ArticleJournal of bacteriology2004
Identification of the Escherichia coli K-12 ybhE gene as pgl, encoding 6-phosphogluconolactonase.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 30 citations in OpenAlex.
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- Complete genome sequence, metabolic model construction and phenotypic characterization of Geobacillus LC300, an extremely thermophilic, fast growing, xylose-utilizing bacterium.Metabolic engineering · 2015Article
- Metabolic engineering of Escherichia coli for the production of riboflavin.Microbial cell factories · 2014Article
- Gene expression studies for the analysis of domoic acid production in the marine diatom Pseudo-nitzschia multiseries.BMC molecular biology · 2013Article
- The role of a periplasmic gluconolactonase (PpgL)-like protein in Pseudomonas syringae pv. syringae B728a.World journal of microbiology & biotechnology · 2011Article
- Extracellular aldonolactonase from Myceliophthora thermophila.Applied and environmental microbiology · 2011Article
- Listeria monocytogenes 6-Phosphogluconolactonase mutants induce increased activation of a host cytosolic surveillance pathway.Infection and immunity · 2009Article
- Reconstruction of biochemical networks in microorganisms.Nature reviews. Microbiology · 2009Review
- Analysis of and function predictions for previously conserved hypothetical or putative proteins in Blochmannia floridanus.BMC microbiology · 2006Article
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
We report identification of the Escherichia coli ybhE gene as the pgl gene that encodes 6-phosphogluconolactonase. A tentative identification was first made based on the known approximate location of the pgl gene and the similarity of the presumptive ybhE-encoded protein sequence to a known Pgl enzyme. To test this notion, the ybhE gene was deleted and replaced with a drug marker. Like previously characterized pgl mutants, the ybhE deletion mutant had a Blu- phenotype (dark-blue staining with iodine due to accumulation of starch after growth on minimal maltose) and demonstrated impaired growth on minimal glucose medium when combined with a pgi mutation. Biochemical assay of crude extracts for 6-phosphogluconolactonase enzymatic activity showed that ybhE encodes this activity. The ybhE gene was transferred from the E. coli chromosome to an expression vector. This ybhE clone complemented both the precise deletion of the ybhE gene and a larger deletion, pglDelta8, for the Blu- phenotype and for phosphogluconolactonase activity, confirming that ybhE is the pgl gene. A newly observed phenotype of pgl strains is a lowered frequency of appearance of Bgl+ mutants that can utilize the beta-glucoside salicin. This is likely due to poor growth of Bgl+ pgl strains on salicin due to the accumulation of 6-phosphogluconolactone.
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