ArticleBiotechnology and bioengineering2009
On the role of protein structural dynamics in the catalytic activity and thermostability of serine protease subtilisin Carlsberg.
Article in Biotechnology and bioengineering, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- Induction of IDO1 and Kynurenine by Serine Proteases Subtilisin, Prostate Specific Antigen, CD26 and HtrA: A New Form of Immunosuppression?Frontiers in immunology · 2022Article
- Graphene oxide as a protein matrix: influence on protein biophysical properties.Journal of nanobiotechnology · 2015Article
- Induction of Cancer Cell Death by Hyaluronic Acid-Mediated Uptake of Cytochrome C.Journal of nanomedicine & nanotechnology · 2015Article
- Chemical glycosylation of cytochrome c improves physical and chemical protein stability.BMC biochemistry · 2014Article
- Delivery of chemically glycosylated cytochrome c immobilized in mesoporous silica nanoparticles induces apoptosis in HeLa cancer cells.Molecular pharmaceutics · 2014Article
- Glycosylation improves α-chymotrypsin stability upon encapsulation in poly(lactic-co-glycolic)acid microspheres.Results in pharma sciences · 2012Article
- Moisture-induced solid state instabilities in alpha-chymotrypsin and their reduction through chemical glycosylation.BMC biotechnology · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The effect of structural dynamics on enzyme activity and thermostability has thus far only been investigated in detail for the serine protease alpha-chymotrypsin (for a recent review see Solá et al., Cell Mol Life Sci 2007, 64(16): 2133-2152). Herein, we extend this type of study to a structurally unrelated serine protease, specifically, subtilisin Carlsberg. The protease was incrementally glycosylated with chemically activated lactose to obtain various subtilisin glycoconjugates which were biophysically characterized. Near UV-CD spectroscopy revealed that the tertiary structure was unaffected by the glycosylation procedure. H/D exchange FT-IR spectroscopy was performed to assess the changes in structural dynamics of the enzyme. It was found that increasing the level of glycosylation caused a linearly dependent reduction in structural dynamics. This led to an increase in thermostability and a decrease in the catalytic turnover rate for both, the enzyme acylation and deacylation steps. These results highlight the possibility that a structural dynamics-activity relationship might be a phenomenon generally found in serine proteases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.