759-05-7Relevant articles and documents
Chemoenzymatic Production of Enantiocomplementary 2-Substituted 3-Hydroxycarboxylic Acids from l-α-Amino Acids
Pickl, Mathias,Marín-Valls, Roser,Joglar, Jesús,Bujons, Jordi,Clapés, Pere
, p. 2866 - 2876 (2021/04/14)
A two-enzyme cascade reaction plus in situ oxidative decarboxylation for the transformation of readily available canonical and non-canonical l-α-amino acids into 2-substituted 3-hydroxycarboxylic acid derivatives is described. The biocatalytic cascade consisted of an oxidative deamination of l-α-amino acids by an l-α-amino acid deaminase from Cosenzaea myxofaciens, rendering 2-oxoacid intermediates, with an ensuing aldol addition reaction to formaldehyde, catalyzed by metal-dependent (R)- or (S)-selective carboligases namely 2-oxo-3-deoxy-l-rhamnonate aldolase (YfaU) and ketopantoate hydroxymethyltransferase (KPHMT), respectively, furnishing 3-substituted 4-hydroxy-2-oxoacids. The overall substrate conversion was optimized by balancing biocatalyst loading and amino acid and formaldehyde concentrations, yielding 36–98% aldol adduct formation and 91–98% ee for each enantiomer. Subsequent in situ follow-up chemistry via hydrogen peroxide-driven oxidative decarboxylation afforded the corresponding 2-substituted 3-hydroxycarboxylic acid derivatives. (Figure presented.).
Exploration of Transaminase Diversity for the Oxidative Conversion of Natural Amino Acids into 2-Ketoacids and High-Value Chemicals
Chen, Yanchun,Cui, Xuexian,Cui, Yinglu,Li, Chuijian,Li, Ruifeng,Li, Tao,Sun, Jinyuan,Wu, Bian,Zhu, Tong
, p. 7950 - 7957 (2020/08/21)
The use of 2-ketoacids is very common in feeds, food additives, and pharmaceuticals, and 2-ketoacids are valuable precursors for a plethora of chemically diverse compounds. Biocatalytic synthesis of 2-ketoacids starting from l-amino acids would be highly desirable because the substrates are readily available from biomass feedstock. Here, we report bioinformatic exploration of a series of aminotransferases (ATs) to achieve the desired conversion. Thermodynamic control was achieved by coupling an l-glutamate oxidation reaction in the cascade for the recycling of the amine acceptor. These enzymes were able to convert a majority of proteinogenic amino acids into the corresponding 2-ketoacids with high conversion (up to 99percent) and atom-efficiency. Furthermore, this enzyme cascade was extendable, and one-pot two-step processes were established for the synthesis of d-amino acids and N-methylated amino acids, achieving great overall conversion (up to 99percent) and high ee values (>99percent). These developed enzymatic methodologies offer convenient routes for utilizing amino acids as synthetic reagents.
Synthesis method of 2-(9H-fluorene-9-methoxycarbonylamino)-3-methyl-2-butenoic acid
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Paragraph 0006; 0009, (2020/12/30)
The invention relates to a synthesis method of 2-(9H-fluorene-9-methoxycarbonylamino)-3-methyl-2-butenoic acid. The method mainly solves the technical problem of lack of an amplified production methodof 2-(9H-fluorene-9-methoxycarbonylamino)-3-methyl-2-butenoic acid at present. The synthesis method comprises the following steps: in methyl tert-butyl ether cooled in an ice bath, acidifying 3-methyl-2-oxobutyrate with concentrated hydrochloric acid to generate a compound 1; in methylbenzene subjected to heating reflux, the compound 1 and fluorenylmethoxycarbonylamide are subjected to dehydration condensation reaction under the catalytic action of p-toluenesulfonic acid to generate a target compound 2. As a medical intermediate and a dehydroamino acid derivative, 2-(9H-fluorene-9-methoxycarbonylamino)-3-methyl-2-butenoic acid is widely applied to the fields of synthesis of peptide active substances and protein engineering.