This is an abbreviated version! For detailed information about 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, go to the full flat file.
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinae is a committed enzyme in the folate pathway of Streptococcus aureus playing an integral role in the biosynthesis of tetrahydrofolate
gene encodes a protein fused of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) and dihydropteroate synthase (DHPS) domains that catalyze sequential reactions in the folate biosynthetic pathway
gene encodes a protein fused of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) and dihydropteroate synthase (DHPS) domains that catalyze sequential reactions in the folate biosynthetic pathway
gene encodes a protein fused of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) and dihydropteroate synthase (DHPS) domains that catalyze sequential reactions in the folate biosynthetic pathway
putative large-scale induced-fit conformational change of enzyme HPPK. The loops 2 and 3 remain rather flexible when the enzyme is in its apoform, but loops 2 and 3 adopt the open, semi-open, and closed conformations throughout its catalytic cycle, flexibility of the three catalytic loops in the apoform of the enzyme. Molecular dynamics simulations of the apoenzyme at two different temperatures, overview
putative large-scale induced-fit conformational change of enzyme HPPK. The loops 2 and 3 remain rather flexible when the enzyme is in its apoform, but loops 2 and 3 adopt the open, semi-open, and closed conformations throughout its catalytic cycle, flexibility of the three catalytic loops in the apoform of the enzyme. Molecular dynamics simulations of the apoenzyme at two different temperatures, overview