Cloning and Characterization of a New Purine Biosynthetic Enzyme: A Non-Folate Glycinamide Ribonucleotide Transformylase from E. coli

Ariane Marolewski, John M. Smith, Stephen J. Benkovic

Research output: Contribution to journalArticle

48 Scopus citations

Abstract

A novel GAR transformylase has been isolated and characterized from E. coli. The protein, a product of the purl gene, is a monomer of molecular weight 42 kDa and catalyzes the production of β-formyl GAR from formate, ATP, and β-GAR. As such it is an alternative to the formyl-folate utilizing purN GAR transformylase. No significant homology exists between the two transformylases. However, the purl protein shows significant homology to the purK protein, also involved in purine biosynthesis. Two different purl reactions have been characterized: one producing fGAR from ATP, β-GAR, and formate and the other producing acetyl phosphate and ADP from acetate and ATP. The purl GAR transformylase is the first unknown de novo purine biosynthetic enzyme to be discovered in the last 30 years and represents another step forward in understanding cellular control of purine levels.

Original languageEnglish (US)
Pages (from-to)2531-2537
Number of pages7
JournalBiochemistry
Volume33
Issue number9
DOIs
StatePublished - Mar 1 1994

All Science Journal Classification (ASJC) codes

  • Biochemistry

Fingerprint Dive into the research topics of 'Cloning and Characterization of a New Purine Biosynthetic Enzyme: A Non-Folate Glycinamide Ribonucleotide Transformylase from E. coli'. Together they form a unique fingerprint.

  • Cite this