Direct Transfer of One-Carbon Units in the Transformylations of de Novo Purine Biosynthesis

Gary K. Smith, W. Thomas Mueller, Lawrence J. Slieker, Charles W. DeBrosse, Stephen J. Benkovic

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

It is shown that the transfer of formyl units in the de novo purine biosynthetic pathway as catalyzed by glycinamide ribonucleotide (GAR) transformylase and 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) transformylase probably proceeds through a direct displacement mechanism involving only formyl donor (10-CHO-H4folate) and formyl acceptor (GAR or AICAR). The inability to observe enzyme-catalyzed solvent oxygen incorporation or uncoupling by hydroxylamine of 1:1 stoichiometry between formylated acceptor [formylglycinamide ribonucleotide or 5-(formylamino)imidazole-4-carboxamide ribonucleotide] and deformylated donor implies the absence of an amidine intermediate and suggests that either a formylated enzyme-bound intermediate is not formed or such an intermediate is not accessible to hydroxylamine.

Original languageEnglish (US)
Pages (from-to)2870-2874
Number of pages5
JournalBiochemistry
Volume21
Issue number12
DOIs
StatePublished - Jun 1982

All Science Journal Classification (ASJC) codes

  • Biochemistry

Fingerprint Dive into the research topics of 'Direct Transfer of One-Carbon Units in the Transformylations of de Novo Purine Biosynthesis'. Together they form a unique fingerprint.

Cite this