15574-38-6

Basic information

• Product Name: D-Glutamic acid, N-[4-[[(2-amino-1,4,7,8-tetrahydro-4-oxo-6-pteridinyl)methyl]amino]benz oyl]-
• CAS NO: 15574-38-6
• Molecular Formula: C19H21N7O6
• Molecular Weight: 443.419
• Mol File: 15574-38-6.mol
• Article Data: 4

Chemical Properties

• CAS DataBase Reference: D-Glutamic acid, N-[4-[[(2-amino-1,4,7,8-tetrahydro-4-oxo-6-pteridinyl)methyl]amino]benz oyl]-(CAS DataBase Reference)
• NIST Chemistry Reference: D-Glutamic acid, N-[4-[[(2-amino-1,4,7,8-tetrahydro-4-oxo-6-pteridinyl)methyl]amino]benz oyl]-(15574-38-6)
• EPA Substance Registry System: D-Glutamic acid, N-[4-[[(2-amino-1,4,7,8-tetrahydro-4-oxo-6-pteridinyl)methyl]amino]benz oyl]-(15574-38-6)

Safety Data

• Hazardous Substances Data: 15574-38-6(Hazardous Substances Data)

Upstream product

• 56-86-0 L-glutamic acid 
• 2134-76-1 dihydropteroate 
• 59-30-3 folate 

Downstream Products

• 135-16-0 (6S,S)-5,6,7,8-tetrahydrofolic acid 
• 76937-22-9 (6S)-N[4-[[(2-amino-1,4,5,6,7,8-hexahydro-4-oxo-5-methyl-6-pteridinyl)methyl]amino]benzoyl]-L-glutamic acid 
• 135-16-0 tetrahydrofolic acid 
• 65981-90-0 (6R)-5,10-methylylidenetetrahydrofolic acid chloride 
• 135-16-0 (6-R,S)-5,6,7,8-tetrahydrofolate 
• 71963-69-4 (6S,S)-5,6,7,8-tetrahydrofolic acid 

Relevant articles and documents

Evidence that a ' dynamic knockoutg' in Escherichia coli dihydrofolate reductase does not affect the chemical step of catalysis

The question of whether protein motions play a role in the chemical step of enzymatic catalysis has generated much controversy in recent years. Debate has recently reignited over possible dynamic contributions to catalysis in dihydrofolate reductase, foll

Binding pocket alterations in dihydrofolate synthase confer resistance to para-aminosalicylic acid in clinical isolates of Mycobacterium tuberculosis

The mechanistic basis for the resistance of Mycobacterium tuberculosis to para-aminosalicylic acid (PAS), an important agent in the treatment of multidrug-resistant tuberculosis, has yet to be fully defined. As a substrate analog of the folate precursor paraaminobenzoic acid, PAS is ultimately bioactivated to hydroxy dihydrofolate, which inhibits dihydrofolate reductase and disrupts the operation of folate-dependent metabolic pathways. As a result, the mutation of dihydrofolate synthase, an enzyme needed for the bioactivation of PAS, causes PAS resistance in M. tuberculosis strain H37Rv. Here, we demonstrate that various missense mutations within the coding sequence of the dihydropteroate (H2Pte) binding pocket of dihydrofolate synthase (FolC) confer PAS resistance in laboratory isolates of M. tuberculosis and Mycobacterium bovis. From a panel of 85 multidrug-resistant M. tuberculosis clinical isolates, 5 were found to harbor mutations in the folC gene within the H2Pte binding pocket, resulting in PAS resistance. While these alterations in the H2Pte binding pocket resulted in reduced dihydrofolate synthase activity, they also abolished the bioactivation of hydroxy dihydropteroate to hydroxy dihydrofolate. Consistent with this model for abolished bioactivation, the introduction of a wild-type copy of folC fully restored PAS susceptibility in folC mutant strains. Confirmation of this novel PAS resistance mechanism will be beneficial for the development of molecular method-based diagnostics for M. tuberculosis clinical isolates and for further defining the mode of action of this important tuberculosis drug. Copyright