2-Amino-4-hydroxy-6-pyrophosphoryl-methylpteridine

2-Amino-4-hydroxy-6-pyrophosphoryl-methylpteridine
Skeletal formula of 2-amino-4-hydroxy-6-pyrophosphoryl-methylpteridine
Skeletal formula of 2-amino-4-hydroxy-6-pyrophosphoryl-methylpteridine
Names
Preferred IUPAC name
(2-Amino-4-oxo-1,4,7,8-tetrahydropteridin-6-yl)methyl trihydrogen diphosphate
Other names
Pteridine diphosphate
Identifiers
3D model (JSmol)
8397629
ChEBI
ChEMBL
ChemSpider
KEGG
MeSH 2-Amino-4-hydroxy-6-pyrophosphoryl-methylpteridine
UNII
  • InChI=1S/C7H11N5O8P2/c8-7-11-5-4(6(13)12-7)10-3(1-9-5)2-19-22(17,18)20-21(14,15)16/h1-2H2,(H,17,18)(H2,14,15,16)(H4,8,9,11,12,13) checkY
    Key: FCQGJGLSOWZZON-UHFFFAOYSA-N checkY
  • C1C(=NC2=C(N1)NC(=NC2=O)N)COP(=O)(O)OP(=O)(O)O
Properties
C7H11N5O8P2
Molar mass 355.140 g·mol−1
log P -2.915
Acidity (pKa) 1.252
Basicity (pKb) 12.745
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Infobox references

2-Amino-4-hydroxy-6-pyrophosphoryl-methylpteridine (7,8-Dihydropterin pyrophosphate, dihydropterin-CH2OH-diphosphate) is a pteridine; a precursor to dihydrofolic acid.[1]

Biosynthesis

The enzyme 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase converts 6-hydroxymethyl-7,8-dihydropterin to 2-amino-4-hydroxy-6-pyrophosphoryl-methylpteridine by transferring a pyrophosphate group from the cofactor, adenosine triphosphate (ATP).[2][3][4]

2D representation of the chemical structure of Q106570944.
6-Hydroxymethyl-7,8-dihydropterin
 
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
ATP
AMP
 
2D representation of the chemical structure of 2-Amino-4-hydroxy-6-pyrophosphoryl-methylpteridine.
2-Amino-4-hydroxy-6-pyrophosphoryl-methylpteridine

In organisms including Escherichia coli and Pneumocystis carinii this is a step in the biosynthesis of dihydrofolic acid.[5][6][1]

References

  1. 1 2 Derrick, J. P (2008). "Chapter 15 the Structure and Mechanism of 6-Hydroxymethyl-7,8-Dihydropterin Pyrophosphokinase". The structure and mechanism of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase. Vitamins & Hormones. Vol. 79. pp. 411–33. doi:10.1016/S0083-6729(08)00415-9. ISBN 9780123742322. PMID 18804704.
  2. ↑ Richey DP, Brown GM (1969). "The biosynthesis of folic acid. IX. Purification and properties of the enzymes required for the formation of dihydropteroic acid". J. Biol. Chem. 244 (6): 1582–92. doi:10.1016/S0021-9258(18)91799-0. PMID 4304228.
  3. ↑ Shiota T, Baugh CM, Jackson R, Dillard R (1969). "The enzymatic synthesis of hydroxymethyldihydropteridine pyrophosphate and dihydrofolate". Biochemistry. 8 (12): 5022–8. doi:10.1021/bi00840a052. PMID 4312465.
  4. ↑ Richey DP, Brown GM (1971). "Hydroxymethyldihydropteridine pyrophosphokinase and dihydropteroate synthetase from Escherichia coli". Vitamins and Coenzymes. Methods Enzymol. Vol. 18B. pp. 765–771. doi:10.1016/s0076-6879(71)18150-5. ISBN 978-0-12-181880-7.
  5. ↑ 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.
  6. ↑ 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.
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