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Application Area

Nα-Benzoyl-L-asparagine 4-nitroanilide

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

L-Amino Acids

Catalog number

BAT-004103

CAS number

201733-11-1

Molecular Formula

C17H16N4O5

Molecular Weight

356.30

IUPAC Name

(2S)-2-benzamido-N-(4-nitrophenyl)butanediamide

Synonyms

Bz-L-Asn-pNA; (2S)-2-benzamido-N-(4-nitrophenyl)butanediamide; Nalpha-Benzoyl-L-asparagine 4-nitroanilide

Purity

≥ 95%

Density

1.406±0.06 g/cm3

Boiling Point

785.1±60.0 °C

Storage

Store at 2-8 °C

InChI

InChI=1S/C17H16N4O5/c18-15(22)10-14(20-16(23)11-4-2-1-3-5-11)17(24)19-12-6-8-13(9-7-12)21(25)26/h1-9,14H,10H2,(H2,18,22)(H,19,24)(H,20,23)/t14-/m0/s1

InChI Key

SLFUSGBNVYEJGY-AWEZNQCLSA-N

Canonical SMILES

C1=CC=C(C=C1)C(=O)NC(CC(=O)N)C(=O)NC2=CC=C(C=C2)[N+](=O)[O-]

Nα-Benzoyl-L-asparagine 4-nitroanilide, a synthetic substrate commonly employed in enzymatic studies, serves as the focal point of diverse applications. Here are four key applications intricately presented with high perplexity and burstiness:

Enzyme Activity Assays: Acting as a chromogenic substrate, Nα-Benzoyl-L-asparagine 4-nitroanilide facilitates the quantification of asparaginase activity. When the enzyme cleaves the substrate, a vivid yellow product is released, enabling precise spectrophotometric measurement. This methodical approach allows for the meticulous monitoring of enzyme kinetics and activity across a spectrum of biological samples.

Drug Screening: Within the realms of high-throughput screening assays, Nα-Benzoyl-L-asparagine 4-nitroanilide is a pivotal component in identifying potential inhibitors of asparaginase activity. By scrutinizing alterations in the cleavage of this compound, researchers evaluate the effectiveness of diverse drug candidates. This critical process underpins the development of novel therapeutic agents targeting pathways associated with asparaginase.

Diagnostic Testing: In the realm of clinical diagnostics, the utilization of Nα-Benzoyl-L-asparagine 4-nitroanilide proves instrumental in discerning aberrations in enzyme activity linked to specific ailments. For instance, deviations in asparaginase activity levels may hint at underlying cancers or metabolic disorders. Incorporating this substrate in diagnostic assessments aids in the early detection and vigilant monitoring of these pathological conditions.

Protein Engineering: At the forefront of protein engineering research, Nα-Benzoyl-L-asparagine 4-nitroanilide serves as a cornerstone in the development of customized asparaginase variants with enhanced characteristics. By investigating the interactions between diverse enzyme iterations and this substrate, scientists unravel crucial insights into structure-function associations. This wealth of knowledge is indispensable for crafting enzymes with bolstered stability, heightened activity, or diminished immunogenic responses, driving forward the realm of protein engineering and biotechnology.

1. Behaviour of L-gamma-glutamyl-4-nitroanilide and L-gamma-glutamyl-3-carboxy-4-nitroanilide with respect to gamma-glutamyltransferases of different origin

P M Verhoeff, F P Peters, H Steigstra, J C Hafkenscheid Clin Chim Acta. 1988 Jul 15;175(2):129-34. doi: 10.1016/0009-8981(88)90002-2.

In this paper we compare the measurement of catalytic activity concentrations of gamma-glutamyltransferase with the non-carboxylated and the carboxylated substrate in preparations of different origin. Fresh human sera, commercial test sera and preparations of gamma-glutamyltransferase purified from human liver, porcine kidney and bovine kidney were used as sample materials. When assayed with both substrates preparations of gamma-glutamyltransferase from bovine kidney behaved in a different manner as did the enzyme in preparations from human liver or porcine kidney and the enzyme in fresh human sera. On account of the results obtained with both substrates we classified the commercial test sera for their enrichment using multi-inductive component analysis. The differences observed for the various methods of determination seem to have significance in quality control.

2. Kinetic peculiarities of human tissue kallikrein: 1--substrate activation in the catalyzed hydrolysis of H-D-valyl-L-leucyl-L-arginine 4-nitroanilide and H-D-valyl-L-leucyl-L-lysine 4-nitroanilide; 2--substrate inhibition in the catalyzed hydrolysis of N alpha-p-tosyl-L-arginine methyl ester

Marinez O Sousa, Tânia L S Miranda, Caroline N Maia, Eustáquio R Bittar, Marcelo M Santoro, Amintas F S Figueiredo Arch Biochem Biophys. 2002 Apr 1;400(1):7-14. doi: 10.1006/abbi.2002.2764.

Hydrolysis of D-valyl-L-leucyl-L-lysine 4-nitroanilide (1), D-valyl-L-leucyl-L-arginine 4-nitroanilide (2), and N alpha-p-tosyl-L-arginine methyl ester (3) by human tissue kallikrein was studied throughout a wide range of substrate concentrations. At low substrate concentrations, the hydrolysis followed Michaelis-Menten kinetics but, at higher substrate concentrations, a deviation from Michaelis-Menten behavior was observed. With the nitroanilides, a significant increase in hydrolysis rates was observed, while with the ester, a significant decrease in hydrolysis rates was observed. The results for substrates (1) and (3) can be accounted for by a model based on the hypothesis that a second substrate molecule binds to the ES complex to produce a more active or an inactive SES complex. The deviation observed for substrate (2) can be explained as a bimolecular reaction between the enzyme-substrate complex and a free substrate molecule.

N-acetyl semax

CAT NO. : BAT-009137