15985-07-6

Basic information

• Product Name: N-(Trimethylsilyl)-L-glutamic acid bis(trimethylsilyl) ester
• Synonyms: N-(Trimethylsilyl)-L-glutamic acid bis(trimethylsilyl) ester
• CAS NO: 15985-07-6
• Molecular Formula: C14H33NO4Si3
• Molecular Weight: 363.67
• Mol File: 15985-07-6.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• CAS DataBase Reference: N-(Trimethylsilyl)-L-glutamic acid bis(trimethylsilyl) ester(CAS DataBase Reference)
• NIST Chemistry Reference: N-(Trimethylsilyl)-L-glutamic acid bis(trimethylsilyl) ester(15985-07-6)
• EPA Substance Registry System: N-(Trimethylsilyl)-L-glutamic acid bis(trimethylsilyl) ester(15985-07-6)

Safety Data

• Hazardous Substances Data: 15985-07-6(Hazardous Substances Data)

Upstream product

• 617-65-2 Glutamic acid 
• 996-50-9 N,N-diethyl-1,1,1-trimethylsilanamine 
• 75-77-4 chloro-trimethyl-silane 
• 56-86-0 L-glutamic acid 

Downstream Products

• 80514-74-5 N-tritylglutamic acid bis(diethylammonium) salt 

Relevant articles and documents

2,4,5-trichlorophenyl-(9H-fluoren-9-ylmethoxycarbonylamino) methylcarbamates: Synthesis, isolation, characterization and utility in the synthesis of dipeptidyl ureas

An efficient synthesis of 2,4,5-trichlorophenyl-(9H-fluoren-9- ylmethoxycarbonylamino)methylcarbamates employing isocyanates derived from several Fmoc-amino acids has been described. All the carbamates made have been obtained as crystalline solids and are

A mechanism for the addition of multiple moles of glutamate by folylpolyglutamate synthetase

The role of the α-carboxyl group in methotrexate (MeAPA-Glu) and the γ-glutamate derivative of methotrexate (MeAPA-Glu-Glu) in the reaction catalyzed by folylpolyglutamate synthetase (FPGS) has been investigated. MeAPA-Glu and MeAPA-Glu-Glu were accepted as substrates by the same FPGS species contained in an (NH4)2SO4 precipitate of mouse liver protein, as judged by a lack of additivity of product formation at saturating concentrations of both substrates. MeAPA-Gaba, the MeAPA-Glu analogue lacking an α-carboxyl, was inactive as a substrate for this enzyme as was MeAPA-Glu-Gaba, the analogue of MeAPA-Glu-Glu that lacked the α-carboxyl of the terminal glutamic acid. However, MeAPA-Gaba-Glu, the analogue of MeAPA-Glu-Glu without an α-carboxyl on the first glutamic acid, had activity as a substrate for FPGS that approached that of MeAPA-Glu-Glu. These results suggest that the α-carboxyl is essential for the binding of folyl monoglutamates to FPGS in the correct orientation to allow catalysis. Moreover, the binding of the terminal α-carboxyl of folyl oligoglutamates to the same residue(s) responsible for the binding of the α-carboxyl of folyl monoglutamates would allow correct positioning of the terminal γ-carboxyl of the chain for reaction. This binding mechanism would be compatible with the utilization of a single enzyme species for the addition of glutamate to the monoglutamate or oligoglutamate forms of folates and folate analogues.