EC 2.7.6.3 - 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase

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IntEnz Enzyme Nomenclature
EC 2.7.6.3

Names

Accepted name:
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
Other names:
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase
7,8-dihydroxymethylpterin-pyrophosphokinase
H2-Pteridine-CH2OH pyrophosphokinase
HPPK
hydroxymethyldihydropteridine pyrophosphokinase
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
6-hydroxymethyl-7,8-dihydropterin diphosphokinase
7,8-dihydro-6-hydroxymethylpterin diphosphokinase
ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6'-diphosphotransferase
Systematic name:
ATP:6-hydroxymethyl-7,8-dihydropterin 6'-diphosphotransferase

Reaction

Cofactor

Comments:

Binds 2 Mg2+ ions that are essential for activity [4]. The enzyme participates in the pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the bacterium Streptococcus pneumoniae also harbours the activity of EC 4.1.2.25, dihydroneopterin aldolase [4], the enzyme from the plant Arabidopsis thaliana harbours the activity of EC 2.5.1.15, dihydropteroate synthase [7], while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities [6].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00631
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003848
CAS Registry Number: 37278-23-2
UniProtKB/Swiss-Prot: (41) [show] [UniProt]

References

  1. Richey, D.P. and Brown, G.M.
    The biosynthesis of folic acid. IX. Purification and properties of the enzymes required for the formation of dihydropteroic acid.
    J. Biol. Chem. 244: 1582-1592 (1969). [PMID: 4304228]
  2. Richey, D.P. and Brown, G.M.
    Hydroxymethyldihydropteridine pyrophosphokinase and dihydropteroate synthetase from Escherichia coli.
    Methods Enzymol. 18B: 765-771 (1971).
  3. Shiota, T., Baugh, C.M., Jackson, R. and Dillard, R.
    The enzymatic synthesis of hydroxymethyldihydropteridine pyrophosphate and dihydrofolate.
    Biochemistry 8: 5022-5028 (1969). [PMID: 4312465]
  4. Lopez, P., Lacks, S. A.
    A bifunctional protein in the folate biosynthetic pathway of Streptococcus pneumoniae with dihydroneopterin aldolase and hydroxymethyldihydropterin pyrophosphokinase activities.
    J. Bacteriol. 175: 2214-2220 (1993). [PMID: 8385663]
  5. Blaszczyk, J., Shi, G., Yan, H., Ji, X.
    Catalytic center assembly of HPPK as revealed by the crystal structure of a ternary complex at 1.25 Å resolution.
    Structure 8: 1049-1058 (2000). [PMID: 11080626]
  6. 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]
  7. Storozhenko, S., Navarrete, O., Ravanel, S., De Brouwer, V., Chaerle, P., Zhang, G. F., Bastien, O., Lambert, W., Rebeille, F., Van Der Straeten, D.
    Cytosolic hydroxymethyldihydropterin pyrophosphokinase/dihydropteroate synthase from Arabidopsis thaliana: a specific role in early development and stress response.
    J. Biol. Chem. 282: 10749-10761 (2007). [PMID: 17289662]

[EC 2.7.6.3 created 1972, modified 2015]