A Convenient Determination of Chiral Pteridines; Application of Fluorescence Detected Circular Dichroism (FDCD) to the Major Pterin from Escherichia coli

Abstract

The major pterin from Escherichia coli was determined as L-monapterin, by applying fluorescence detected circular dichroism (FDCD).FDCD was highly sensitive and specific to fluorescent chiral pterin, and allowed structure determination even in the presence of non-fluorescent contaminants.The conversion of guanosine triphosphate (GTP) into 7,8-dihydroneopterin triphosphate by the action of GTP cyclohydrolase I is the first step in the biosynthetic pathway leading to biopterin cofactor in mammals.1 Biopterin cofactor, (6R)-5,6,7,8-tetrahydrobiopterin, is a natural cofactor for pteridine dependent aromatic amino acid monooxygenases 2 -4 and nitric oxide synthase. 5In prokaryotes, 7,8-dihydroneopterin triphosphate is used as the substrate in the biosynthesis of folic acid.6