18465-19-5 Usage
Description
5-amino-2,5-dioxo-pentanoic acid, also known as 2-oxoglutaramic acid, is an important glutamine metabolite found in mammals, plants, and various bacteria. It plays a crucial role in the metabolism and energy production within these organisms.
Uses
Used in Pharmaceutical Industry:
5-amino-2,5-dioxo-pentanoic acid is used as a key intermediate in the synthesis of various pharmaceutical compounds. Its presence in the metabolic pathways of different organisms makes it a valuable compound for the development of drugs targeting metabolic disorders and diseases.
Used in Biotechnology:
In the biotechnology industry, 5-amino-2,5-dioxo-pentanoic acid is utilized as a building block for the production of amino acids and other bioactive molecules. Its role in the metabolic pathways of various organisms allows for the creation of novel bioproducts with potential applications in medicine, agriculture, and other fields.
Used in Nutritional Supplements:
As a component of the metabolic pathways in living organisms, 5-amino-2,5-dioxo-pentanoic acid can be used in the development of nutritional supplements aimed at supporting overall health and well-being. It may contribute to the enhancement of energy production and the maintenance of proper metabolic function.
Used in Research and Development:
5-amino-2,5-dioxo-pentanoic acid serves as an essential compound for research purposes, particularly in the fields of biochemistry, molecular biology, and cell biology. It can be used to study the mechanisms of glutamine metabolism and its role in various cellular processes, leading to a better understanding of the underlying biology and potential therapeutic applications.
Used in Agriculture:
In the agricultural industry, 5-amino-2,5-dioxo-pentanoic acid may be employed as a component in the development of biostimulants and other products designed to enhance plant growth and productivity. Its role in the metabolic pathways of plants can contribute to the improvement of crop yields and overall plant health.
Check Digit Verification of cas no
The CAS Registry Mumber 18465-19-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,8,4,6 and 5 respectively; the second part has 2 digits, 1 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 18465-19:
(7*1)+(6*8)+(5*4)+(4*6)+(3*5)+(2*1)+(1*9)=125
125 % 10 = 5
So 18465-19-5 is a valid CAS Registry Number.
InChI:InChI=1/C5H7NO4/c6-4(8)2-1-3(7)5(9)10/h1-2H2,(H2,6,8)(H,9,10)/p-1
18465-19-5Relevant articles and documents
Crystal Structure of the ATPPase Subunit and Its Substrate-Dependent Association with the GATase Subunit: A Novel Regulatory Mechanism for a Two-Subunit-Type GMP Synthetase from Pyrococcus horikoshii OT3
Maruoka, Shintaro,Horita, Shoichiro,Lee, Woo Cheol,Nagata, Koji,Tanokura, Masaru
, p. 417 - 429 (2010)
Guanosine 5′-monophosphate synthetase(s) (GMPS) catalyzes the final step of the de novo synthetic pathway of purine nucleotides. GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase (GATase) and ATP pyrophosphatase (ATPPase). GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATPPase utilizes ammonia to convert adenyl xanthosine 5′-monophosphate (adenyl-XMP) into guanosine 5′-monophosphate. Here we report the crystal structure of PH-ATPPase (the ATPPase subunit of the two-subunit-type GMPS from the hyperthermophilic archaeon Pyrococcus horikoshii OT3). PH-ATPPase consists of two domains (N-domain and C-domain) and exists as a homodimer in the crystal and in solution. The N-domain contains an ATP-binding platform called P-loop, whereas the C-domain contains the xanthosine 5'-monophosphate (XMP)-binding site and also contributes to homodimerization. We have also demonstrated that PH-GATase (the glutamine amidotransferase subunit of the two-subunit-type GMPS from the hyperthermophilic archaeon P. horikoshii OT3) alone is inactive, and that all substrates of PH-ATPPase except for ammonia (Mg2+, ATP and XMP) are required to stabilize the active complex of PH-ATPPase and PH-GATase subunits.
