ArticleJournal of inorganic biochemistry2018
To what extent do structural changes in catalytic metal sites affect enzyme function?
Article in Journal of inorganic biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 77 citations in OpenAlex.
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- Iron: Life's primeval transition metal.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
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- Selective Oxidation of Halophenols Catalyzed by an Artificial Miniaturized Peroxidase.International journal of molecular sciences · 2023Article
- Essential oil-grafted copper nanoparticles as a potential next-generation fungicide for holistic disease management in maize.Frontiers in microbiology · 2023Article
- The zinc proteome of SARS-CoV-2.Metallomics : integrated biometal science · 2022Article
- Structural Bioinformatics and Deep Learning of Metalloproteins: Recent Advances and Applications.International journal of molecular sciences · 2022Review
- Learning to Identify Physiological and Adventitious Metal-Binding Sites in the Three-Dimensional Structures of Proteins by Following the Hints of a Deep Neural Network.Journal of chemical information and modeling · 2022Review
- The role of divalent iron cations in the growth, adhesive properties and extracellular adaptation mechanisms ofSaudi journal of biological sciences · 2022Article
- Innovation and tinkering in the evolution of oxidases.Protein science : a publication of the Protein Society · 2022Review
- Protein metalation in biology.Current opinion in chemical biology · 2022Review
- New Inhibitors of Laccase and Tyrosinase by Examination of Cross-Inhibition between Copper-Containing Enzymes.International journal of molecular sciences · 2021Article
- Interchangeable utilization of metals: New perspectives on the impacts of metal ions employed in ancient and extant biomolecules.The Journal of biological chemistry · 2021Review
- Force Field Parameters for FeMolecules (Basel, Switzerland) · 2021Article
- Analysis of Kojic Acid Derivatives as Competitive Inhibitors of Tyrosinase: A Molecular Modeling Approach.Molecules (Basel, Switzerland) · 2021Article
- Transfer hydrogenation catalysis in cells.RSC chemical biology · 2021Review
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
About half of known enzymatic reactions involve metals. Enzymes belonging to the same superfamily often evolve to catalyze different reactions on the same structural scaffold. The work presented here investigates how functional differentiation, within superfamilies that contain metalloenzymes, relates to structural changes at the catalytic metal site. In general, when the catalytic metal site is unchanged across the enzymes of a superfamily, the functional differentiation within the superfamily tends to be low and the mechanism conserved. Conversely, all types of structural changes in the metal binding site are observed for superfamilies with high functional differentiation. Overall, the catalytic role of the metal ions appears to be one of the most conserved features of the enzyme mechanism within metalloenzyme superfamilies. In particular, when the catalytic role of the metal ion does not involve a redox reaction (i.e. there is no exchange of electrons with the substrate), this role is almost always maintained even when the site undergoes significant structural changes. In these enzymes, functional diversification is most often associated with modifications in the surrounding protein matrix, which has changed so much that the enzyme chemistry is significantly altered. On the other hand, in more than 50% of the examples where the metal has a redox role in catalysis, changes at the metal site modify its catalytic role. Further, we find that there are no examples in our dataset where metal sites with a redox role are lost during evolution. SYNOPSIS: In this paper we investigate how functional diversity within superfamilies of metalloenzymes relates to structural changes at the catalytic metal site. Evolution tends to strictly conserve the metal site. When changes occur, they do not modify the catalytic role of non-redox metals whereas they affect the role of redox-active metals.
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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.