ArticlePloS one2014
Characterization of the PH1704 protease from Pyrococcus horikoshii OT3 and the critical functions of Tyr120.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 11 citations in OpenAlex.
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- Genomic attributes of thermophilic and hyperthermophilic bacteria and archaea.World journal of microbiology & biotechnology · 2022Review
- Cohnella 1759 cysteine protease shows significant long term half-life and impressive increased activity in presence of some chemical reagents.Scientific reports · 2021Article
- Identification, overexpression, purification, and biochemical characterization of a novel hyperthermostable keratinase from3 Biotech · 2021Article
- Structural and biochemical characterization of a novel thermophilic Coh01147 protease.PloS one · 2020Article
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Biotechnological applications of archaeal enzymes from extreme environments.Biological research · 2018Review
- Structural and functional studies of SAV0551 fromBioscience reports · 2017Article
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5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The PH1704 protease from hyperthermophilic archaean Pyrococcus horikoshii OT3 is a member of DJ-1/ThiJ/PfpI superfamily with diverse functional subclasses. The recombinant PH1704 was efficiently purified and was systematically characterized by a combination of substrate specificity analysis, steady-state kinetics study and molecular docking research. The homogeneous protease was obtained as a presumed dodecamer with molecular weight of ∼240 kDa. Iodoacetamide strongly inhibited the peptidase activity, confirming that Cys100 is a nucleophilic residue. The recombinant protein was identified as both an aminopeptidase and an endopeptidase. Experimental data showed that L-R-amc was the best substrate of PH1704. Structural interaction fingerprint analysis (SIFt) indicated the binding pose of PH1704 and showed that Tyr120 is important in substrate binding. Kinetic parameters Kcat and Kcat/Km of the Y120P mutant with L-R-amc was about 7 and 7.8 times higher than that of the wild type (WT). For the endopeptidase Y120P with AAFR-amc, Kcat and Kcat/Km is 10- and 21-fold higher than that of WT. Experimental data indicate the important functions of Tyr120: involvement in enzyme activity to form a hydrogen bond with Cys100 and as an entrance gate of the substrate with Lys43. The results of this study can be used to investigate the DJ-1/ThiJ/PfpI superfamily.
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