Isotopes in Environmental and Health Studies 2010-06-01

Enzymatic synthesis of some (15)N-labelled L-amino acids.

Maria Chiriac, Iulia Lupan, Flavia Popa, Nicolae Palibroda, Octavian Popescu

Index: Isotopes Environ. Health Stud. 46(2) , 249-54, (2010)

Full Text: HTML

Abstract

Our group has developed a stereospecific enzymatic method, which is very efficient for the in vitro synthesis of l-[(15)N]serine, l-[(15)N]methionine and l-[(15)N]glutamic acid. These amino acids were prepared from the corresponding alpha -ketoacids in the suitable enzymatic systems. The bacterial NAD-dependent amino acid dehydrogenases alanin dehydrogenase, leucin dehydrogenase and glutamate dehydrogenase were used as catalysts. Glucose dehydrogenase was used for the regeneration of NADH and (15)NH(4)Cl as isotopically labelled material at 99 at.% (15)N. All reactions are inexpensive and easy to perform on a synthetically useful scale (1-10g) giving high yields of l-amino acids. The (15)N isotope content was determined by mass spectrometry.


Related Compounds

Related Articles:

An efficient and selective enzymatic oxidation system for the synthesis of enantiomerically pure D-tert-leucine.

2003-10-02

[Org. Lett. 5(20) , 3649-50, (2003)]

Foot odor due to microbial metabolism and its control.

2006-04-01

[Can. J. Microbiol. 52(4) , 357-64, (2006)]

Investigation of mathematical methods for efficient optimisation of aqueous two-phase extraction.

2000-06-23

[J. Chromatogr. B. Biomed. Sci. Appl. 743(1-2) , 21-30, (2000)]

Investigating expression systems for the stable large-scale production of recombinant L-leucine-dehydrogenase from Bacillus cereus in Escherichia coli.

2000-06-01

[Appl. Microbiol. Biotechnol. 53(6) , 668-73, (2000)]

Production of recombinant L-leucine dehydrogenase from Bacillus cereus in pilot scale using the runaway replication system E. coli[pIET98].

2000-06-05

[Biotechnol. Bioeng. 68(5) , 557-62, (2000)]

More Articles...