30315-93-6

Basic information

• Product Name: N,N-dimethylarginine
• Synonyms: N,N-dimethylarginine;(S)-2-Amino-5-(3,3-dimethylguanidino)pentanoic acid;N(omega),N(omega)-dimethyl-L-arginine;N,N-dimethylarginine, 2-amino-5-(3,3-dimethylguanidino)pentanoic acid L-Arg(Me, Me)-OH (asymmetrical);N5-[(Dimethylamino)iminomethyl]-L-ornithine, 97%
• CAS NO: 30315-93-6
• Molecular Formula: C8H18N4O2
• Molecular Weight: 202.254120
• Mol File: 30315-93-6.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 372.6 °C at 760 mmHg
• Flash Point: 179.1 °C
• Appearance: /
• Density: 1.23 g/cm³
• Storage Temp.: 2-8°C(protect from light)
• PKA: 2.50±0.24(Predicted)
• CAS DataBase Reference: N,N-dimethylarginine(CAS DataBase Reference)
• NIST Chemistry Reference: N,N-dimethylarginine(30315-93-6)
• EPA Substance Registry System: N,N-dimethylarginine(30315-93-6)

Safety Data

• Hazardous Substances Data: 30315-93-6(Hazardous Substances Data)

Usage

Uses

Metabolomics

Definition

ChEBI: A L-arginine derivative having two methyl groups both attached to the primary amino moiety of the guanidino group.

General Description

Asymmetric dimethylarginine (ADMA) is a naturally occurring chemical found in blood plasma. It is a metabolic by-product of continual protein modification processes in the cytoplasm of all human cells. It is closely related to L-arginine, a conditionally-essential amino acid. ADMA interferes with L-arginine in the production of nitric oxide, a key chemical to endothelial and hence cardiovascular health. Asymmetric dimethylarginine is created in protein methylation, a common mechanism of post-translational protein modification. This reaction is catalyzed by an enzyme set called S-adenosylmethionine protein N-methyltransferases (protein methylases I and II). The methyl groups transferred to create ADMA are derived from the methyl group donor S-adenosylmethionine, an intermediate in the metabolism of homocysteine. (Homocysteine is an important blood chemical, because it is also a marker of cardiovascular disease). After synthesis, ADMA migrates into the extracellular space and then into blood plasma.

Upstream product

• 506-68-3 bromocyane 
• 70-26-8 L-ornithine 
• 124-40-3 dimethyl amine 

Relevant articles and documents

Binding Methylarginines and Methyllysines as Free Amino Acids: A Comparative Study of Multiple Host Classes**

Methylated free amino acids are an important class of targets for host-guest chemistry that have recognition properties distinct from those of methylated peptides and proteins. We present comparative binding studies for three different host classes that are each studied with multiple methylated arginines and lysines to determine fundamental structure-function relationships. The hosts studied are all anionic and include three calixarenes, two acyclic cucurbiturils, and two other cleft-like hosts, a clip and a tweezer. We determined the binding association constants for a panel of methylated amino acids using indicator displacement assays. The acyclic cucurbiturils display stronger binding to the methylated amino acids, and some unique patterns of selectivity. The two other cleft-like hosts follow two different trends, shallow host (clip) following similar trends to the calixarenes, and the other more closed host (tweezer) binding certain less-methylated amino acids stronger than their methylated counterparts. Molecular modelling sheds some light on the different preferences of the various hosts. The results identify hosts with new selectivities and with affinities in a range that could be useful for biomedical applications. The overall selectivity patterns are explained by a common framework that considers the geometry, depth of binding pockets, and functional group participation across all host classes.

Isolation and identification of N-G,N-G- and N-G,N'-G-dimethyl-arginine, N-epsilon-mono-, di-, and trimethyllysine, and glucosylgalactosyl- and galactosyl-delta-hydroxylysine from human urine.

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