Cloning and expression of Escherichia coli 5'-methylthioadenosine/S- adenosylhomocysteine nucleosidase identification of the pfs gene product

Kenneth A. Cornell, Michael K. Riscoe

Research output: Contribution to journalArticle

41 Scopus citations

Abstract

The enzyme 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (EC 3.2.2.9) is responsible for cleavage of the glycosidic bond in both 5'- methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH). Based on amino acid sequence analysis of this enzyme from Klebsiella, we recently speculated that an open reading frame found in E. coli (designated pfs) encoded MTA/SAH nucleosidase. To explore this possibility, we amplified, cloned, and expressed the complete pfs gene from E. coli genomic DNA. The recombinant protein exhibited a molecular weight and Michaelis constants for MTA that are in agreement with those reported for native enzyme. From this biochemical evidence we confirm our original assignment of the pfs gene as encoding MTA/SAH nucleosidase.

Original languageEnglish (US)
Pages (from-to)8-14
Number of pages7
JournalBiochimica et Biophysica Acta - Gene Structure and Expression
Volume1396
Issue number1
DOIs
StatePublished - Mar 4 1998

Keywords

  • (E. coli)
  • MTA phosphorylase
  • MTA/SAH nucleosidase
  • MTR kinase
  • Methionine
  • Pfs gene
  • Salvage

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics

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