Nucleotide sequence and deduced amino add sequence of Escherichia coli pyruvate oxidase, a lipid-activated flavoprotein

Charlotte Grabau, John E. Cronan

Research output: Contribution to journalArticle

Abstract

The entire nucleotide sequence of the poxB (pyruvate oxidase) gene of Eseherichia coli K-12 has been determined by the dideoxynucleotide (Sanger) sequencing of fragments of the gene cloned into a phage M13 vector. The gene is 1716 nucleotides In length and has an open reading frame which encodes a protein of Mr 62,018. This open reading frame was shown to encode pyruvate oxidase by alignment of the amino acid sequences deduced for the amino and carboxy termini and several internal segments of the mature protein with sequences obtained by amino acid sequence analysis. The deduced amino acid sequence of the oxidase was not unusually rich in hydrophobic sequences despite the peripheral membrane location and lipid binding properties of the protein. The codon usage of the oxidase gene was typical of a moderately expressed protein. The deduced amino acid sequence shares homology with the large subunits of the acetohydroxy acid synthase isozymes I, II,and III, encoded by the ilvB, ilvG, and ilvI genes of E. coli.

Original languageEnglish (US)
Pages (from-to)5449-5460
Number of pages12
JournalNucleic acids research
Volume14
Issue number13
DOIs
StatePublished - Jul 11 1986

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ASJC Scopus subject areas

  • Genetics

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