Identification and characterization of an archaeon-specific riboflavin kinase

Zahra Mashhadi, Hong Zhang, Huimin Xu, Robert H. White

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

The riboflavin kinase in Methanocaldococcus jannaschii has been identified as the product of the MJ0056 gene. Recombinant expression of the MJ0056 gene in Escherichia coli led to a large increase in the amount of flavin mononucleotide (FMN) in the E. coli cell extract. The unexpected features of the purified recombinant enzyme were its use of CTP as the phosphoryl donor and the absence of a requirement for added metal ion to catalyze the formation of FMN. Identification of this riboflavin kinase fills another gap in the archaeal flavin biosynthetic pathway. Some divalent metals were found to be potent inhibitors of the reaction. The enzyme represents a unique CTP-dependent family of kinases.

Original languageEnglish (US)
Pages (from-to)2615-2618
Number of pages4
JournalJournal of bacteriology
Volume190
Issue number7
DOIs
StatePublished - Apr 1 2008

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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