ReviewBioMed research international2013
Extremophilic SHMTs: from structure to biotechnology.
Review in BioMed research international, 2013. 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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Who cites it
10 citing papers in PubMed.
- Characterization of thermostable serine hydroxymethyltransferase for β-hydroxy amino acids synthesis.Amino acids · 2023Article
- Serine and one-carbon metabolisms bring new therapeutic venues in prostate cancer.Discover oncology · 2021Review
- Heterologous gene expression and characterization of two serine hydroxymethyltransferases from Thermoplasma acidophilum.Extremophiles : life under extreme conditions · 2021Article
- Exploring the Cold-Adaptation Mechanism of Serine Hydroxymethyltransferase by Comparative Molecular Dynamics Simulations.International journal of molecular sciences · 2021Article
- Novel Enzymes From the Red Sea Brine Pools: Current State and Potential.Frontiers in microbiology · 2021Review
- Functional Identification of Serine Hydroxymethyltransferase as a Key Gene Involved in Lysostaphin Resistance and Virulence Potential ofInternational journal of molecular sciences · 2020Article
- Editorial: PLP-Dependent Enzymes: Extraordinary Versatile Catalysts and Ideal Biotechnological Tools for the Production of Unnatural Amino Acids and Related Compounds.Frontiers in bioengineering and biotechnology · 2020Article
- Determinants of Thermostability in Serine Hydroxymethyltransferase Identified by Principal Component Analysis.Scientific reports · 2017Article
- Cytosine-type nucleosides from marine-derived Streptomyces rochei 06CM016.The Journal of antibiotics · 2016Article
- Kinetic mechanism and the rate-limiting step of Plasmodium vivax serine hydroxymethyltransferase.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent advances in molecular and structural biology have improved the availability of virtually any biocatalyst in large quantity and have also provided an insight into the detailed structure-function relationships of many of them. These results allowed the rational exploitation of biocatalysts for use in organic synthesis. In this context, extremophilic enzymes are extensively studied for their potential interest for many biotechnological and industrial applications, as they offer increased rates of reactions, higher substrate solubility, and/or longer enzyme half-lives at the conditions of industrial processes. Serine hydroxymethyltransferase (SHMT), for its ubiquitous nature, represents a suitable model for analyzing enzyme adaptation to extreme environments. In fact, many SHMT sequences from Eukarya, Eubacteria and Archaea are available in data banks as well as several crystal structures. In addition, SHMT is structurally conserved because of its critical metabolic role; consequently, very few structural changes have occurred during evolution. Our research group analyzed the molecular basis of SHMT adaptation to high and low temperatures, using experimental and comparative in silico approaches. These structural and functional studies of SHMTs purified from extremophilic organisms can help to understand the peculiarities of the enzyme activity at extreme temperatures, indicating possible strategies for rational enzyme engineering.
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