91425-24-0

Basic information

• Product Name: (S)-2-{4-[(2,4-Diamino-pteridin-6-ylmethyl)-methyl-amino]-benzoylamino}-4-(3-methoxycarbonyl-propylcarbamoyl)-butyric acid benzyl ester
• Synonyms: (S)-2-{4-[(2,4-Diamino-pteridin-6-ylmethyl)-methyl-amino]-benzoylamino}-4-(3-methoxycarbonyl-propylcarbamoyl)-butyric acid benzyl ester
• CAS NO: 91425-24-0
• Molecular Weight: 643.702
• Mol File: 91425-24-0.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: (S)-2-{4-[(2,4-Diamino-pteridin-6-ylmethyl)-methyl-amino]-benzoylamino}-4-(3-methoxycarbonyl-propylcarbamoyl)-butyric acid benzyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-2-{4-[(2,4-Diamino-pteridin-6-ylmethyl)-methyl-amino]-benzoylamino}-4-(3-methoxycarbonyl-propylcarbamoyl)-butyric acid benzyl ester(91425-24-0)
• EPA Substance Registry System: (S)-2-{4-[(2,4-Diamino-pteridin-6-ylmethyl)-methyl-amino]-benzoylamino}-4-(3-methoxycarbonyl-propylcarbamoyl)-butyric acid benzyl ester(91425-24-0)

Safety Data

• Hazardous Substances Data: 91425-24-0(Hazardous Substances Data)

Upstream product

• 13031-60-2 methyl γ-aminobutyrate hydrochloride 
• 89106-05-8 2-{4-[(2,4-diamino-6-pteridinylmethyl)methylamino]benzoylamino}pentanedioic acid 1-benzyl ester 

Downstream Products

• 91425-23-9 methotrexate γ-N-(3-carboxypropyl)amide 

Relevant articles and documents

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.