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[Amidophosphoribosyltransferase]

H Iwahana¹, M Itakura

¹Otsuka Department of Clinical and Molecular Nutrition, School of Medicine, University of Tokushima.

Nihon Rinsho. Japanese Journal of Clinical Medicine

|December 1, 1996

Summary

Amidophosphoribosyltransferase (ATase), a key enzyme in purine synthesis, was studied across 15 species. Its structure and gene linkage provide insights into nucleotide biosynthesis regulation.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Context:

Amidophosphoribosyltransferase (ATase) is the rate-limiting enzyme in de novo purine nucleotide biosynthesis.
Understanding ATase is crucial for comprehending cellular metabolism and potential therapeutic targets.
Gene linkage and transcriptional regulation of ATase and AIRC (aminoimidazole ribonucleotide carboxylase) were investigated.

Purpose:

To clone and characterize ATase cDNAs and genomic DNAs from diverse species.
To elucidate the structural features of ATase through crystal structure determination.
To investigate the genetic organization and regulatory mechanisms of purine biosynthesis.

Summary:

ATase cDNAs and genomic DNAs were successfully cloned from 15 different species.
The genes for ATase and AIRC are closely linked and divergently transcribed in chicken, rat, and human.
The crystal structure of Bacillus subtilis ATase reveals a tetrameric, doughnut-shaped molecule with four [4 Fe-4 S] clusters, and its activity is allosterically regulated by PRPP, GMP, and AMP.

Impact:

Provides a structural basis for understanding ATase function and allosteric regulation.
Highlights conserved gene organization and regulatory strategies in purine biosynthesis across species.
Offers insights into the evolution of metabolic pathways and potential targets for drug development.

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