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a gene folX deletion mutant shows normal growth properties on complete medium as well as on minimal medium
deletion of gene folX selectively eliminates tetrahydromonapterin production
enzymes, encoded by genes folX and folB, are involved in the tetrahydrofolate biosynthesis. The aldolase can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin and dihydromonapterinat appreciable velocity. The epimerase catalyzes the epimerization of carbon 2' in the triphosphates of dihydroneopterin and dihydromonapterin. The enzyme can also catalyze the cleavage of the position 6 side chain of several pteridine derivatives at a slow rate. The polarization of the 2'-hydroxy group of the substrate can serve as the initial reaction step for the aldolase as well as for the epimerase activity. Epimerase- as well as aldolase-type reactions can be catalyzed by both the FolB and FolX proteins
in Escherichia coli, L-monapterin is made from dihydromonapterin triphosphate after successive dephosphorylation and oxidation. Dihydromonapterin triphosphate is formed by an epimerase acting on C2' carbon of dihydroneopterin triphosphate, which is made from GTP by GTP cyclohydrolase I (EC
tetrahydromonapterin formation requires both FolX and FolM, a dihydrofolate and dihydrobiopterin reductase. Tetrahydromonapterin is the physiological cofactor for phenylalanine hydroxylase, and tetrahydromonapterin can outrank folate as an end product of pterin biosynthesis, pterin pathway overview
the epimerase catalyzes one step of the tetrahydrofolate biosynthetic pathway, dihydroneopterin triphosphate is converted to dihydromonapterin triphosphate
the active site of FolX is predicted to comprise residues from two adjacent subunits, which suggests that the tetramer is essential for the activity of the enzyme. Formation of the octamer may play a role in the stability of enzyme FolX
Results 1 - 7 of 7