ChemInform Abstract: ELECTROCHEMICAL SYNTHESIS OF AMINO ACIDS BY REDUCTIVE AMINATION OF KETO ACIDS. I. REDUCTION AT MERCURY ELECTRODES

1978 ◽  
Vol 9 (15) ◽  
Author(s):  
E. A. JEFFERY ◽  
A. MEISTERS
Keyword(s):  
Amino Acids ◽  
Electrochemical Synthesis ◽  
Reductive Amination ◽  
Keto Acids ◽  
Mercury Electrodes

Electrochemical synthesis of amino acids by reductive amination of keto acids. I. Reduction at mercury electrodes

1978 ◽  
Vol 31 (1) ◽  
pp. 73 ◽  
Author(s):  
EA Jeffery ◽  
A Meisters
Keyword(s):  
Reductive Amination ◽  
Phenylacetic Acid ◽  
Reduction Potential ◽  
Aqueous Ammonia ◽  
Saturated Calomel Electrode ◽  
Mercury Electrode ◽  
Ammonia Concentration ◽  
Initial Current ◽  
Keto Acids ◽  
Mercury Electrodes

Racemic 2-amino-2-phenylacetic acid, monoammonium glutamate, 2-aminobutyric acid, α-alanine and ammonium 5-amino-5-phenylvalerate have been prepared by electrochemical reductive amination of the corresponding keto acids in aqueous ammonia/ammonium chloride solution at a mercury electrode. The yields ranged from 24% for ammonium 5-amino-5-phenylvalerate to 88% for 2-amino-2-phenylacetic acid. The current efficiency and yield of 2-amino-2-phenylacetic acid from reductive amination of 2-oxo-2-phenylacetic acid increased with increase in ammonia concentration. Also, decreasing the reduction potential from -1.10 to -1.30 V (with respect to a saturated calomel electrode) in 2 M ammonia raised the initial current density from c. 2 mA/cm2 to c. 7 mA/cm2 but halved the yield of 2-amino-2-phenylacetic acid.

Development of β-Amino Acid Dehydrogenase for the Synthesis of β-Amino Acids via Reductive Amination of β-Keto Acids

ACS Catalysis ◽  
2015 ◽  
Vol 5 (4) ◽  
pp. 2220-2224 ◽  
Author(s):  
Dalong Zhang ◽  
Xi Chen ◽  
Rui Zhang ◽  
Peiyuan Yao ◽  
Qiaqing Wu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Reductive Amination ◽  
Acid Dehydrogenase ◽  
Amino Acid Dehydrogenase ◽  
Keto Acids

scholarly journals Electrochemical Molecular Conversion of α-Keto Acid to Amino Acid at a Low Overpotential Using a Nanoporous Gold Catalyst

2021 ◽  
Vol 22 (17) ◽  
pp. 9442
Author(s):  
Yasuhiro Mie ◽  
Shizuka Katagai ◽  
Chitose Mikami
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Gold Electrode ◽  
Reductive Amination ◽  
Gold Catalyst ◽  
Nanoporous Gold ◽  
Keto Acid ◽  
Applied Potential ◽  
Keto Acids ◽  
Optimized Conditions

A nanoporous gold (NPG) electrode prepared through a facile anodization technique was employed in the electrochemical reductive amination of biomass-derivable α-keto acids in the presence of a nitrogen source to produce the corresponding amino acids. NPG showed a clear reductive current in the presence of α-keto acid and NH2OH, and the electrolysis experiments confirmed the production of L-amino acid. A reductive voltammetric signal at the NPG electrode appeared at a more positive potential by 0.18–0.79 V, compared with those at the planar-gold electrode without anodization and other previously reported electrode systems, indicating the high activity of the prepared nanostructure for the electrochemical reaction. Maximum Faradaic efficiencies (FEs) of 74–93% in the reductive molecular conversion to amino acids of Ala, Asp, Glu, Gly, and Leu were obtained under the optimized conditions. The FE values were strongly dependent on the applied potential in the electrolysis, suggesting that the hydrogen evolution reaction at the electrode surface was more significant as the applied potential became more negative. The effect of potential at the NPG was lower than that at the planar-gold electrode. These results indicate that nanostructurization decreases the overpotential for the electrochemical reductive amination, resulting in high FE.

Enantioselective Reductive Amination of α-Keto Acids to α-Amino Acids by a Pyridoxamine Cofactor in a Protein Cavity

1996 ◽  
Vol 118 (44) ◽  
pp. 10702-10706 ◽  
Author(s):  
Hao Kuang ◽  
Matthew L. Brown ◽  
Ronald R. Davies ◽  
Eva C. Young ◽  
Mark D. Distefano
Keyword(s):  
Amino Acids ◽  
Reductive Amination ◽  
Keto Acids ◽  
Protein Cavity

scholarly journals ω-Amino Acid:Pyruvate Transaminase from Alcaligenes denitrificans Y2k-2: a New Catalyst for Kinetic Resolution of β-Amino Acids and Amines

2004 ◽  
Vol 70 (4) ◽  
pp. 2529-2534 ◽  
Author(s):  
Hyungdon Yun ◽  
Seongyop Lim ◽  
Byung-Kwan Cho ◽  
Byung-Gee Kim
Keyword(s):  
Amino Acids ◽  
Kinetic Resolution ◽  
Specific Activity ◽  
Expression System ◽  
Enantiomeric Excess ◽  
Selective Enrichment ◽  
Alcaligenes Denitrificans ◽  
Keto Acids ◽  
Optically Pure ◽  
High Stereoselectivity

ABSTRACT Alcaligenes denitrificans Y2k-2 was obtained by selective enrichment followed by screening from soil samples, which showed ω-amino acid:pyruvate transaminase activity, to kinetically resolve aliphatic β-amino acid, and the corresponding structural gene (aptA) was cloned. The gene was functionally expressed in Escherichia coli BL21 by using an isopropyl-β-d-thiogalactopyranoside (IPTG)-inducible pET expression system (9.6 U/mg), and the recombinant AptA was purified to show a specific activity of 77.2 U/mg for l-β-amino-n-butyric acid (l-β-ABA). The enzyme converts various β-amino acids and amines to the corresponding β-keto acids and ketones by using pyruvate as an amine acceptor. The apparent Km and V max for l-β-ABA were 56 mM and 500 U/mg, respectively, in the presence of 10 mM pyruvate. In the presence of 10 mM l-β-ABA, the apparent Km and V max for pyruvate were 11 mM and 370 U/mg, respectively. The enzyme exhibits high stereoselectivity (E > 80) in the kinetic resolution of 50 mM d,l-β-ABA, producing optically pure d-β-ABA (99% enantiomeric excess) with 53% conversion.

Sign in / Sign up

Export Citation Format

Share Document