3-[(Aminocarbony)amino]-L-alanine
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3-[(Aminocarbony)amino]-L-alanine

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3-[(Aminocarbony)amino]-L-alanine is a glutamase inhibitor, a glutaminyl-tRNA synthetase inhibitor as well as an intermediate in the synthesis of heterocycles. It is also a potential effector group in affinity chromatography.

Category
Inhibitors containing Unusual Amino Acids
Catalog number
BAT-007822
CAS number
1483-07-4
Molecular Formula
C4H9N3O3
Molecular Weight
147.13
3-[(Aminocarbony)amino]-L-alanine
IUPAC Name
(2S)-2-amino-3-(carbamoylamino)propanoic acid
Synonyms
L-Ala(ureido)-OH; L-Albizzine; L-(-)-2-Amino-3-uraeidopropionic acid; Albizziin; L-2-Amino-3-ureidopropionic acid; L-Alanine, 3-[(aminocarbonyl)amino]-; (2S)-2-amino-3-(carbamoylamino)propanoic acid
Appearance
White crystalline powder
Purity
≥ 99% (Titration)
Density
1.430 g/cm3
Melting Point
217 °C (dec.)
Boiling Point
359.1 °C at 760 mmHg
Storage
Store at 2-8 °C
InChI
InChI=1S/C4H9N3O3/c5-2(3(8)9)1-7-4(6)10/h2H,1,5H2,(H,8,9)(H3,6,7,10)/t2-/m0/s1
InChI Key
GZYFIMLSHBLMKF-REOHCLBHSA-N
Canonical SMILES
C(C(C(=O)O)N)NC(=O)N

3-[(Aminocarbony)amino]-L-alanine, also known as BMAA, is a non-proteinogenic amino acid that has gained significant attention in various fields of research and practical applications. One critical area of use is in neurobiological studies, particularly in the investigation of neurodegenerative diseases. BMAA has been implicated in the pathogenesis of conditions such as Amyotrophic Lateral Sclerosis (ALS) and Alzheimer's disease. By studying the effects of BMAA on neurons and neural networks, scientists can better understand the molecular mechanisms that underpin these debilitating diseases. The compound’s ability to induce neurotoxicity provides a valuable model for developing potential therapeutic interventions.

Another important application of 3-[(Aminocarbony)amino]-L-alanine is in environmental science, specifically in the monitoring of cyanobacterial blooms. BMAA is produced by cyanobacteria, a group of photosynthetic bacteria commonly found in aquatic environments. When cyanobacteria proliferate, often as harmful algal blooms (HABs), they can release BMAA into water systems, posing a risk to both human and animal health. Monitoring BMAA levels can serve as an early warning system for HABs, enabling timely public health responses and the management of water quality. This application is especially important in regions where water sources are prone to nutrient pollution and eutrophication.

In the field of analytical chemistry, 3-[(Aminocarbony)amino]-L-alanine serves as a standard compound for the calibration and validation of analytical methods. High-performance liquid chromatography (HPLC) and mass spectrometry (MS) are two techniques often used to detect and quantify BMAA in various samples, including biological tissues and environmental matrices. Reliable standards are crucial for ensuring the accuracy and reproducibility of these measurements. The availability of BMAA as a standard compound enables scientists to develop robust analytical protocols, which in turn supports research across multiple disciplines, from toxicology to environmental monitoring.

Lastly, 3-[(Aminocarbony)amino]-L-alanine finds applications in the study of amino acid metabolism and protein synthesis. As a non-proteinogenic amino acid, BMAA can be incorporated into proteins by mistake, leading to the production of dysfunctional proteins. This characteristic makes BMAA a useful tool for studying the fidelity of the protein synthesis machinery and the mechanisms by which cells maintain the accuracy of genetic translation. Research in this area can provide insights into the prevention of errors in protein synthesis, which has implications for understanding a variety of diseases and developing strategies to enhance cellular function. This application highlights the broader relevance of BMAA in biochemistry and molecular biology.

1.Pig kidney legumain: an asparaginyl endopeptidase with restricted specificity.
Dando PM1, Fortunato M, Smith L, Knight CG, McKendrick JE, Barrett AJ. Biochem J. 1999 May 1;339 ( Pt 3):743-9.
Legumain was recently discovered as a lysosomal endopeptidase in mammals [Chen, Dando, Rawlings, Brown, Young, Stevens, Hewitt, Watts and Barrett (1997) J. Biol. Chem. 272, 8090-8098], having been known previously only from plants and invertebrates. It has been shown to play a key role in processing of the C fragment of tetanus toxin for presentation by the MHC class-II system [Manoury, Hewitt, Morrice, Dando, Barrett and Watts (1998) Nature (London) 396, 695-699]. We examine here the specificity of the enzyme from pig kidney by use of protein, oligopeptide and synthetic arylamide substrates, all determinations being made at pH 5.8. In proteins, only about one in ten of the asparaginyl bonds were hydrolysed, and these were mostly predicted to be located at turns on the protein surface. Bonds that were not cleaved in tetanus toxin were cleaved when presented in oligopeptides, sometimes faster than an equivalent oligopeptide based on a bond that was cleaved in the protein.
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