Molecular and General Genetics MGG

, Volume 217, Issue 1, pp 126–131

Isolation and characterization of the phosphoglucose isomerase gene from Escherichia coli

  • Byron E. Froman
  • Robert C. Tait
  • L. D. Gottlieb


The nucleotide sequence of the gene encoding the glycolytic enzyme phosphoglucose isomerase (PGI) from Escherichia coli is presented. The gene encodes a polypeptide of 549 amino acids. The transcriptional start point of the gene was determined and found to lie within a consensus promoter region. The amino acid sequence derived from the E. coli PGI gene can be aligned without insertions or deletions to the predicted amino acid sequence of a nuclear-encoded chloroplast isozyme of PGI from a higher plant, and the two sequences have a similarity of 87.6%. The amino acid sequence similarity between E. coli and that predicted from cDNA sequences for mouse and pig PGI is approximately 65%.

Key words

Glycolytic enzyme Molecular evolution 





amino acid(s)




open reading frame


phosphoglucose isomerase


molecular weight


kilo Daltons


single strand


replicative form


Luria broth




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Copyright information

© Springer-Verlag 1989

Authors and Affiliations

  • Byron E. Froman
    • 1
  • Robert C. Tait
    • 1
  • L. D. Gottlieb
    • 1
  1. 1.Department of GeneticsUniversity of CaliforniaDavisUSA

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