High impact information on N-(4-(((2-Amino-1,4-dihydro-4-oxo-6-quinazolinyl)methyl)formylamino)benzoyl)-L-glutamic acid

• Thymidylate synthetase from mouse leukemic L1210 cells was purified to electrophoretic homogeneity with 70% yield as a result of an affinity chromatography procedure based on reversible deoxyuridylate-dependent binding of the enzyme to a stable biospecific adsorbent, 10-formyl-5,8-dideazafolate, immobilized on aminoethyl-Sepharose [1].
• Recombinant 10-formyltetrahydrofolate dehydrogenase catalyses both dehydrogenase and hydrolase reactions utilizing the synthetic substrate 10-formyl-5,8-dideazafolate [2].
• The location of the cross-linked 10-formyl 5,8-dideazafolate at the active site was determined by amino acid sequencing of an isolated tryptic peptide [3].
• Use of 10-formyl-5,8-dideazafolate as substrate for rat 10-formyltetrahydrofolate dehydrogenase [4].

Associations of N-(4-(((2-Amino-1,4-dihydro-4-oxo-6-quinazolinyl)methyl)formylamino)benzoyl)-L-glutamic acid with other chemical compounds

• The cross-linked substrate analog was converted to the cross-linked product complex by adding either NADP+ or 2-mercaptoethanol, proving that the 10-formyl 5,8-dideazafolate was bound at the active site [3].

References