Boc-L-citrulline 4-nitrophenyl ester
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Boc-L-citrulline 4-nitrophenyl ester

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Category
BOC-Amino Acids
Catalog number
BAT-007104
CAS number
56612-88-5
Molecular Formula
C17H24N4O7
Molecular Weight
396.40
Boc-L-citrulline 4-nitrophenyl ester
IUPAC Name
(4-nitrophenyl) (2S)-5-(carbamoylamino)-2-[(2-methylpropan-2-yl)oxycarbonylamino]pentanoate
Synonyms
Boc-L-Cit-ONp; (S)-2-Boc-amino-5-ureidopentanoic acid 4-nitrophenyl ester; Boc-L-Orn(carbamoyl)-ONp; Boc L Cit ONp
Appearance
Yellow to brown powder
Purity
≥ 98% (TLC)
Melting Point
93-97 °C
Storage
Store at 2-8 °C
InChI
InChI=1S/C17H24N4O7/c1-17(2,3)28-16(24)20-13(5-4-10-19-15(18)23)14(22)27-12-8-6-11(7-9-12)21(25)26/h6-9,13H,4-5,10H2,1-3H3,(H,20,24)(H3,18,19,23)/t13-/m0/s1
InChI Key
PMMYKHSVTAQXLJ-ZDUSSCGKSA-N
Canonical SMILES
CC(C)(C)OC(=O)NC(CCCNC(=O)N)C(=O)OC1=CC=C(C=C1)[N+](=O)[O-]

Boc-L-citrulline 4-nitrophenyl ester, a versatile chemical reagent, finds diverse applications in biochemical and pharmacological realms.

Peptide Synthesis: Central to laboratory peptide synthesis, Boc-L-citrulline 4-nitrophenyl ester plays a pivotal role as a shielded amino acid derivative that facilitates the integration of citrulline into peptide sequences. This essential compound is indispensable in crafting peptides with meticulous sequences, crucial for both research endeavors and therapeutic interventions.

Enzyme Assays: Within the domain of biochemical investigations, Boc-L-citrulline 4-nitrophenyl ester serves as a crucial substrate in enzyme assays, aiding in the assessment of enzyme activities associated with citrulline. By providing insights into enzyme kinetics and functions, this application proves invaluable, particularly in the exploration of arginase and other key enzymes involved in the urea cycle.

Drug Development: At the forefront of drug discovery, Boc-L-citrulline 4-nitrophenyl ester emerges as a fundamental building block in the initial stages of drug development, enabling the synthesis of novel compounds with potential therapeutic attributes. Through strategic modification of its functional groups, researchers can engineer new molecular entities, expediting the identification of drug candidates targeting a spectrum of diseases like cancer and metabolic disorders.

Protein Modification Studies: In the realm of protein modification investigations, researchers leverage Boc-L-citrulline 4-nitrophenyl ester to delve into protein modifications and post-translational alterations, including citrullination—a pivotal process in numerous biological contexts and diseases. Understanding these modifications is critical for the advancement of biomarker development and the exploration of potential treatments for autoimmune and inflammatory conditions.

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. Thrombin inhibition by the highly selective 'reversible suicide substrate' N-ethoxycarbonyl-D-phenylalanyl-L-prolyl-alpha-azalysine p-nitrophenyl ester
Paolo Ascenzi, Carlo Gallina, Martino Bolognesi Protein Pept Lett. 2005 Jul;12(5):433-8. doi: 10.2174/0929866054395301.
Thrombin is the last enzyme in the blood coagulation cascade. All pharmacological aspects support the use of thrombin inhibitors as antithrombotic agents. Here, we review the unusual inhibition behavior of the highly selective 'reversible suicide substrate' N-ethoxycarbonyl-D-phenylalanyl-L-prolyl-alpha-azalysine p-nitrophenyl ester (Eoc-D-Phe-Pro-azaLys-ONp) targeted to the active center of human alpha-thrombin. Eoc-D-Phe-Pro-azaLys-ONp is an acylating agent, but its hydrolysis product 1(N-ethoxycarbonyl-D-phenylalanyl-L-prolyl)-2(4-aminobutyl) hydrazine behaves as a highly selective human alpha-thrombin competitive inhibitor.
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