67836-01-5 Usage
Uses
Used in Pharmaceutical Industry:
GLYCINE-13C2 is used as a tracer for [application reason] in the pharmaceutical industry. The stable isotope labeling allows for the tracking and analysis of metabolic pathways and the study of protein structures and interactions.
Used in Neurological Research:
GLYCINE-13C2 is used as a research tool for studying the role of glycine as an inhibitory neurotransmitter in the spinal cord. This helps in understanding the underlying mechanisms of various neurological disorders and the development of potential therapeutic strategies.
Used in NMDA Receptor Research:
GLYCINE-13C2 is used as a regulatory agent for investigating the allosteric regulation of NMDA receptors. This application aids in the study of the receptor's function in the central nervous system and its involvement in various cognitive and neurological processes.
Used in Sports Nutrition:
GLYCINE-13C2 is used as a supplement for enhancing athletic performance and recovery. The stable isotope labeling allows for the monitoring of glycine metabolism and its effects on muscle protein synthesis and overall muscle health.
Used in Agricultural Research:
GLYCINE-13C2 is used as a research tool for studying the role of glycine in plant metabolism and its potential applications in improving crop yield and stress resistance. The stable isotope labeling enables the tracking of glycine's role in plant growth and development.
Check Digit Verification of cas no
The CAS Registry Mumber 67836-01-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 6,7,8,3 and 6 respectively; the second part has 2 digits, 0 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 67836-01:
(7*6)+(6*7)+(5*8)+(4*3)+(3*6)+(2*0)+(1*1)=155
155 % 10 = 5
So 67836-01-5 is a valid CAS Registry Number.
67836-01-5Relevant academic research and scientific papers
Mechanistic insight into metal ion-catalyzed transamination
Mayer, Robert J.,Kaur, Harpreet,Rauscher, Sophia A.,Moran, Joseph
supporting information, p. 19099 - 19111 (2021/11/22)
Several classes of biological reactions that are mediated by an enzyme and a co-factor can occur, to a slower extent, not only without the enzyme but even without the co-factor, under catalysis by metal ions. This observation has led to the proposal that metabolic pathways progressively evolved from using inorganic catalysts to using organocatalysts of increasing complexity. Transamination, the biological process by which ammonia is transferred between amino acids and α-keto acids, has a mechanism that has been well studied under enzyme/co-factor catalysis and under co-factor catalysis, but the metal ion-catalyzed variant was generally studied mostly at high temperatures (70-100 °C), and the details of its mechanism remained unclear. Here, we investigate which metal ions catalyze transamination under conditions relevant to biology (pH 7, 20-50 °C) and study the mechanism in detail. Cu2+, Ni2+, Co2+, and V5+ were identified as the most active metal ions under these constraints. Kinetic, stereochemical, and computational studies illuminate the mechanism of the reaction. Cu2+ and Co2+ are found to predominantly speed up the reaction by stabilizing a key imine intermediate. V5+ is found to accelerate the reaction by increasing the acidity of the bound imine. Ni2+ is found to do both to a limited extent. These results show that direct metal ion-catalyzed amino group transfer is highly favored even in the absence of co-factors or protein catalysts under biologically compatible reaction conditions.
