Dihydroneopterin aldolase

In enzymology, a dihydroneopterin aldolase is an enzyme that catalyzes the chemical reaction


 * 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8- dihydropteridine $$\rightleftharpoons$$ 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde

Thus, the two substrates of this enzyme are 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8- and dihydropteridine, whereas its two products are 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine and glycolaldehyde.

This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropt eridine glycolaldehyde-lyase (2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-forming). Other names in common use include 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-, and dihydropteridine glycolaldehyde-lyase. This enzyme participates in folate biosynthesis.

Structural studies
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , , , , and.