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Prog. Nucleic Acid Res. Mol. : Mammalian phosphoribosyl-pyrophosphate synthetase. Adv. : Binding of divalent magnesium by Escherichia coli phosphoribosyl diphosphate synthetase. : Overexpression of the normal phosphoribosylpyrophosphate synthetase 1 isoform underlies catalytic superactivity of human phosphoribosylpyrophosphate synthetase. J. Biol. : Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase. Nat. Struct. : Purification and characterization of phosphoribosylpyrophosphate synthetase from rubber tree latex.

Biol. : Physicochemical and enzymatic properties of ATP:nucleotide pyrophosphotransferase. Agric. Biol. : Nucleotide 2',3'-cyclic monophosphokinase action of Streptomyces nucleotide 3'-pyrophosphokinase. Agric. Biol. : Synthesis of guanosine-3'-diphosphate-5'-diphosphate by nucleotide pyrophosphotransferase. Agric. Biol.

1-4> [1-7,13]) [1-7, 13] P AMP + 6-hydroxymethyl-7,8-dihydropterine diphosphate <1> [2] S dATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine <1> (Reversibility: ? <1> [11]) [11] P dAMP + 2-amino-7,8-dihydro-4-hydroxy-6-(diphosphooxymethyl)pteridine S Additional information <1> (<1> binding affinity for GTP and GMP, 75fold weaker than for ATP [2]) [2] P ? 3 Purification <1> [1, 11, 13] <3> (recombinant bifunctional protein 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase is involved in tetrahydrofolate [4]) [4] <4> [7] <5> (partial [8]) [8, 9] Crystallization <4> (a complex of the purified protein with a substrate analog is crystallized and its structure is solved by multiple anomalous dispersion using phase information obtained from a single crystal of selenomethionine-labeled protein [7]) [7] Cloning <2> (the hydroxymethyldihydropterin pyrophosphokinase domain of the multifunctional folic acid synthesis Fas protein expressed as an independent enzyme in Escherichia coli, high level expression in inclusion bodies using an inducible tac promoter expression system [3]; multifunctional folic acid synthesis fas gene that encodes dihydroneopterin aldolase, hydroxymethyldihydropterin pyrophosphokinase and dihydropteroate synthase, in cultured Spodoptera frugiperda SF9 insect cells [12]) [3, 12] <3> (bifunctional protein 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase is involved in tetrahydrofolate expressed in Escherichia coli [4]) [4] <4> (expression in Escherichia coli [7]) [7] Engineering R82A <1> (<1> mutation causes a decrease in the rate constant for the chemical step by a factor of 380, no significant change in the binding energy or kinetics of either substrate [6]) [6] R92A <1> (<1> mutation causes a decrease in the rate constant for the chemical step by a factor of 35000.

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