Glutamine-Dependent Enzyme Regulation in Purine Biosynthesis
Summary
De novo purine biosynthesis begins with the conversion of phosphoribosyl pyrophosphate (PRPP) to phosphoribosylamine, a reaction catalysed by glutamine phosphoribosylpyrophosphate amidotransferase (PPAT). This enzyme harnesses the amide nitrogen of glutamine to initiate the assembly of the purine ring. Its activity is finely tuned by substrate availability and by feedback inhibition from downstream purine nucleotides, notably AMP and GMP. Allosteric transitions between active and inactive conformations underpin cooperative binding and end-product control, ensuring balanced nucleotide pools and preventing wasteful overproduction. Dysregulation of this step has implications for proliferative disorders, immune function and metabolic diseases, making PPAT an attractive target for therapeutic intervention and metabolic engineering.
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Glutamine-Dependent Enzyme Regulation in Purine Biosynthesis publication trend
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Technical terms
Phosphoribosylpyrophosphate (PRPP): An activated ribose donor that provides the sugar backbone in nucleotide synthesis.
Glutamine phosphoribosylpyrophosphate amidotransferase (PPAT): The enzyme that catalyses the first committed step of de novo purine biosynthesis, using glutamine as a nitrogen donor.
Allosteric regulation: Modulation of enzyme activity through conformational changes induced by ligand binding at sites distinct from the active centre.
Feedback inhibition: A control mechanism in which the end-product of a pathway binds to an upstream enzyme to decrease its activity.
Cooperativity: A phenomenon where binding of a substrate or effector to one site on a multimeric enzyme alters the affinity of additional sites.
References
- Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Purification and properties.. Journal of Biological Chemistry (1979).
- The Interaction of 6-Diazo-5-oxo-l-norleucine with Phosphoribosyl Pyrophosphate Amidotransferase. Journal of Biological Chemistry (1963).
- Human Glutamine Phosphoribosylpyrophosphate Amidotransferase KINETIC AND REGULATORY PROPERTIES. Journal of Biological Chemistry (1973).
- Human Glutamine Phosphoribosylpyrophosphate Amidotransferase TWO MOLECULAR FORMS INTERCONVERTIBLE BY PURINE RIBONUCLEOTIDES AND PHOSPHORIBOSYLPYROPHOSPHATE. Journal of Biological Chemistry (1973).
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