7xn3

Structural highlights

Function

[KPRS_ECOLI] Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).[HAMAP-Rule:MF_00583]^{[1] [2] [3] [4] [5] [6] [7]}

References

1. ↑ Willemoes M, Hove-Jensen B, Larsen S. Steady state kinetic model for the binding of substrates and allosteric effectors to Escherichia coli phosphoribosyl-diphosphate synthase. J Biol Chem. 2000 Nov 10;275(45):35408-12. doi: 10.1074/jbc.M006346200. PMID:10954724 doi:http://dx.doi.org/10.1074/jbc.M006346200
2. ↑ Bower SG, Harlow KW, Switzer RL, Hove-Jensen B. Characterization of the Escherichia coli prsA1-encoded mutant phosphoribosylpyrophosphate synthetase identifies a divalent cation-nucleotide binding site. J Biol Chem. 1989 Jun 15;264(17):10287-91. PMID:2542328
3. ↑ 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. PMID:3009477
4. ↑ Hove-Jensen B, Nygaard P. Phosphoribosylpyrophosphate synthetase of Escherichia coli, Identification of a mutant enzyme. Eur J Biochem. 1982 Aug;126(2):327-32. doi: 10.1111/j.1432-1033.1982.tb06782.x. PMID:6290219 doi:http://dx.doi.org/10.1111/j.1432-1033.1982.tb06782.x
5. ↑ Hilden I, Hove-Jensen B, Harlow KW. Inactivation of Escherichia coli phosphoribosylpyrophosphate synthetase by the 2',3'-dialdehyde derivative of ATP. Identification of active site lysines. J Biol Chem. 1995 Sep 1;270(35):20730-6. doi: 10.1074/jbc.270.35.20730. PMID:7657655 doi:http://dx.doi.org/10.1074/jbc.270.35.20730
6. ↑ Willemoes M, Nilsson D, Hove-Jensen B. Effects of mutagenesis of aspartic acid residues in the putative phosphoribosyl diphosphate binding site of Escherichia coli phosphoribosyl diphosphate synthetase on metal ion specificity and ribose 5-phosphate binding. Biochemistry. 1996 Jun 25;35(25):8181-6. doi: 10.1021/bi9528560. PMID:8679571 doi:http://dx.doi.org/10.1021/bi9528560
7. ↑ Willemoes M, Hove-Jensen B. Binding of divalent magnesium by Escherichia coli phosphoribosyl diphosphate synthetase. Biochemistry. 1997 Apr 22;36(16):5078-83. doi: 10.1021/bi962610a. PMID:9125530 doi:http://dx.doi.org/10.1021/bi962610a