EC - 7,8-dihydroneopterin epimerase

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IntEnz Enzyme Nomenclature


Accepted name:
7,8-dihydroneopterin epimerase
Systematic name:
7,8-dihydroneopterin 2'-epimerase



The enzyme, which has been characterized in bacteria and plants, also has the activity of EC, dihydroneopterin aldolase. The enzyme from the bacterium Mycobacterium tuberculosis has an additional oxygenase function (EC, 7,8-dihydroneopterin oxygenase) [4].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (18) [show] [UniProt]


  1. Haussmann, C., Rohdich, F., Schmidt, E., Bacher, A., Richter, G.
    Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase.
    J. Biol. Chem. 273: 17418-17424 (1998). [PMID: 9651328]
  2. Goyer, A., Illarionova, V., Roje, S., Fischer, M., Bacher, A., Hanson, A. D.
    Folate biosynthesis in higher plants. cDNA cloning, heterologous expression, and characterization of dihydroneopterin aldolases.
    Plant Physiol. 135: 103-111 (2004). [PMID: 15107504]
  3. Czekster, C. M., Blanchard, J. S.
    One substrate, five products: reactions catalyzed by the dihydroneopterin aldolase from Mycobacterium tuberculosis.
    J. Am. Chem. Soc. 134: 19758-19771 (2012). [PMID: 23150985]
  4. Blaszczyk, J., Lu, Z., Li, Y., Yan, H., Ji, X.
    Crystallographic and molecular dynamics simulation analysis of Escherichia coli dihydroneopterin aldolase.
    Cell Biosci 4: 52 (2014). [PMID: 25264482]

[EC created 2015]