15088-34-3

Basic information

• Product Name: 1,3-BenzenedicarboxaMide, N,N,N',N'-tetrakis(1-Methylethyl)-
• Synonyms: 1,3-BenzenedicarboxaMide, N,N,N',N'-tetrakis(1-Methylethyl)-
• CAS NO: 15088-34-3
• Molecular Formula: C₂₀H₃₂N₂O₂
• Molecular Weight: 332.48028
• Mol File: 15088-34-3.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 481.4±28.0 °C(Predicted)
• Appearance: /
• Density: 0.996±0.06 g/cm3(Predicted)
• PKA: -1.50±0.70(Predicted)
• CAS DataBase Reference: 1,3-BenzenedicarboxaMide, N,N,N',N'-tetrakis(1-Methylethyl)-(CAS DataBase Reference)
• NIST Chemistry Reference: 1,3-BenzenedicarboxaMide, N,N,N',N'-tetrakis(1-Methylethyl)-(15088-34-3)
• EPA Substance Registry System: 1,3-BenzenedicarboxaMide, N,N,N',N'-tetrakis(1-Methylethyl)-(15088-34-3)

Safety Data

• Hazardous Substances Data: 15088-34-3(Hazardous Substances Data)

Upstream product

• 121-91-5 isophthalic acid 
• 108-18-9 diisopropylamine 
• 99-63-8 benzene-1,3-dicarbonyl dichloride 

Relevant articles and documents

NADP-dependent glutamate dehydrogenases in a dimorphic zygomycete Benjaminiella poitrasii: Purification, characterization and their evaluation as an antifungal drug target

Background: It has been reported that the genes coding for NADP-dependent glutamate dehydrogenases (NADP-GDHs) showed a cause-effect relationship with Yeast-Hypha (Y[sbnd]H) reversible transition in a zygomycete Benjaminiella poitrasii. As Y[sbnd]H transition is significant in human pathogenic fungi for their survival and proliferation in the host, the NADP-GDHs can be explored as antifungal drug targets. Methods: The yeast-form specific BpNADPGDH I and hyphal-form specific BpNADPGDH II of B. poitrasii were purified by heterologous expression in E. coli BL-21 cells and characterized. The structural analogs of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives were designed, synthesized and screened for inhibition of NADP-GDH activity as well as Y[sbnd]H transition in B. poitrasii, and also in human pathogenic Candida albicans strains. Results: The BpNADPGDH I and BpNADPGDH II were found to be homo-hexameric proteins with native molecular mass of 282 kDa and 298 kDa, respectively and subunit molecular weights of 47 kDa and 49 kDa, respectively. Besides the distinct kinetic properties, BpNADPGDH I and BpNADPGDH II were found to be regulated by cAMP-dependent- and Calmodulin (CaM) dependent- protein kinases, respectively. The DMIP compounds showed a more pronounced effect on H-form specific BpNADPGDH II and inhibited Y[sbnd]H transition as well as growth in B. poitrasii and C. albicans strains. Conclusion: The present study will be useful to design and develop antifungal drugs against dimorphic human pathogens using glutamate dehydrogenase as a target. Significance: Glutamate dehydrogenases can be explored as a target against human pathogenic fungi.