side competing reactions and subsequent conversions of HB into its derivatives. In this study, we have developed a high-performance CdS-based photocatalyst for synthesizing HB with precisely controlled surface properties and structure, achieving high selectivity for HB synthesis. We employed strategies such as cysteamine passivation and Pt deposition to address issues related to photogenerated charge trapping and recombination, thereby enhancing the photocatalytic capability of CdS.
View Article and Find Full Text PDFMethods Enzymol
September 2024
Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA, United States. Electronic address:
Kainoid natural products are a series of potent ionotropic glutamate receptor agonists produced by a variety of divergent marine micro- and macro-algae. The key biosynthetic step in the construction of the pyrrolidine ring pharmacophore involves a unique branch of non-heme iron α-ketoglutarate dependent dioxygenases (Fe/αKGs) termed the kainoid synthases. These Fe/αKG homologs catalyze a stereoselective C-H abstraction followed by a radical carbon-carbon bond reaction to form the bioactive core on N-prenylated L-glutamic acid substrates.
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