l-Isoasparagine
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l-Isoasparagine

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Category
L-Amino Acids
Catalog number
BAT-015743
CAS number
28057-52-5
Molecular Formula
C4H8N2O3
Molecular Weight
132.12
l-Isoasparagine
IUPAC Name
(3S)-3,4-diamino-4-oxobutanoic acid
Synonyms
H-Asp-NH2; L-aspartic acid 1-amide; L-alpha-asparagine; (S)-3,4-Diamino-4-oxobutanoic acid; 3,4-Diamino-4-oxobutanoic acid
Density
1.404±0.06 g/cm3
Boiling Point
404.4±40.0 °C at 760 mmHg
Storage
Store at -20°C
InChI
InChI=1S/C4H8N2O3/c5-2(4(6)9)1-3(7)8/h2H,1,5H2,(H2,6,9)(H,7,8)/t2-/m0/s1
InChI Key
PMLJIHNCYNOQEQ-REOHCLBHSA-N
Canonical SMILES
C(C(C(=O)N)N)C(=O)O

L-Isoasparagine is a stereoisomer of asparagine, an amino acid involved in protein synthesis and various metabolic processes. It differs from the common L-asparagine in the structure of its side chain, specifically at the amide group, leading to distinct biochemical properties. L-Isoasparagine is often studied for its role in protein aging and degradation, as well as its occurrence in modified proteins. Its unique molecular structure makes it a point of interest in the fields of enzymology, structural biology, and biochemistry.

One key industrial application of L-isoasparagine is in the pharmaceutical industry. Its role in the development and stabilization of peptide-based drugs is critical. As proteins degrade over time, L-isoasparagine can form, leading to changes in drug efficacy. Understanding its impact helps pharmaceutical companies design more stable formulations and extend the shelf life of therapeutic proteins. This research is essential for developing biopharmaceuticals that are safe and effective over extended periods.

L-Isoasparagine is also important in the food industry, particularly in food processing and preservation. Proteins in food products can undergo modifications, such as the formation of isoasparagine, which can affect texture, flavor, and nutritional quality. By studying L-isoasparagine and its effects, food scientists can develop methods to prevent undesirable protein modifications, ensuring that processed foods retain their intended qualities and remain safe for consumption.

In the field of biotechnology, L-isoasparagine serves as a model compound for studying protein aging and degradation. Its formation is often used as a marker for protein damage, which can be critical in various biotechnological applications, such as enzyme production and biocatalysis. Researchers aim to control or minimize its occurrence to improve the efficiency and longevity of enzymes used in industrial processes.

Lastly, L-isoasparagine plays a role in the field of analytical chemistry. It is used as a reference compound for protein and peptide analysis, helping to identify and quantify protein modifications in complex mixtures. This is vital for quality control in industries such as pharmaceuticals and food production, where precise analysis of protein content and integrity is required.

1. Directed evolution of alpha-aspartyl dipeptidase from Salmonella typhimurium
X Kong, Y Liu, X Gou, S Zhu, H Zhang, X Wang, J Zhang Biochem Biophys Res Commun. 2001 Nov 23;289(1):137-42. doi: 10.1006/bbrc.2001.5937.
Model-free approaches (error-prone PCR to introduce random mutations, DNA shuffling to combine positive mutations, and screening of the resultant mutant libraries) have been used to enhance the catalytic activity and thermostability of alpha-aspartyl dipeptidase from Salmonella typhimurium, which is uniquely able to hydrolyze Asp-X dipeptides (where X is any amino acid) and one tripeptide (Asp-Gly-Gly). Under double selective pressures of activity and thermostability, through two rounds of error-prone PCR and three sequential generations of DNA shuffling, coupled with screening, a mutant pepEM3074 with approximately 47-fold increased enzyme activity compared with its wild-type parent was obtained. Moreover, the stability of pepEM3074 is increased significantly. Three amino acid substitutions (Asn89His, Gln153Glu, and Leu205Arg), two of them are near the active site and substrate binding pocket, were identified by sequencing the genes encoding this evolved enzyme. The mechanism of the enhancement of activity and stability was analyzed in this paper.
2. Peptide synthesis of aspartame precursor using organic-solvent-stable PST-01 protease in monophasic aqueous-organic solvent systems
Shotaro Tsuchiyama, Noriyuki Doukyu, Masahiro Yasuda, Kosaku Ishimi, Hiroyasu Ogino Biotechnol Prog. 2007 Jul-Aug;23(4):820-3. doi: 10.1021/bp060382y. Epub 2007 May 5.
The PST-01 protease is a metalloprotease that has zinc ion at the active center and is very stable in the presence of water-soluble organic solvents. The reaction rates and the equilibrium yields of the aspartame precursor N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester (Cbz-Asp-Phe-OMe) synthesis from N-carbobenzoxy-L-aspartic acid (Cbz-Asp) and L-phenylalanine methyl ester (Phe-OMe) in the presence of water-soluble organic solvents were investigated under various conditions. Higher reaction rate and yield of Cbz-Asp-Phe-OMe were attained by the PST-01 protease when 30 mM Cbz-Asp and 500 mM Phe-OMe were used. The maximum reaction rate was obtained pH 8.0 and 37 degrees C. In the presence of dimethylsulfoxide (DMSO), glycerol, methanol, and ethylene glycol, higher reaction rates were obtained. The equilibrium yield was the highest in the presence of DMSO. The equilibrium yield of Cbz-Asp-Phe-OMe using the PST-01 protease attained 83% in the presence of 50% (v/v) DMSO.
3. Purification of Synechocystis sp. strain PCC6308 cyanophycin synthetase and its characterization with respect to substrate and primer specificity
E Aboulmagd, F B Oppermann-Sanio, A Steinbüchel Appl Environ Microbiol. 2001 May;67(5):2176-82. doi: 10.1128/AEM.67.5.2176-2182.2001.
Synechocystis sp. strain PCC6308 cyanophycin synthetase was purified 72-fold in three steps by anion exchange chromatography on Q Sepharose, affinity chromatography on the triazine dye matrix Procion Blue HE-RD Sepharose, and gel filtration on Superdex 200 HR from recombinant cells of Escherichia coli. The native enzyme, which catalyzed the incorporation of arginine and aspartic acid into cyanophycin, has an apparent molecular mass of 240 +/- 30 kDa and consists of identical subunits of 85 +/- 5 kDa. The K(m) values for arginine (49 microM), aspartic acid (0.45 mM), and ATP (0.20 mM) indicated that the enzyme had a high affinity towards these substrates. During in vitro cyanophycin synthesis, 1.3 +/- 0.1 mol of ATP per mol of incorporated amino acid was converted to ADP. The optima for the enzyme-catalyzed reactions were pH 8.2 and 50 degrees C, respectively. Arginine methyl ester (99.5 and 97% inhibition), argininamide (99 and 96%), S-(2-aminoethyl) cysteine (43 and 42%), beta-hydroxy aspartic acid (35 and 37%), aspartic acid beta-methyl ester (38 and 40%), norvaline (0 and 3%), citrulline (9 and 7%), and asparagine (2 and 0%) exhibited an almost equal inhibitory effect on the incorporation of both arginine and aspartic acid, respectively, when these compounds were added to the complete reaction mixture. In contrast, the incorporation of arginine was diminished to a greater extent than that of aspartic acid, respectively, with canavanine (82 and 53%), lysine (36 and 19%), agmatine (33 and 25%), D-aspartic acid (37 and 30%), L-glutamic acid (13 and 5%), and ornithine (23 and 11%). On the other hand, canavanine (45% of maximum activity) and lysine (13%) stimulated the incorporation of aspartic acid, whereas aspartic acid beta-methyl ester (53%) and asparagine (9%) stimulated the incorporation of arginine. [(3)H]lysine (15% of maximum activity) and [(3)H]canavanine (13%) were incorporated into the polymer, when they were either used instead of arginine or added to the complete reaction mixture, whereas L-glutamic acid was not incorporated. No effect on arginine incorporation was obtained by the addition of other amino acids (i.e., alanine, histidine, leucine, proline, tryptophan, and glycine). Various samples of chemically synthesized poly-alpha,beta-D,L-aspartic acid served as primers for in vitro synthesis of cyanophycin, whereas poly-alpha-L-aspartic acid was almost inactive.
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