18465-19-5

Basic information

• Product Name: 5-amino-2,5-dioxo-pentanoic acid
• Synonyms: 2-Keto-glutaramic acid;5-amino-2,5-dioxo-pentanoic acid;alpha-ketoglutaramate;2-Oxoglutaramidic acid;5-Ketoneglutaramic acid;4-Oxoglutaramic acid;alpha-Ketoglutaramic acid;2-oxoglutaramate
• CAS NO: 18465-19-5
• Molecular Formula: C₅H₇NO₄
• Molecular Weight: 145.11
• Mol File: 18465-19-5.mol
• Article Data: 2

Chemical Properties

• Melting Point: 158-160℃ (isopropanol )
• Boiling Point: 405.4°C at 760 mmHg
• Flash Point: 199°C
• Appearance: /
• Density: 1.400±0.06 g/cm3(Predicted)
• Vapor Pressure: 1.05E-07mmHg at 25°C
• PKA: 2.50±0.54(Predicted)
• CAS DataBase Reference: 5-amino-2,5-dioxo-pentanoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 5-amino-2,5-dioxo-pentanoic acid(18465-19-5)
• EPA Substance Registry System: 5-amino-2,5-dioxo-pentanoic acid(18465-19-5)

Safety Data

• Hazardous Substances Data: 18465-19-5(Hazardous Substances Data)

Usage

Uses

2-Oxoglutaramic Acid is an important glutamine metabolite in mammals, plants, and many bacteria.

InChI:InChI=1/C5H7NO4/c6-4(8)2-1-3(7)5(9)10/h1-2H2,(H2,6,8)(H,9,10)/p-1

Upstream product

• 56-85-9 L-glutamine 
• 53-59-8 NADP 

Relevant 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

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.