ArticleCurrent microbiology2008
Influence of N-terminal truncations on the functional expression of Bacillus licheniformis gamma-glutamyltranspeptidase in recombinant Escherichia coli.
Article in Current microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Bacterial Gamma-Glutamyl Transpeptidase, an Emerging Biocatalyst: Insights Into Structure-Function Relationship and Its Biotechnological Applications.Frontiers in microbiology · 2021Review
- Disorder prediction-based construct optimization improves activity and catalytic efficiency of Bacillus naganoensis pullulanase.Scientific reports · 2016Article
- Heterogeneous nucleation helps the search for initial crystallization conditions of γ-glutamyl transpeptidase from Bacillus licheniformis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Covalent Immobilization of Bacillus licheniformis γ-Glutamyl Transpeptidase on Aldehyde-Functionalized Magnetic Nanoparticles.International journal of molecular sciences · 2013Article
- Unfolding analysis of the mature and unprocessed forms of Bacillus licheniformis γ-glutamyltranspeptidase.Journal of biological physics · 2011Article
- Role of the conserved Thr399 and Thr417 residues of Bacillus licheniformis gamma-Glutamyltranspeptidase as evaluated by mutational analysis.Current microbiology · 2009Article
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4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The full-length Bacillus licheniformis gamma-glutamyltranspeptidase (BlGGT) gene and six truncations lacking 36, 129, 132, 135, 144, and 174 bp, respectively, at the 5' end were prepared by polymerase chain reaction and cloned into the expression vector pQE-30. Isopropyl-beta-D-thiogalactopyranoside induction of Escherichia coli M15 cells bearing the recombinant plasmids resulted in the overexpression of His(6)-tagged proteins BlGGT, BlGGT/DeltaN12, BlGGT/DeltaN43, BlGGT/DeltaN44, BlGGT/DeltaN45, BlGGT/DeltaN48, and BlGGT/DeltaN58. Except for BlGGT/DeltaN58, the overexpressed enzymes could be purified to near-homogeneity by Ni(2+)-NTA resin. The molecular masses of the precursor and subunits of BlGGT, BlGGT/DeltaN12, and BlGGT/DeltaN43 were determined to be 63, 41, and 22 kDa, respectively, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, but other recombinant enzymes exhibited predominantly as a precursor form. The specific activity for purified BlGGT, BlGGT/DeltaN12, BlGGT/DeltaN43, and BlGGT/DeltaN44 was 51.9+/-5.6, 1.3+/-0.2, 0.8+/-0.05, and 0.2+/-0.03 U/mg protein, respectively, whereas the remaining two enzymes had shown no GGT activity under the enzyme assay conditions. BlGGT, BlGGT/DeltaN12, BlGGT/DeltaN43, and BlGGT/DeltaN44 could process autocatalytically their precursors into alpha- and beta-subunits at 4 degrees C. These results indicate that removal of the signal peptide significantly affects the functional expression of BlGGT in recombinant E. coli.
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