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

Class of enzyme 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase 2.7.6.3 37278-23-2 0003848 4m5n.jpg 270 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase monomer, E.Coli HPPK 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK) PDB 1cbk EBI.jpg 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase from haemophilus influenzae PF01288 IPR000550 PDOC00631 1hka cd00483 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (2.7.6.3) is an enzyme that catalyzes the chemical reaction 60% Q106570944 6-Hydroxymethyl-7,8-dihydropterin reversible ATP AMP AMP ATP 2-Amino-4-hydroxy-6-pyrophosphoryl-methylpteridine 1.2 The enzyme characterised from Escherichia coli 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), which is converted to adenosine monophosphate (AMP).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 1582–92 4304228 6 10.1016/S0021-9258(18)91799-0 free Shiota T, Baugh CM, Jackson R, Dillard R 1969 The enzymatic synthesis of hydroxymethyldihydropteridine pyrophosphate and dihydrofolate Biochemistry 8 5022–8 4312465 10.1021/bi00840a052 12 Richey DP, Brown GM Hydroxymethyldihydropteridine pyrophosphokinase and dihydropteroate synthetase from Escherichia coli 1971 Vitamins and Coenzymes Methods Enzymol. 18B 765–771 10.1016/s0076-6879(71)18150-5 978-0-12-181880-7 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.Talarico TL, Ray PH, Dev IK, Merrill BM, Dallas WS 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 September 1992 1325970 207135 10.1128/jb.174.18.5971-5977.1992 In the lower eukaryote Pneumocystis carinii, HPPK is the central domain of a multifunctional folate synthesis enzyme (gene fas).Volpe F, Dyer M, Scaife JG, Darby G, Stammers DK, Delves CJ The multifunctional folic acid synthesis fas gene of Pneumocystis carinii appears to encode dihydropteroate synthase and hydroxymethyldihydropterin pyrophosphokinase Gene 112 2 213–8 March 1992 1313386 10.1016/0378-1119(92)90378-310.1016/S0083-6729(08)00415-9 18804704 2008 Derrick J. P The structure and mechanism of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase Chapter 15 79 411–33 Vitamins & Hormones 9780123742322 Nomenclature The enzyme is a transferases, specifically one 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.2.7.6.3 Structural studies As of late 2007, 23 structures have been solved for this class of enzymes, with Protein Data Bank 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. References IPR000550 Biology no Category:Protein domains Category:EC 2.7.6 Category:Enzymes of known structure