ArticleScientific reports2016
Tuned by metals: the TET peptidase activity is controlled by 3 metal binding sites.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 13 citations in OpenAlex.
- Wide Diversity and Complex Evolution of M42 Aminopeptidases With Contrasted Functional Properties in Archaea.Molecular biology and evolution · 2025Article
- Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR.Nature communications · 2022Article
- How metal cofactors drive dimer-dodecamer transition of the M42 aminopeptidase TmPep1050 ofThe Journal of biological chemistry · 2019Article
- Characterization of a Glycyl-Specific TET Aminopeptidase Complex from Pyrococcus horikoshii.Journal of bacteriology · 2018Article
- Calcium-driven DNA synthesis by a high-fidelity DNA polymerase.Nucleic acids research · 2017Article
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TET aminopeptidases are dodecameric particles shared in the three life domains involved in various biological processes, from carbon source provider in archaea to eye-pressure regulation in humans. Each subunit contains a dinuclear metal site (M1 and M2) responsible for the enzyme catalytic activity. However, the role of each metal ion is still uncharacterized. Noteworthy, while mesophilic TETs are activated by Mn(2+), hyperthermophilic TETs prefers Co(2+). Here, by means of anomalous x-ray crystallography and enzyme kinetics measurements of the TET3 aminopeptidase from the hyperthermophilic organism Pyrococcus furiosus (PfTET3), we show that M2 hosts the catalytic activity of the enzyme, while M1 stabilizes the TET3 quaternary structure and controls the active site flexibility in a temperature dependent manner. A new third metal site (M3) was found in the substrate binding pocket, modulating the PfTET3 substrate preferences. These data show that TET activity is tuned by the molecular interplay among three metal sites.
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