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Pathway Description
PRPP Biosynthesis
Escherichia coli
Metabolic Pathway
The biosynthesis of phosphoribosyl pyrophosphate begins as a product of the pentose phosphate and D-ribose 5-phosphate interaction. When catalyzed with a phosphopentomutase, the product is a ribose 1-phosphate. Ribose 1-phosphate can interact spontaneously with ATP resulting in a release of hydrogen ion, ADP and a ribose 1,5-biphosphate. Ribose 1,5-biphosphate is then phosphorylated through a ribose 1,5-bisphosphokinase resulting in the release of ADP and phosphoribosyl pyrophosphate. Phosphoribosyl pyrophosphate will then participate in the purine nucleotides de novo biosynthesis pathway. Alternatively pentose phosphate and D-ribose 5-phosphate's interaction can be phosphorylated through an ATP driven ribose-phosphate diphosphokinase resulting in a release of a hydrogen ion, an AMP and a phosphoribosyl pyrophosphate which will again participate in the purine nucleotides de novo biosynthesis pathway.
References
PRPP Biosynthesis References
Hove-Jensen B, Nygaard P: Phosphoribosylpyrophosphate synthetase of Escherichia coli, Identification of a mutant enzyme. Eur J Biochem. 1982 Aug;126(2):327-32.
Pubmed: 6290219
Hove-Jensen B, Harlow KW, King CJ, Switzer RL: Phosphoribosylpyrophosphate synthetase of Escherichia coli. Properties of the purified enzyme and primary structure of the prs gene. J Biol Chem. 1986 May 25;261(15):6765-71.
Pubmed: 3009477
Hove-Jensen B, Rosenkrantz TJ, Haldimann A, Wanner BL: Escherichia coli phnN, encoding ribose 1,5-bisphosphokinase activity (phosphoribosyl diphosphate forming): dual role in phosphonate degradation and NAD biosynthesis pathways. J Bacteriol. 2003 May;185(9):2793-801.
Pubmed: 12700258
Hove-Jensen B: Phosphoribosyl diphosphate synthetase-independent NAD de novo synthesis in Escherichia coli: a new phenotype of phosphate regulon mutants. J Bacteriol. 1996 Feb;178(3):714-22.
Pubmed: 8550505
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