Simple enzymatic procedure for preparation of 15N-labeled l-glutamic acid

Bojan, O.; Bologa, M.; Niac, Gavril; Palibroda, Nicolae; Vargha, E.; Bârzu, Octavian

doi:10.1016/0003-2697(80)90034-2

Cited by 11 publications

(3 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In some studies, racemic mixtures are useful, but if the mixture must be resolved there is either a 50% reduction in yield or the additional effort required to alter the stereochemistry. Enzymatic synthesis is an attractive alternative, and techniques have been described for the preparation of L-[15N]glutamate (1,2).…”

mentioning

confidence: 99%

Biosynthetic preparation of L-[13C]- and [15N]glutamate by Brevibacterium flavum

Walker¹,

London²

1987

Appl Environ Microbiol

View full text Add to dashboard Cite

The biosynthesis of isotopically labeled L-glutamic acid by the microorganism Brevibacterium flavum was studied with a variety of carbon-13-enriched precursors. The purpose of this study was twofold: (i) to develop techniques for the efficient preparation of labeled L-glutamate with a variety of useful labeling patterns which can be used for other metabolic studies, and (ii) to better understand the metabolic events leading to label scrambling in these strains. B. flavum, which is used commercially for the production of monosodium glutamate, has the capability of utilizing glucose or acetate as a sole carbon source, an important criterion from the standpoint of developing labeling strategies. Unfortunately, singly labeled glucose precursors lead to excessive isotopic dilution which reduces their usefulness. Studies with [3-13C]pyruvate indicate that this problem can in principle be overcome by using labeled three-carbon precursors; however, conditions could not be found which would lead to an acceptable yield of isotopically labeled L-glutamate. In contrast, [1-_3C]or [2-13C]acetate provides relatively inexpensive, readily available precursors for the production of selectively labeled, highly enriched L-glutamate. The preparation of L-[1s5Nglutamate from ['5N]ammonium sulfate was carried out and is a very effective labeling strategy. Analysis of the isotopic distribution in labeled glutamate provides details about the metabolic pathways in these interesting organisms.

show abstract

mentioning

confidence: 99%

Biosynthetic preparation of L-[13C]- and [15N]glutamate by Brevibacterium flavum

Walker¹,

London²

1987

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…The use of the [ 15 N]ammonium ion or isotopically labeled a-keto acids for this reaction has led to a general method for the synthesis of a range of isotopically labeled a-amino acids [3][4][5][6]. An early example of this approach developed by Ducrocq et al, involved the preparation of 4-[ 2 H 2 ]L-glutamic acid 1 using glutamate dehydrogenase to carry out the reductive amination and alcohol dehydrogenase to recycle the NAD þ [3].…”

Section: Enzyme-catalyzed Methodsmentioning

confidence: 99%

Synthesis of Isotopically Labeled α‐Amino Acids

Reid

Sutherland

2009

Amino Acids, Peptides and Proteins in Organic Chemistry

View full text Add to dashboard Cite

“…Thus, by coupling the reaction catalysed by one of the well-characterized amino acid dehydrogenases (glutamate-, alanine-, leucine-or phenylalanine dehydrogenase) with a NADH generating reaction (glucose-6-phosphate/glucose-6-phosphate dehydrogenase; ethanol/alcohol dehydrogenase; lactate/lactate dehydrogenase; formic acid/formate dehydrogenase) ten proteinogenic L-amino acids labelled with 15 N can be produced from millimolar to molar scale. [6][7][8][9][10] The required specific enzymes could be obtained currently at low cost by recombinant DNA technology.…”

Section: Introductionmentioning

confidence: 99%

Stereoselective synthesis of L‐[¹⁵N] amino acids with glucose dehydrogenase and galactose mutarotase as NADH regenerating system

Chiriac

Lupan

Bucurenci

et al. 2008

Labelled Comp Radiopharmac

Self Cite

View full text Add to dashboard Cite

aWe have developed an efficient stereospecific enzymatic synthesis of L-15 N]-norleucine and L-[ 15 N]-isoleucine from the corresponding a-keto acids by coupling the reactions catalysed by leucine dehydrogenase and glucose dehydrogenase/galactose mutarotase. Giving high yields of L-amino acids, the procedure is economical and easy to perform and to monitor at a synthetically useful scale (1-10 g).

show abstract

Simple enzymatic procedure for preparation of 15N-labeled l-glutamic acid

Cited by 11 publications

References 6 publications

Biosynthetic preparation of L-[13C]- and [15N]glutamate by Brevibacterium flavum

Biosynthetic preparation of L-[13C]- and [15N]glutamate by Brevibacterium flavum

Synthesis of Isotopically Labeled α‐Amino Acids

Stereoselective synthesis of L‐[¹⁵N] amino acids with glucose dehydrogenase and galactose mutarotase as NADH regenerating system

Contact Info

Product

Resources

About

Simple enzymatic procedure for preparation of 15N-labeled l-glutamic acid

Cited by 11 publications

References 6 publications

Biosynthetic preparation of L-[13C]- and [15N]glutamate by Brevibacterium flavum

Biosynthetic preparation of L-[13C]- and [15N]glutamate by Brevibacterium flavum

Synthesis of Isotopically Labeled α‐Amino Acids

Stereoselective synthesis of L‐[15N] amino acids with glucose dehydrogenase and galactose mutarotase as NADH regenerating system

Contact Info

Product

Resources

About

Stereoselective synthesis of L‐[¹⁵N] amino acids with glucose dehydrogenase and galactose mutarotase as NADH regenerating system