Arabidospsis thaliana PrRs (pinoresinol/lariciresinol reductases)
From Proteopedia
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1. '''General Aspects''' | 1. '''General Aspects''' | ||
| - | Pinoresinol/Lariciresinol Reductases ( | + | '''Pinoresinol/Lariciresinol Reductases (PLRs)''' are NADPH-dependent reductases that constitute a family of enzymes involved in the '''lignans''' biosynthetic pathway (Xiao et al., 2021). Lignans are secondary metabolites, formed by '''dimers of phenylpropanoids''', that can be present in all organs of non-vascular plants and Gymnosperms. Although their biological role is not yet totally clarified, they are associated mainly with plants defense mechanisms, especially towards herbivores and pathogenic microorganisms (Markulin et al., 2019). The presence or absence of the 8’,8’ bond between phenylpropanoid monomers differentiate lignans from neolignans, however overall both are associated with similar biological activities, including antiinflammatory, antioxidant, neuroprotective, antiviral, insecticidal and antitumor proliferation effects (Wang et al., 2022) Therefore, given the possibility of positively impacting human health, lignans are thoroughly explored by the pharmaceutical industry (Markulin et al., 2019). |
| - | Arabidopsis thaliana pinoresinol reductase 1 (AtPrR1) and A.thaliana pinoresinol reductase 2 (AtPrR2) are enzymes from the PLR family. These enzymes first reduce pinoresinol to lariciresinol and then lariciresinol to secoisolariciresinol (Nakatsubo et al., 2008). Even so, a study conducted by Nakastsubo and collaborators (2008) showed that the recombinant AtPLRs exhibit a strong preference for pinoresinol, having almost no activity regarding lariciresinol. Because of that difference towards the family of PLRs, AtPLRs have been renamed by these authors as pinoresinol reductases (PrRs). Phylogeny analysis shows Isatis indigotica PLR1 (IiPLR1) holds the biggest relationship to AtPrR, with more than 80% of amino-acid sequence identity. However, IlPLR1 is able to use both pinoresinol and lariciresinol as substrates, meaning that the substrate specificity in AtPrR is due to few aminoacid residues alterations, causing alterations in protein structure enlightened in the next sessions (Xiao et al., 2021). | + | '''''Arabidopsis thaliana'' pinoresinol reductase 1 (AtPrR1) and A.thaliana pinoresinol reductase 2 (AtPrR2)''' are enzymes from the PLR family. These enzymes first reduce pinoresinol to lariciresinol and then lariciresinol to secoisolariciresinol (Nakatsubo et al., 2008). Even so, a study conducted by Nakastsubo and collaborators (2008) showed that the recombinant AtPLRs exhibit a '''strong preference for pinoresinol''', having almost no activity regarding lariciresinol. Because of that difference towards the family of PLRs, AtPLRs have been renamed by these authors as '''pinoresinol reductases''' (PrRs). Phylogeny analysis shows Isatis indigotica PLR1 (IiPLR1) holds the biggest relationship to AtPrR, with more than 80% of amino-acid sequence identity. However, IlPLR1 is able to use both pinoresinol and lariciresinol as substrates, meaning that the substrate specificity in AtPrR is due to few aminoacid residues alterations, causing alterations in protein structure enlightened in the next sessions (Xiao et al., 2021). |
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Revision as of 21:17, 30 May 2024
Página sobre a PrR1 e PrR2 de Arabidopsis feita por alunos da Biologia da USP São Paulo.
1. General Aspects
Pinoresinol/Lariciresinol Reductases (PLRs) are NADPH-dependent reductases that constitute a family of enzymes involved in the lignans biosynthetic pathway (Xiao et al., 2021). Lignans are secondary metabolites, formed by dimers of phenylpropanoids, that can be present in all organs of non-vascular plants and Gymnosperms. Although their biological role is not yet totally clarified, they are associated mainly with plants defense mechanisms, especially towards herbivores and pathogenic microorganisms (Markulin et al., 2019). The presence or absence of the 8’,8’ bond between phenylpropanoid monomers differentiate lignans from neolignans, however overall both are associated with similar biological activities, including antiinflammatory, antioxidant, neuroprotective, antiviral, insecticidal and antitumor proliferation effects (Wang et al., 2022) Therefore, given the possibility of positively impacting human health, lignans are thoroughly explored by the pharmaceutical industry (Markulin et al., 2019).
Arabidopsis thaliana pinoresinol reductase 1 (AtPrR1) and A.thaliana pinoresinol reductase 2 (AtPrR2) are enzymes from the PLR family. These enzymes first reduce pinoresinol to lariciresinol and then lariciresinol to secoisolariciresinol (Nakatsubo et al., 2008). Even so, a study conducted by Nakastsubo and collaborators (2008) showed that the recombinant AtPLRs exhibit a strong preference for pinoresinol, having almost no activity regarding lariciresinol. Because of that difference towards the family of PLRs, AtPLRs have been renamed by these authors as pinoresinol reductases (PrRs). Phylogeny analysis shows Isatis indigotica PLR1 (IiPLR1) holds the biggest relationship to AtPrR, with more than 80% of amino-acid sequence identity. However, IlPLR1 is able to use both pinoresinol and lariciresinol as substrates, meaning that the substrate specificity in AtPrR is due to few aminoacid residues alterations, causing alterations in protein structure enlightened in the next sessions (Xiao et al., 2021).
2. Protein Structure
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Proteopedia Page Contributors and Editors (what is this?)
Gabriel Fontanella Pileggi, Maisa Ganz Sanchez Sennes, Melissa Siolin Martins, Michal Harel, Angel Herraez
