Nα-Z-L-asparagine 4-nitrophenyl ester
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Nα-Z-L-asparagine 4-nitrophenyl ester

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Category
CBZ-Amino Acids
Catalog number
BAT-003221
CAS number
3256-57-3
Molecular Formula
C18H17N3O7
Molecular Weight
387.30
Nα-Z-L-asparagine 4-nitrophenyl ester
IUPAC Name
(4-nitrophenyl) (2S)-4-amino-4-oxo-2-(phenylmethoxycarbonylamino)butanoate
Synonyms
Z-L-Asn-Onp; Benzyloxycarbonyl-L-Asparagine P-Nitrophenyl Ester
Appearance
White to off-white powder
Purity
≥ 98%
Density
1.387 g/cm3
Storage
Store at 2-8 °C
InChI
InChI=1S/C18H17N3O7/c19-16(22)10-15(20-18(24)27-11-12-4-2-1-3-5-12)17(23)28-14-8-6-13(7-9-14)21(25)26/h1-9,15H,10-11H2,(H2,19,22)(H,20,24)/t15-/m0/s1
InChI Key
YLWIFNIVONXXMG-HNNXBMFYSA-N
Canonical SMILES
C1=CC=C(C=C1)COC(=O)NC(CC(=O)N)C(=O)OC2=CC=C(C=C2)[N+](=O)[O-]

Nα-Z-L-asparagine 4-nitrophenyl ester, a versatile biochemical reagent, finds applications in diverse research and industrial settings. Here are the key applications depicted with elevated levels of perplexity and burstiness:

Protease Assays: Serving as a pivotal substrate in protease activity assays, Nα-Z-L-asparagine 4-nitrophenyl ester undergoes cleavage by specific proteases, yielding a detectable product that enables precise quantification of enzyme activity. This application is indispensable in conducting comprehensive enzyme kinetics studies and screening potential protease inhibitors for therapeutic purposes.

Protein Synthesis Research: Playing a crucial role in elucidating the intricate mechanisms of protein synthesis and post-translational modifications, researchers utilize Nα-Z-L-asparagine 4-nitrophenyl ester to explore the integration of asparagine residues into peptide chains. A profound understanding of these processes can potentially inform the design of innovative peptides and therapeutic proteins, paving the way for groundbreaking advancements in the field.

Pharmaceutical Development: Within the realm of drug discovery, Nα-Z-L-asparagine 4-nitrophenyl ester serves as a valuable tool for assessing the efficacy of potential drug compounds on target enzymes. By incorporating this substrate into high-throughput screening assays, scientists can efficiently identify and optimize lead compounds that modulate enzyme function, thereby expediting the discovery and development of novel therapeutic agents that hold promise for addressing unmet medical needs.

Analytical Biochemistry: Nα-Z-L-asparagine 4-nitrophenyl ester plays a critical role in analytical biochemistry, where it is employed to evaluate enzyme activity in complex biological samples. Leveraging its utility in colorimetric assays, this reagent provides a straightforward and dependable method for quantifying enzyme activity, essential for ensuring the consistency and efficacy of enzyme-based products in research and quality control settings. This application underscores the significance of precise enzymatic analysis in advancing scientific understanding and product development processes.

1. β-Glucuronidase-coupled assays of glucuronoyl esterases
Lucia Fraňová, Vladimír Puchart, Peter Biely Anal Biochem. 2016 Oct 1;510:114-119. doi: 10.1016/j.ab.2016.07.023. Epub 2016 Jul 22.
Glucuronoyl esterases (GEs) are microbial enzymes with potential to cleave the ester bonds between lignin alcohols and xylan-bound 4-O-methyl-d-glucuronic acid in plant cell walls. This activity renders GEs attractive research targets for biotechnological applications. One of the factors impeding the progress in GE research is the lack of suitable substrates. In this work, we report a facile preparation of methyl esters of chromogenic 4-nitrophenyl and 5-bromo-4-chloro-3-indolyl β-D-glucuronides for qualitative and quantitative GE assay coupled with β-glucuronidase as the auxiliary enzyme. The indolyl derivative affording a blue indigo-type product is suitable for rapid and sensitive assay of GE in commercial preparations as well as for high throughput screening of microorganisms and genomic and metagenomic libraries.
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