The hemB gene of Escherichia coli K12, coding for porphobilinogen synthase (PBG-S; syn., 5-aminolevulinic acid dehydratase, ALA-D), was cloned following insertion of an EcoRI fragment of plasmid F'13 into the mobilizable vector pCR1. The hybrid plasmid carrying the hemB gene was able to complement a
Nucleotide sequence of the triose phosphate isomerase gene of Escherichia coli
β Scribed by Pichersky, E. ;Gottlieb, L. D. ;Hess, J. F.
- Publisher
- Springer
- Year
- 1984
- Tongue
- English
- Weight
- 707 KB
- Volume
- 195
- Category
- Article
- ISSN
- 0026-8925
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β¦ Synopsis
We report here the complete nucleotide sequence of the E. coli triose phosphate isomerase gene. The gene encodes a polypeptide of 255 amino acids which is approximately 46% homologous to eukaryotic triose phosphate isomerases, and approximately 38% homologous to the enzyme from a thermophilic bacterium, Bacillus stearothermophilus. The nucleotide sequence is 55% homologous to that of the corresponding gene in the yeast Saccharomyces cerevisiae. To our knowledge, this is the first report of the sequence of a gene coding a glycolytic enzyme from a prokaryotic organism.
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