Reaction: 7,8-dihydroneopterin 3'-triphosphate = 6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
Other name(s): PTPS-III
Systematic name: 7,8-dihydroneopterin 3'-triphosphate glycolaldehyde phosphate-lyase [6-(hydroxymethyl)-7,8-dihydropterin-forming]
Comments: The enzyme, which participates in a pathway for folate biosynthesis, is found in the Stramenopiles, a large group that includes oomycetes, various microalgae and brown algae, as well as in several bacterial phyla. It provides a bypass mechanism compensating for the lack of EC 126.96.36.199, dihydroneopterin aldolase. In the malaria parasite Plasmodium falciparum the enzyme is bifunctional and also catalyses the activity of EC 188.8.131.52, 6-pyruvoyltetrahydropterin synthase. cf. EC 184.108.40.206, dihydroneopterin phosphate aldolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
1. Dittrich, S., Mitchell, S.L., Blagborough, A.M., Wang, Q., Wang, P., Sims, P.F. and Hyde, J.E. An atypical orthologue of 6-pyruvoyltetrahydropterin synthase can provide the missing link in the folate biosynthesis pathway of malaria parasites. Mol. Microbiol. 67 (2008) 609-618. [PMID: 18093090]
2. Hyde, J.E., Dittrich, S., Wang, P., Sims, P.F., de Crecy-Lagard, V. and Hanson, A.D. Plasmodium falciparum: a paradigm for alternative folate biosynthesis in diverse microorganisms. Trends Parasitol. 24 (2008) 502-508. [PMID: 18805734]
3. Pribat, A., Jeanguenin, L., Lara-Nunez, A., Ziemak, M.J., Hyde, J.E., de Crecy-Lagard, V. and Hanson, A.D. 6-Pyruvoyltetrahydropterin synthase paralogs replace the folate synthesis enzyme dihydroneopterin aldolase in diverse bacteria. J. Bacteriol. 191 (2009) 4158-4165. [PMID: 19395485]