71-00-1Relevant articles and documents
An unprecedented trans-oriented product from the cleavage of a dipeptide.
Saha, Manas K,Bernal, Ivan
, p. 612 - 613 (2003)
An unusual trans cleavage reaction was observed when trans-[Co(3,2,3-tet)Cl2]Cl (3,2,3-tet = N,N'-bis(3-aminopropyl)ethylenediamine), was allowed to react with beta-alanyl-L-histidine (a bioactive dipeptide) in an aqueous medium at pH approximately 7.5 and 45 degrees C for 6 h.
Fluorinated S-Adenosylmethionine as a Reagent for Enzyme-Catalyzed Fluoromethylation
Bauer, Carsten,Liao, Cangsong,Peng, Jiaming,Seebeck, Florian P.
, p. 27178 - 27183 (2021/11/16)
Strategic replacement of protons with fluorine atoms or functional groups with fluorine-containing fragments has proven a powerful strategy to optimize the activity of therapeutic compounds. For this reason, the synthetic chemistry of organofluorides has been the subject of intense development and innovation for many years. By comparison, the literature on fluorine biocatalysis still makes for a slim chapter. Herein we introduce S-adenosylmethionine (SAM) dependent methyltransferases as a new tool for the production of fluorinated compounds. We demonstrate the ability of halide methyltransferases to form fluorinated SAM (S-adenosyl-S-(fluoromethyl)-L-homocysteine) from S-adenosylhomocysteine and fluoromethyliodide. Fluorinated SAM (F-SAM) is too unstable for isolation, but is accepted as a substrate by C-, N- and O-specific methyltransferases for enzyme-catalyzed fluoromethylation of small molecules.
Safe and Effective Method of Treating Ulcerative Colitis with Anti-IL12/IL23 Antibody
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, (2020/04/10)
Described are methods and compositions for clinical proven safe and effective treatment of ulcerative colitis, particularly moderately to severely active ulcerative colitis in patients who have had an inadequate response to or are intolerant of a conventional or existing therapy by intravenous and/or subcutaneous administration of an anti-IL-12/IL-23p40 antibody.
A green-by-design bioprocess for l-carnosine production integrating enzymatic synthesis with membrane separation
Yin, Dong-Ya,Pan, Jiang,Zhu, Jie,Liu, You-Yan,Xu, Jian-He
, p. 5971 - 5978 (2019/11/14)
l-Carnosine (l-Car, β-alanyl-l-histidine) is a bioactive dipeptide with important physiological functions. Direct coupling of unprotected β-Ala (β-alanine) with l-His (l-histidine) mediated by an enzyme is a promising method for l-Car synthesis. In this study, a new recombinant dipeptidase (SmPepD) from Serratia marcescens with a high synthetic activity toward l-Car was identified by a genome mining approach and successfully expressed in Escherichia coli. Divalent metal ions strongly promoted the synthetic activity of SmPepD, with up to 21.7-fold increase of activity in the presence of 0.1 mM MnCl2. Higher temperature, lower pH and increasing substrate loadings facilitated the l-Car synthesis. Pilot biocatalytic syntheses of l-Car were performed comparatively in batch and continuous modes. In the continuous process, an ultra-filtration membrane reactor with a working volume of 5 L was employed for catalyst retention. The dipeptidase, SmPepD, showed excellent operational stability without a significant decrease in space-time yield after 4 days. The specific yield of l-Car achieved was 105 gCar gcatalyst-1 by the continuous process and 30.1 gCar gcatalyst-1 by the batch process. A nanofiltration membrane was used to isolate the desired product l-Car from the reaction mixture by selectively removing the excess substrates, β-Ala and l-His. As a result, the final l-Car content was effectively enriched from 2.3% to above 95%, which gave l-Car in 99% purity after ethanol precipitation with a total yield of 60.2%. The recovered substrate mixture of β-Ala and l-His can be easily reused, which will enable the economically attractive and environmentally benign production of the dipeptide l-Car.