35455-20-0Relevant articles and documents
A new and simple method of resolution. Preparation of 3-fluoro-D-alanine-2-d.
Gal,Chemerda,Reinhold,Purick
, p. 142 - 143 (1977)
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ω-Transaminase-catalyzed asymmetric synthesis of unnatural amino acids using isopropylamine as an amino donor
Park, Eul-Soo,Dong, Joo-Young,Shin, Jong-Shik
, p. 6929 - 6933 (2013/10/08)
Isopropylamine is an ideal amino donor for reductive amination of carbonyl compounds by ω-transaminase (ω-TA) owing to its cheapness and high volatility of a ketone product. Here we developed asymmetric synthesis of unnatural amino acids via ω-TA-catalyzed amino group transfer between α-keto acids and isopropylamine.
Thermodynamics and kinetic aspects involved in the enzymatic resolution of (R,S)-3-fluoroalanine in a coupled system of redox reactions catalyzed by dehydrogenases
Goncalves, Luciana P. B.,Antunes,Oestreicher, Enrique G.
, p. 673 - 677 (2012/12/22)
Two systems of redox enzymatic reactions were tested, looking forward to the preparation of (S)-3-fluoroalanine, a potent antibiotic, by kinetic resolution of rac-3-fluoroalanine. This starting material was the main substrate for the deaminative oxidation reaction catalyzed by L-alanine dehydrogenase (L-AlaDH) in the presence of NAD+. One system was formed by coupling this reaction (main reaction) to the reduction of 3-fluoropyruvate (a cascade system) produced in the main reaction catalyzed by L-lactate dehydrogenase (L-LDH) in the presence of NADH, also formed in the main reaction. This system, that was able to achieve 92% of conversion, allows the accumulation of NH 4+, one of the secondary products of the main reaction. The other coupled redox system involved the coupling to the L-AlaDH reaction to the aminative reduction reaction of α-ketoglutarate in the presence of NADH and NH4+ (both side products of the main reaction) catalyzed by L-glutamate dehydrogenase (L-GluDH), that allows accumulation of 3-fluoropyruvate. With this system, the extent of the reaction in the coupled system was only 22%. This big difference in the efficiency of both systems was identified as being the result of a different potency of the products that accumulates in both systems, acting as inhibitors of L-AlaDH. It was demonstrated that 3-fluoropyruvate is a much stronger inhibitor of L-AlaDH than NH4+. This fact, and not thermodynamic considerations, explains the results obtained with both systems.
Simultaneous enzymatic synthesis of (S)-3-fluoroalanine and (R)-3-fluorolactic acid
Goncalves,Antunes,Pinto,Oestreicher
, p. 1465 - 1468 (2007/10/03)
A coupled enzymatic system for the simultaneous synthesis of (S)-3-fluoroalanine (1a) and (R)-3-fluorolactic acid (3) with L-alanine dehydrogenase (L-AlaDH) from Bacillus subtilis and rabbit muscle L-lactate dehydrogenase (L-LDH) using rac-1 and NAD+ is described. Analysis of isolated products of the laboratory preparative scale process revealed 1a in 60% yield and 88% ee and 3 in 80% yield and over 99% ee. The compounds 1a and 3 represent chiral building blocks for the synthesis of several products with pharmacological activity. Copyright (C) 2000 Elsevier Science Ltd.