2487-26-5 Usage
Uses
Used in Research and Laboratory Settings:
O-NITROPHENYL N-BUTYRATE is used as a reagent for the determination of esterase enzyme activity, serving as a substrate that, upon enzymatic hydrolysis, releases a yellow-colored product, o-nitrophenol, which can be easily measured spectrophotometrically. This property makes it valuable for the study of enzyme kinetics and the assessment of enzyme activity levels.
Used in Pharmaceutical Development:
O-NITROPHENYL N-BUTYRATE has potential applications in the development of pharmaceuticals, particularly as a tool compound for the optimization of drug candidates targeting esterase enzymes. Its reactivity and the ease of monitoring its hydrolysis make it a useful probe in medicinal chemistry and drug discovery processes.
Used in Enzyme Kinetics Studies:
In the field of biochemistry, O-NITROPHENYL N-BUTYRATE is used as a substrate to investigate the kinetics of esterase enzymes. The release of o-nitrophenol upon enzymatic cleavage allows researchers to monitor the reaction progress and determine key kinetic parameters such as the Michaelis-Menten constant (Km) and the maximum reaction velocity (Vmax).
Used in Toxicology and Safety Assessments:
Given its potential to cause irritation, O-NITROPHENYL N-BUTYRATE can also be employed in toxicological studies to evaluate the safety and potential hazards of substances in various applications, ensuring that materials and products are safe for their intended use.
Check Digit Verification of cas no
The CAS Registry Mumber 2487-26-5 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 2,4,8 and 7 respectively; the second part has 2 digits, 2 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 2487-26:
(6*2)+(5*4)+(4*8)+(3*7)+(2*2)+(1*6)=95
95 % 10 = 5
So 2487-26-5 is a valid CAS Registry Number.
InChI:InChI=1/C10H11NO4/c1-2-5-10(12)15-9-7-4-3-6-8(9)11(13)14/h3-4,6-7H,2,5H2,1H3
2487-26-5Relevant academic research and scientific papers
Activity and specificity studies of the new thermostable esterase EstDZ2
Myrtollari, Kamela,Katsoulakis, Nikolaos,Zarafeta, Dimitra,Pavlidis, Ioannis V.,Skretas, Georgios,Smonou, Ioulia
, (2020/09/16)
In this paper, we study the activity and specificity of EstDZ2, a new thermostable carboxyl esterase of unknown function, which was isolated from a metagenome library from a Russian hot spring. The biocatalytic reaction employing EstDZ2 proved to be an efficient method for the hydrolysis of aryl p-, o- or m-substituted esters of butyric acid and esters of secondary alcohols. Docking studies revealed structural features of the enzyme that led to activity differences among the different substrates.
