19996-87-3 Usage
Uses
Used in Pharmaceutical Research:
1-Phenyl-3-(pyrrolidin-3-yl)urea is used as a research drug for its potential to inhibit specific enzymes, which is crucial for understanding its therapeutic effects and possible applications in medicine.
Used in Biochemical Research:
In the field of biochemical research, 1-Phenyl-3-(pyrrolidin-3-yl)urea is utilized to explore its interactions with biological systems and to investigate its potential as a lead compound for the development of new drugs.
Used in Drug Development:
1-Phenyl-3-(pyrrolidin-3-yl)urea is employed as a starting point for the development of new pharmaceuticals, given its enzyme-inhibiting properties and its potential to be optimized for specific medical applications.
Used in Enzyme Inhibition Studies:
1-Phenyl-3-(pyrrolidin-3-yl)urea is used as a tool in enzyme inhibition studies to understand the mechanisms of action and to identify new targets for therapeutic intervention.
Check Digit Verification of cas no
The CAS Registry Mumber 19996-87-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,9,9,9 and 6 respectively; the second part has 2 digits, 8 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 19996-87:
(7*1)+(6*9)+(5*9)+(4*9)+(3*6)+(2*8)+(1*7)=183
183 % 10 = 3
So 19996-87-3 is a valid CAS Registry Number.
InChI:InChI=1/C11H15N3O/c15-11(14-10-6-7-12-8-10)13-9-4-2-1-3-5-9/h1-5,10,12H,6-8H2,(H2,13,14,15)
19996-87-3Relevant academic research and scientific papers
Synthesis and Structure–Activity Relationship Studies of Benzo[b][1,4]oxazin-3(4H)-one Analogues as Inhibitors of Mycobacterial Thymidylate Synthase X
Modranka, Jakub,Li, Jiahong,Parchina, Anastasia,Vanmeert, Michiel,Dumbre, Shrinivas,Salman, Mayla,Myllykallio, Hannu,Becker, Hubert F.,Vanhoutte, Roeland,Margamuljana, Lia,Nguyen, Hoai,Abu El-Asrar, Rania,Rozenski, Jef,Herdewijn, Piet,De Jonghe, Steven,Lescrinier, Eveline
, p. 645 - 662 (2019/02/25)
Since the discovery of a flavin-dependent thymidylate synthase (ThyX or FDTS) that is absent in humans but crucial for DNA biosynthesis in a diverse group of pathogens, the enzyme has been pursued for the development of new antibacterial agents against Mycobacterium tuberculosis, the causative agent of the widespread infectious disease tuberculosis (TB). In response to a growing need for more effective anti-TB drugs, we have built upon our previous screening efforts and report herein an optimization campaign of a novel series of inhibitors with a unique inhibition profile. The inhibitors display competitive inhibition toward the methylene tetrahydrofolate cofactor of ThyX, enabling us to generate a model of the compounds bound to their target, thus offering insight into their structure–activity relationships.
