56892-79-6

Basic information

• Product Name: N^α-(4-amino-4-deoxy-N¹⁰-methylpteroyl)-N^ε-carbobenzoxy-L-lysine methyl ester
• Synonyms: N^α-(4-amino-4-deoxy-N¹⁰-methylpteroyl)-N^ε-carbobenzoxy-L-lysine methyl ester
• CAS NO: 56892-79-6
• Molecular Weight: 601.665
• Mol File: 56892-79-6.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: N^α-(4-amino-4-deoxy-N¹⁰-methylpteroyl)-N^ε-carbobenzoxy-L-lysine methyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: N^α-(4-amino-4-deoxy-N¹⁰-methylpteroyl)-N^ε-carbobenzoxy-L-lysine methyl ester(56892-79-6)
• EPA Substance Registry System: N^α-(4-amino-4-deoxy-N¹⁰-methylpteroyl)-N^ε-carbobenzoxy-L-lysine methyl ester(56892-79-6)

Safety Data

• Hazardous Substances Data: 56892-79-6(Hazardous Substances Data)

Upstream product

• 7532-09-4 methotrexate sodium salt 
• 19741-14-1 4-[(2,4-diaminopteridin-6-ylmethyl)methylamino]benzoic acid 

Downstream Products

• 82339-36-4 N^α-(4-amino-4-deoxy-N¹⁰-methylpteroyl)-N^ε-(iodoacetyl)-L-lysine 
• 80407-56-3 N^α-(4-amino-4-deoxy-N¹⁰-methylpteroyl)-L-lysine 
• 51865-82-8 N^α-(4-amino-4-deoxy-N¹⁰-methylpteroyl)-N^ε-carbobenzoxy-L-lysine 

Relevant articles and documents

Methotrexate analogues. 15. A methotrexate analogue designed for active-site-directed irreversible inactivation of dihydrofolate reductase

N(a)-(4-Amino-4-deoxy-N10-methylpteroyl)-N4-(iodoacetyl)-L-lysine (1) was synthesized as a potential active-site-directed irreversible inhibitor or dihydrofolate reductase (DHFR). In an ultraviolet spectrophotometric assay of dihydrofolate reduction by Lactobacillus casei DHFR, 1 and methotrexate (MTX, 4-amino-4-deoxy-N10-methylpteroyl-L-glutamic acid) had ID50 values of 4.5 and 6.2 nM. The corresponding ID50 values in a competitive radioligand binding assay against [3H]MTX were 31 and 16 nM. Thus, as reversible inhibitors of this enzyme over a short exposure time, 1 and MTX had comparable activity. On the other hand, when L. casei DHFR was incubated for up to 6 h with 0.1 or 1.0 μM 1, a progressive decrease in the ability of [3H]MTX to subsequently displace the drug was observed. When MTX itself was used at the same concentrations, the extent of displacement of [3H]MTX did not decrease with time. These results were consistent with rapid reversible binding of 1 to the enzyme, followed more slowly by covalent bond formation near the active site. The pH profile for this effect followed a curve with a sigmoidal shape. The apparent inflection point near pH 7.2 was consistent with alkylation of a histidine residue.