86296-75-5

Basic information

• Product Name: 2-amino-6-(methylamino)-5-nitrosopyrimidin-4(1H)-one
• CAS NO: 86296-75-5
• Molecular Formula: C₅H₇N₅O₂
• Molecular Weight: 169.1414
• Mol File: 86296-75-5.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 283.4°C at 760 mmHg
• Flash Point: 125.2°C
• Density: 1.8g/cm³
• Vapor Pressure: 0.00317mmHg at 25°C
• Refractive Index: 1.762
• CAS DataBase Reference: 2-amino-6-(methylamino)-5-nitrosopyrimidin-4(1H)-one(CAS DataBase Reference)
• NIST Chemistry Reference: 2-amino-6-(methylamino)-5-nitrosopyrimidin-4(1H)-one(86296-75-5)
• EPA Substance Registry System: 2-amino-6-(methylamino)-5-nitrosopyrimidin-4(1H)-one(86296-75-5)

Safety Data

• Hazardous Substances Data: 86296-75-5(Hazardous Substances Data)

Usage

General Description

2-amino-6-(methylamino)-5-nitrosopyrimidin-4(1H)-one, also known as MAMN, is a chemical compound that is commonly used in organic synthesis and pharmaceutical research. It is a nitrosamine derivative, which is known to have potential carcinogenic properties. MAMN has been studied for its mutagenic and genotoxic effects, as well as its potential role in cancer development. It is important to handle this chemical with caution and follow proper safety protocols when working with it in a laboratory setting. Additionally, its potential health risks should be carefully considered when evaluating its use in various applications.

Upstream product

• 54004-20-5 2-amino-6-(methylamino)pyrimidin-4(3H)-one 

Downstream Products

• 5502-78-3 9-Methylguanine 

Relevant articles and documents

8-Mercaptoguanine Derivatives as Inhibitors of Dihydropteroate Synthase

Dihydropteroate synthase (DHPS) is an enzyme of the folate biosynthesis pathway, which catalyzes the formation of 7,8-dihydropteroate (DHPt) from 6-hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPPP) and para-aminobenzoic acid (pABA). DHPS is the long-standing target of the sulfonamide class of antibiotics that compete with pABA. In the wake of sulfa drug resistance, targeting the structurally rigid (and more conserved) pterin site has been proposed as an alternate strategy to inhibit DHPS in wild-type and sulfa drug resistant strains. Following the work on developing pterin-site inhibitors of the adjacent enzyme 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK), we now present derivatives of 8-mercaptoguanine, a fragment that binds weakly within both enzymes, and quantify sub-μm binding using surface plasmon resonance (SPR) to Escherichia coli DHPS (EcDHPS). Eleven ligand-bound EcDHPS crystal structures delineate the structure–activity relationship observed providing a structural framework for the rational development of novel, substrate-envelope-compliant DHPS inhibitors.

Monocyclic Pteridine Analogues. Inhibition of Escherichia coli Dihydropteroate Synthase by 6-Amino-5-nitrosoisocytosines

A variety of 5,6-disubstituted isocytosine derivatives were evaluated in vitro as inhibitors of dihydropteroate synthase from Escherichia coli.A number of 6-(alkylamino)-5-nitrosoisocytosines have in vitro potency equivalent with or superior to that of therapeutically effective sulfonamide inhibitors of the synthase.The sulfonamide drugs are known to complete for the p-aminobenzoic acid binding site of the synthase, and kinetic analysis of inhibition of the synthase by 6-(methylamino)-5-nitrosoisocytosine (16; I50 = 1.6 μM) and by the 6-(3-phenoxypropyl)amino analogue (33; I50 = 3.7 μM) indicated that the nitrosoisocytosine inhibitors compete with the pteridine substrate for the enzyme.Structure-activity studies demonstrated that the enzyme surface has a low tolerance for steric bulk in the region surrounding the isocytosine 6-amino function.However, this steric intolerance may be counterbalanced to a significant degree by positive allosteric interactions achieved by certain analogues that have a 6-(ω-phenylalkyl)amino substituent.For example, 6--5-nitrosoisocytosine (28) is as effective an inhibitor (I50 = 1.4 μM) as the 6-methylamino compound 16.Although several members of the 5-nitroso series were potent synthase inhibitors, none of the nitrosoisocytosines exhibited significant antibacterial activity.This observation may reflect poor transport of these compounds through the bacterial cell wall or, alternatively, may result from a rapid metabolic inactivation process.