21709-90-0 Usage
Description
N-(1-oxopropyl)-Glycine, also known as a metabolite of methylmalonic acid and propionic acid, is a N-acylglycine derived from the formal condensation of the carboxy group of propionic acid with the amino group of glycine. It plays a significant role in the metabolism of certain organic acids and is particularly relevant in the context of metabolic disorders.
Uses
Used in Medical Applications:
N-(1-oxopropyl)-Glycine is used as a diagnostic marker for the detection and monitoring of methylmalonic acid and propionic acid metabolic disorders in children. Its presence in the body can indicate the presence of these disorders, aiding in early diagnosis and treatment.
Used in Metabolic Research:
In the field of biochemistry and molecular biology, N-(1-oxopropyl)-Glycine is used as a research tool to study the metabolic pathways and mechanisms involving methylmalonic acid and propionic acid. Understanding its role can contribute to the development of therapeutic strategies for related metabolic disorders.
Used in Pharmaceutical Development:
N-(1-oxopropyl)-Glycine may also be utilized in the development of pharmaceuticals targeting metabolic disorders. By understanding its interaction with the metabolic pathways, researchers can potentially design drugs that modulate these pathways, offering new treatment options for patients with such conditions.
Check Digit Verification of cas no
The CAS Registry Mumber 21709-90-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,1,7,0 and 9 respectively; the second part has 2 digits, 9 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 21709-90:
(7*2)+(6*1)+(5*7)+(4*0)+(3*9)+(2*9)+(1*0)=100
100 % 10 = 0
So 21709-90-0 is a valid CAS Registry Number.
InChI:InChI=1/C5H9NO3/c1-2-4(7)6-3-5(8)9/h2-3H2,1H3,(H,6,7)(H,8,9)
21709-90-0Relevant articles and documents
Enzymatic characterization and elucidation of the catalytic mechanism of a recombinant bovine glycine N-acyltransferase
Badenhorst, Christoffel P. S.,Jooste, Maritza,Van Dijk, Alberdina A.
experimental part, p. 346 - 352 (2012/06/30)
Glycine conjugation, a phase II detoxification process, is catalyzed by glycine N-acyltransferase (GLYAT; E.C. 2.3.1.13). GLYAT detoxifies various xenobiotics, such as benzoic acid, and endogenous organic acids, such as isovaleric acid, which makes GLYAT important in the management of organic acidemias in humans. We cloned the open reading frame encoding the bovine ortholog of GLYAT from bovine liver mRNA into the bacterial expression vector pColdIII. The recombinant enzyme was expressed, partially purified, and enzymatically characterized. Protein modeling was used to predict Glu 226 of bovine GLYAT to be catalytically important. This was assessed by constructing an E226Q mutant and comparing its enzyme kinetics to that of the wild-type recombinant bovine GLYAT. The Michaelis constants for benzoyl-CoA and glycine were determined and were similar for wild-type recombinant GLYAT, E226Q recombinant GLYAT, and GLYAT present in bovine liver. At pH 8.0, the E226Q mutant GLYAT had decreased activity, which could be compensated for by increasing the reaction pH. This suggested a catalytic mechanism in which Glu226 functions to deprotonate glycine, facilitating nucleophilic attack on the acyl- CoA. The recombinant bovine GLYAT enzyme, combined with this new understanding of its active site and reaction mechanism, could be a powerful tool to investigate the functional significance of GLYAT sequence variations. Eventually, this should facilitate investigations into the impact of known and novel sequence variations in the human GLYAT gene. Copyright
