ArticleExtremophiles : life under extreme conditions2013
A hydrolytic γ-glutamyl transpeptidase from thermo-acidophilic archaeon Picrophilus torridus: binding pocket mutagenesis and transpeptidation.
Article in Extremophiles : life under extreme conditions, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- A comprehensive review on structural insights through molecular visualization: tools, applications, and limitations.Journal of molecular modeling · 2025Review
- Effects of pH and NaCl on hydrolysis and transpeptidation activities of a salt-tolerant γ-glutamyltranspeptidase fromFood science and biotechnology · 2021Article
- Bacterial Gamma-Glutamyl Transpeptidase, an Emerging Biocatalyst: Insights Into Structure-Function Relationship and Its Biotechnological Applications.Frontiers in microbiology · 2021Review
- γ-Glutamyl transpeptidase-activatable near-infrared nanoassembly for tumor fluorescence imaging-guided photothermal therapy.Theranostics · 2021Article
- Purification and characterization of a novel thermophilic β-galactosidase from Picrophilus torridus of potential industrial application.Extremophiles : life under extreme conditions · 2019Article
- Development of transgenic Brassica juncea lines for reduced seed sinapine content by perturbing phenylpropanoid pathway genes.PloS one · 2017Article
- Characterization of group II chaperonins from an acidothermophilic archaeon Picrophilus torridus.FEBS open bio · 2016Article
- "Phylogenetic and evolutionary analysis of functional divergence among Gamma glutamyl transpeptidase (GGT) subfamilies".Biology direct · 2015Article
- 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
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4 authors at 1 institution in 1 country.
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Abstract
γ-Glutamyl transpeptidase of a thermo-acidophilic archaeon Picrophilus torridus was cloned and expressed using E. coli Rosetta-pET 51b(+) expression system. The enzyme was expressed at 37 °C/200 rpm with γ-GT production of 1.99 U/mg protein after 3 h of IPTG induction. It was improved nearby 10-fold corresponding to 18.92 U/mg protein in the presence of 2 % hexadecane. The enzyme was purified by Ni(2+)-NTA with a purification fold of 3.6 and recovery of 61 %. It was synthesized as a precursor heterodimeric protein of 47 kDa with two subunits of 30 kDa and 17 kDa, respectively, as revealed by SDS-PAGE and western blot. The enzyme possesses hydrolase activity with optima at pH 7.0 and 55 °C. It was thermostable with a t (1/2) of 1 h at 50 °C and 30 min at 60 °C, and retained 100 % activity at 45 °C even after 24 h. It was inhibited by azaserine and DON and PMSF. Ptγ-GT shared 37 % sequence identity and 53 % homology with an extremophile γ-GT from Thermoplasma acidophilum. Functional residues identified by in silico approaches were further validated by site-directed mutagenesis where Tyr327 mutated by Asn327 introduced significant transpeptidase activity.
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