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

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2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
4m5n.jpg
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase monomer, E.Coli
Identifiers
EC no. 2.7.6.3
CAS no. 37278-23-2
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BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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PubMed articles
NCBI proteins
7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK)
PDB 1cbk EBI.jpg
7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase from haemophilus influenzae
Identifiers
SymbolHPPK
Pfam PF01288
InterPro IPR000550
PROSITE PDOC00631
SCOP2 1hka / SCOPe / SUPFAM
CDD cd00483
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

In enzymology, a 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (EC 2.7.6.3) is an enzyme that catalyzes the chemical reaction

Contents

ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate

Thus, the two substrates of this enzyme are ATP and 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine, whereas its two products are AMP and (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate.

This enzyme belongs to the family of transferases, specifically those transferring two phosphorus-containing groups (diphosphotransferases). The systematic name of this enzyme class is ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6'-diphosphotransferase. Other names in common use include 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase, H2-pteridine-CH2OH pyrophosphokinase, 7,8-dihydroxymethylpterin-pyrophosphokinase, HPPK, 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase, and hydroxymethyldihydropteridine pyrophosphokinase. This enzyme participates in folate biosynthesis.

This enzyme catalyses the first step in a three-step pathway leading to 7,8 dihydrofolate. Bacterial HPPK (gene folK or sulD) is a protein of 160 to 270 amino acids. [1] In the lower eukaryote Pneumocystis carinii , HPPK is the central domain of a multifunctional folate synthesis enzyme (gene fas). [2]

Structural studies

As of late 2007, 23 structures have been solved for this class of enzymes, with PDB accession codes 1DY3, 1EQ0, 1EQM, 1EX8, 1F9H, 1F9Y, 1G4C, 1HKA, 1HQ2, 1IM6, 1KBR, 1Q0N, 1RAO, 1RB0, 1RTZ, 1RU1, 1RU2, 1TMJ, 1TMM, 2BMB, 2CG8, 2F63, and 2F65.

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References

  1. Talarico TL, Ray PH, Dev IK, Merrill BM, Dallas WS (September 1992). "Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase". J. Bacteriol. 174 (18): 5971–7. doi:10.1128/jb.174.18.5971-5977.1992. PMC   207135 . PMID   1325970.
  2. Volpe F, Dyer M, Scaife JG, Darby G, Stammers DK, Delves CJ (March 1992). "The multifunctional folic acid synthesis fas gene of Pneumocystis carinii appears to encode dihydropteroate synthase and hydroxymethyldihydropterin pyrophosphokinase". Gene. 112 (2): 213–8. doi:10.1016/0378-1119(92)90378-3. PMID   1313386.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR000550