Z-S-benzyl-L-cysteine 4-nitrophenyl ester
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Z-S-benzyl-L-cysteine 4-nitrophenyl ester

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Category
CBZ-Amino Acids
Catalog number
BAT-003419
CAS number
3401-37-4
Molecular Formula
C24H22N2O6S
Molecular Weight
466.50
Z-S-benzyl-L-cysteine 4-nitrophenyl ester
IUPAC Name
(4-nitrophenyl) (2R)-3-benzylsulfanyl-2-(phenylmethoxycarbonylamino)propanoate
Synonyms
Z-L-Cys(Bzl)-ONp; (4-nitrophenyl)3-benzylsulfanyl-2-(phenylmethoxycarbonylamino)propanoate; Nalpha-Z-S-benzyl-L-cysteine 4-nitrophenyl ester; p-Nitrophenylester of benzyloxycarbonyl-S-benzylcysteine; S-benzyl-N-carbobenzoxy-L-cysteine p-nitrophenyl ester
Appearance
Light yellow powder
Purity
≥ 98% (HPLC)
Density
1.321 g/cm3
Melting Point
87-91 °C
Boiling Point
674.8 °C at 760 mmHg
Storage
Store at 2-8 °C
InChI
InChI=1S/C24H22N2O6S/c27-23(32-21-13-11-20(12-14-21)26(29)30)22(17-33-16-19-9-5-2-6-10-19)25-24(28)31-15-18-7-3-1-4-8-18/h1-14,22H,15-17H2,(H,25,28)/t22-/m0/s1
InChI Key
LQPKVCBYFUURJM-QFIPXVFZSA-N
Canonical SMILES
C1=CC=C(C=C1)COC(=O)NC(CSCC2=CC=CC=C2)C(=O)OC3=CC=C(C=C3)[N+](=O)[O-]

Z-S-benzyl-L-cysteine 4-nitrophenyl ester, a specialized chemical reagent with diverse applications in biochemistry and molecular biology, plays a pivotal role in various realms.

Enzyme Inhibition Studies: Delving into the intricacies of enzyme inhibition mechanisms, Z-S-benzyl-L-cysteine 4-nitrophenyl ester emerges as a critical tool for investigating the actions of cysteine proteases. By mimicking enzyme substrates, it sheds light on how different inhibitors impact enzyme functionality. These profound insights serve as a cornerstone for developing therapeutic agents that target proteases implicated in diseases like cancer and parasitic infections.

Peptide Synthesis: In the realm of synthetic chemistry, Z-S-benzyl-L-cysteine 4-nitrophenyl ester stands out as a foundational component for crafting intricate peptides. Employed as a building block in solid-phase synthesis methodologies, this reagent enables the construction of peptide chains with specific functional groups essential for biochemical assays and drug discovery endeavors. Its role in peptide synthesis showcases its versatility and significance in the field.

Proteomics Research: Unveiling the intricacies of proteomics, Z-S-benzyl-L-cysteine 4-nitrophenyl ester finds application in labeling cysteine residues within proteins. This labeling technique aids in the identification and quantification of cysteine-containing peptides during mass spectrometry analysis, thereby facilitating a deeper understanding of protein structure, function, and post-translational modifications.

Assay Development: A stalwart in the realm of assay development, Z-S-benzyl-L-cysteine 4-nitrophenyl ester plays a crucial role in crafting colorimetric and fluorometric assays for measuring enzyme activity levels. Upon interaction with specific enzymes, this reagent triggers a discernible signal that correlates with enzyme activity, making it an indispensable tool in both basic research endeavors and pharmaceutical screening protocols. Its utility in assay development underscores its significance in advancing scientific exploration and drug discovery paradigms.

2. 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.
3. Derivatives of S-9-fluorenylmethyl-L-cysteine
M Bodanszky, M A Bednarek Int J Pept Protein Res. 1982 Nov;20(5):434-7. doi: 10.1111/j.1399-3011.1982.tb03064.x.
The 9-fluorenylmethyl (Fm) group was examined with respect to its potential for blocking the sulfhydryl function. The S-Fm group is resistant to acids and to catalytic hydrogenation but is cleaved by ammonia in methanol or by organic bases, such as a 20% solution of piperidine in dimethylformamide. Synthesis of N-tert.-butyloxycarbonyl-S-9-fluorenylmethyl-L-cysteine p-nitrophenyl ester and of cysteinyl peptides protected with the S-Fm group are described.
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