The Enzyme Database

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Accepted name: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
Reaction: ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate
For diagram of folate biosynthesis (late stages), click here and for diagram of methanopterin biosynthesis (part 1), click here
Other name(s): 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase; H2-pteridine-CH2OH pyrophosphokinase; 7,8-dihydroxymethylpterin-pyrophosphokinase; HPPK; 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase; hydroxymethyldihydropteridine pyrophosphokinase; ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6′-diphosphotransferase
Systematic name: ATP:6-hydroxymethyl-7,8-dihydropterin 6′-diphosphotransferase
Comments: Binds 2 Mg2+ ions that are essential for activity [4]. The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants, fungi, and some archaeal species, including the haloarchaea) and methanopterin (in some archaeal species such as the Archaeoglobi and Methanobacteria). 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, dihydroneopterin aldolase [4], the enzyme from the plant Arabidopsis thaliana harbours the activity of EC, 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-23-2
1.  Shiota, T., Baugh, C.M., Jackson, R. and Dillard, R. The enzymatic synthesis of hydroxymethyldihydropteridine pyrophosphate and dihydrofolate. Biochemistry 8 (1969) 5022–5028. [PMID: 4312465]
2.  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 (1969) 1582–1592. [PMID: 4304228]
3.  Richey, D.P. and Brown, G.M. Hydroxymethyldihydropteridine pyrophosphokinase and dihydropteroate synthetase from Escherichia coli. Methods Enzymol. 18B (1971) 765–771.
4.  Lopez, P. and Lacks, S.A. A bifunctional protein in the folate biosynthetic pathway of Streptococcus pneumoniae with dihydroneopterin aldolase and hydroxymethyldihydropterin pyrophosphokinase activities. J. Bacteriol. 175 (1993) 2214–2220. [DOI] [PMID: 8385663]
5.  Blaszczyk, J., Shi, G., Yan, H. and Ji, X. Catalytic center assembly of HPPK as revealed by the crystal structure of a ternary complex at 1.25 Å resolution. Structure 8 (2000) 1049–1058. [DOI] [PMID: 11080626]
6.  Güldener, U., Koehler, G.J., Haussmann, C., Bacher, A., Kricke, J., Becher, D. and Hegemann, J.H. Characterization of the Saccharomyces cerevisiae Fol1 protein: starvation for C1 carrier induces pseudohyphal growth. Mol. Biol. Cell 15 (2004) 3811–3828. [DOI] [PMID: 15169867]
7.  Storozhenko, S., Navarrete, O., Ravanel, S., De Brouwer, V., Chaerle, P., Zhang, G.F., Bastien, O., Lambert, W., Rebeille, F. and 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 (2007) 10749–10761. [DOI] [PMID: 17289662]
[EC created 1972, modified 2015]

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