Escherichia coli QueD Is a 6-Carboxy-5,6,7,8-tetrahydropterin synthase

Reid M. McCarty, Árpád Somogyi, Vahe Bandarian

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

Abstract

To elucidate the early steps required during biosynthesis of a broad class of 7-deazapurine-containing natural products, we have studied the reaction catalyzed by Escherichia coli QueD, a 6-pyruvoyl-5,6,7,8-tetrahydropterin synthase (PTPS) homologue possibly involved in queuosine biosynthesis. While mammalian PTPS homologues convert 7,8-dihydroneopterin triphosphate (H 2NTP) to 6-pyruvoyltetrahydropterin (PPH 4) in biopterin biosynthesis, E. coli QueD catalyzes the conversion of H 2NTP to 6-carboxy-5,6,7,8-tetrahydropterin (CPH 4). E. coli QueD can also convert PPH4 and sepiapterin to CPH 4, allowing a mechanism to be proposed.

Original languageEnglish (US)
Pages (from-to)2301-2303
Number of pages3
JournalBiochemistry
Volume48
Issue number11
DOIs
StatePublished - Mar 24 2009

ASJC Scopus subject areas

  • Biochemistry

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