EC 4.1.2.25 - Dihydroneopterin aldolase

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IntEnz Enzyme Nomenclature
EC 4.1.2.25

Names

Accepted name:
dihydroneopterin aldolase
Other names:
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine glycolaldehyde-lyase
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine glycolaldehyde-lyase (2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-forming)
7,8-dihydroneopterin aldolase
DHNA
mptD (gene name)
folB (gene name)
Systematic name:
7,8-dihydroneopterin glycolaldehyde-lyase (6-hydroxymethyl-7,8-dihydropterin-forming)

Reaction

Comments:

The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis. The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyse the epimerisation of the 2' hydroxy-group (EC 5.1.99.8, 7,8-dihydroneopterin epimerase) [2,3]. The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyses EC 5.1.99.8, and EC 1.13.11.81, 7,8-dihydroneopterin oxygenase [6]. The enzyme from the yeast Saccharomyces cerevisiae also catalyses the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, and EC 2.5.1.15, dihydropteroate synthase [4].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102083 , GO:0004150
CAS Registry Number: 37290-59-8
UniProtKB/Swiss-Prot: (43) [show] [UniProt]

References

  1. Mathis, J.B. and Brown, G.M.
    The biosynthesis of folic acid. XI. Purification and properties of dihydroneopterin aldolase.
    J. Biol. Chem. 245: 3015-3025 (1970). [PMID: 4912541]
  2. 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]
  3. 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]
  4. Guldener, U., Koehler, G. J., Haussmann, C., Bacher, A., Kricke, J., Becher, D., Hegemann, J. H.
    Characterization of the Saccharomyces cerevisiae Fol1 protein: starvation for C1 carrier induces pseudohyphal growth.
    Mol. Biol. Cell 15: 3811-3828 (2004). [PMID: 15169867]
  5. 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]
  6. Wang, Y., Xu, H., Grochowski, L. L., White, R. H.
    Biochemical characterization of a dihydroneopterin aldolase used for methanopterin biosynthesis in methanogens.
    J. Bacteriol. 196: 3191-3198 (2014). [PMID: 24982305]
  7. 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 4.1.2.25 created 1972, modified 2015]