1118-68-9 Usage
Description
N,N-Dimethylglycine (DMG) is a quaternary ammonium compound and a N-methylated product of the amino acid glycine. It is found in beans and liver and can be formed from trimethylglycine upon the loss of one of its methyl groups. It is also a byproduct of the metabolism of choline. DMG is a white to slightly yellow crystalline powder and exhibits a variety of biological effects. Although initially referred to as vitamin B16, it does not meet the definition of a vitamin as its deficiency in the diet does not lead to any ill-effects.
Uses
Used in Athletic Performance and Immune System:
N,N-Dimethylglycine is used as an athletic performance enhancer and immunostimulant, potentially improving physical performance and immune response.
Used in Medical Treatments:
N,N-Dimethylglycine is used in the treatment of autism, epilepsy, and mitochondrial disease, although published studies have shown little to no difference between DMG treatment and placebo in autism spectrum disorders.
Used as a Biomarker in COPD Patients:
N,N-Dimethylglycine serves as a biomarker of protein degradation in chronic obstructive lung disease (COPD) patients, aiding in the identification and monitoring of the disease.
Used in Enzyme Research:
It is employed as a substrate to identify, differentiate, and characterize amino acid methyltransferase(s), contributing to the understanding of these enzymes' functions and roles in biological processes.
Used in the Development of Ionic Liquids and Emulsifiers:
N,N-Dimethylglycine plays an important role in the development of glycine-based ionic liquids and emulsifiers, which have various applications in the chemical and pharmaceutical industries.
Used in Comparative Analysis:
DMG is used in comparative analysis with other N-methylated glycines, providing insights into their structural and functional similarities and differences.
Preparation
N,N-Dimethylglycine is commercially available as the free form amino acid, and as the hydrochloride salt [2491-06-7 ]. DMG may be prepared by the alkylation of glycine via the Eschweiler–Clarke reaction. In this reaction, glycine is treated with aqueous formaldehyde in formic acid that serves as both solvent and reductant. Hydrochloric acid is added thereafter to give the hydrochloride salt. The free amino acid may been obtained by neutralization of the acid salt, which has been performed with silver oxide. H2NCH2COOH + 2 CH2O + 2 HCOOH →(CH3)2NCH2COOH + 2 CO2 + 2 H2O.
Biochem/physiol Actions
N,N-Dimethylglycine (DMG) is a natural N-methylated glycine that is used in comparative analysis with other N-methylated glycines such as sarcosine and βine. N,N-Dimethylglycine is used in the development of glycine-based ionic liquids and emulsifiers. N,N-Dimethylglycine is potentially useful as a biomarker of protein degradation in COPD patients. DMG is used as a substrate to identify, differentiate and characterize amino acid methyltransferase(s).
References
J. K. Kern, V. S. Miller, L. Cauller, R. Kendall, J. Mehta, M. Dodd, Effectiveness of N,N-Dimethylglycine in Autism and Pervasive Developmental Disorder, Journal of Child Neurology, 2001, vol. 16, pp. 169-173
Check Digit Verification of cas no
The CAS Registry Mumber 1118-68-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 1,1,1 and 8 respectively; the second part has 2 digits, 6 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 1118-68:
(6*1)+(5*1)+(4*1)+(3*8)+(2*6)+(1*8)=59
59 % 10 = 9
So 1118-68-9 is a valid CAS Registry Number.
InChI:InChI=1/C4H9NO2/c1-5(2)3-4(6)7/h3H2,1-2H3,(H,6,7)
1118-68-9Relevant articles and documents
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Pearson,Bruton
, p. 864 (1951)
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Properties of monolayers of normal alkyl betaines at the air-water interface.
Evans,Pilpel
, p. 1228 - 1232 (1969)
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A New Microbial Pathway for Organophosphonate Degradation Catalyzed by Two Previously Misannotated Non-Heme-Iron Oxygenases
Rajakovich, Lauren J.,Pandelia, Maria-Eirini,Mitchell, Andrew J.,Chang, Wei-Chen,Zhang, Bo,Boal, Amie K.,Krebs, Carsten,Bollinger, J. Martin
, p. 1627 - 1647 (2019/03/19)
The assignment of biochemical functions to hypothetical proteins is challenged by functional diversification within many protein structural superfamilies. This diversification, which is particularly common for metalloenzymes, renders functional annotations that are founded solely on sequence and domain similarities unreliable and often erroneous. Definitive biochemical characterization to delineate functional subgroups within these superfamilies will aid in improving bioinformatic approaches for functional annotation. We describe here the structural and functional characterization of two non-heme-iron oxygenases, TmpA and TmpB, which are encoded by a genomically clustered pair of genes found in more than 350 species of bacteria. TmpA and TmpB are functional homologues of a pair of enzymes (PhnY and PhnZ) that degrade 2-aminoethylphosphonate but instead act on its naturally occurring, quaternary ammonium analogue, 2-(trimethylammonio)ethylphosphonate (TMAEP). TmpA, an iron(II)- and 2-(oxo)glutarate-dependent oxygenase misannotated as a γ-butyrobetaine (γbb) hydroxylase, shows no activity toward γbb but efficiently hydroxylates TMAEP. The product, (R)-1-hydroxy-2-(trimethylammonio)ethylphosphonate [(R)-OH-TMAEP], then serves as the substrate for the second enzyme, TmpB. By contrast to its purported phosphohydrolytic activity, TmpB is an HD-domain oxygenase that uses a mixed-valent diiron cofactor to enact oxidative cleavage of the C-P bond of its substrate, yielding glycine betaine and phosphate. The high specificities of TmpA and TmpB for their N-trimethylated substrates suggest that they have evolved specifically to degrade TMAEP, which was not previously known to be subject to microbial catabolism. This study thus adds to the growing list of known pathways through which microbes break down organophosphonates to harvest phosphorus, carbon, and nitrogen in nutrient-limited niches.
Novel Isobaric Tandem Mass Tags for Quantitative Proteomics and Peptidomics
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Sheet 4, (2013/04/10)
Compositions and methods of tagging peptides and other molecules using novel isobaric tandem mass tagging reagents, including novel N,N-dimethylated amino acid 8-plex and 16-plex isobaric tandem mass tagging reagents. The tagging reagents comprise: a) a reporter group having at least one atom that is optionally isotopically labeled; b) a balancing group, also having at least one atom that is optionally isotopically labeled, and c) an amine reactive group. The tagging reagents disclosed herein serve as attractive alternatives for isobaric tag for relative and absolute quantitation (iTRAQ) and tandem mass tags (TMTs) due to their synthetic simplicity, labeling efficiency and improved fragmentation efficiency.