62886-02-6

Basic information

• Product Name: (2R)-N-benzyl-2-[(2-methylpropanoyl)amino]-N-nitroso-3-phenylpropanamide (non-preferred name)
• CAS NO: 62886-02-6
• Molecular Formula: C₂₀H₂₃N₃O₃
• Molecular Weight: 353.4149
• Mol File: 62886-02-6.mol
• Article Data: 1

Chemical Properties

• Density: 1.14g/cm³
• Refractive Index: 1.576
• CAS DataBase Reference: (2R)-N-benzyl-2-[(2-methylpropanoyl)amino]-N-nitroso-3-phenylpropanamide (non-preferred name)(CAS DataBase Reference)
• NIST Chemistry Reference: (2R)-N-benzyl-2-[(2-methylpropanoyl)amino]-N-nitroso-3-phenylpropanamide (non-preferred name)(62886-02-6)
• EPA Substance Registry System: (2R)-N-benzyl-2-[(2-methylpropanoyl)amino]-N-nitroso-3-phenylpropanamide (non-preferred name)(62886-02-6)

Safety Data

• Hazardous Substances Data: 62886-02-6(Hazardous Substances Data)

Usage

General Description

The chemical "(2R)-N-benzyl-2-[(2-methylpropanoyl)amino]-N-nitroso-3-phenylpropanamide" is a compound with a complex structure consisting of benzyl, methylpropanoyl, nitroso, and phenyl groups. It is a non-preferred name for a specific chemical compound, and its exact properties and uses may vary depending on its specific structure and composition. (2R)-N-benzyl-2-[(2-methylpropanoyl)amino]-N-nitroso-3-phenylpropanamide (non-preferred name) may have potential applications in various industries, including pharmaceuticals, chemicals, and materials, but further research and testing would be necessary to fully understand its characteristics and potential uses.

Upstream product

• 70148-19-5 N-isobutyryl-D-phenylalanine methyl ester 
• 13033-84-6 D-phenylalanine methyl ester hydrochloride 
• 673-06-3 D-(R)-phenylalanine 
• 78130-83-3 N-benzyl-N'-isobutyryl-D-phenylalaninamide 

Relevant articles and documents

Active-Site-Directed Inhibition of &α-Chymotrypsin by Deaminatively Produced Carbonium Ions: An Example of Suicide or Enzyme-Activated-Substrate Inhibition

N-Nitroso amides derived from phenylalanine and alanine were utilized as inhibitors of α-chymotrypsin.During the enzyme-catalyzed hydrolysis of these substrates, carbonium ions capable of alkylating nucleophilic groups are released in the active site.Nitroso lactams were also tested as substrates since they produce carbonium ions while still tethered to the enzyme at the acyl-enzyme stage.Kinetic studies indicated that at substrate/α-chymotrypsin ratios of 40:1 the acyclic substrates caused the following percent inhibition of α-chymotrypsin activity (substrate, percent inhibition): D-1a, 100; L-1a, 9; D-1c, 100; L-1c, 9.Nitroso lactams 2 and 3, in substrate/enzyme ratios of 54:1 and 20:1, respectively, caused 91 and 97percent inhibition of α-chymotrypsin activity.At low (6:1) substrate/enzyme ratios, the inhibition of nitroso lactam 3 was partially reversible.The extents of inhibition were decreased by the competitive inhibitor N-acetyl-L-tryptophan, indicating that the inhibitor substrates were acting at the active site.Radioactive analogues of D- and L-1a and of 3(14C) provided evidence that the inhibition was irreversible, since ca. 1.0 mol of the benzyl group of D-1a and ca. 1.6 mol of the aryl moiety in the case of 3 remained bound to the inhibited enzyme after dialysis or Sephadex G-25 chromatography (no alkylation occurred with L-1a).The enzymatic hydrolyses of the L isomers of phenylalanine substrates (1a,b) were faster than those of the D enantiomers, whereas in the alanine series (1c) the rate ratio was reversed.A model based on "reverse" binding of the two aromatic groups of substrates D-1a and D-1c in the enzyme active site is proposed to explain the hydrolysis rate and the preferential inhibition of α-chymotrypsin by the D antipodes.