Journal: Synthetic and Systems Biotechnology

Article Title: Identification, characterization, and application of an NADPH-dependent carbonyl reductase in Saccharomyces cerevisiae AS2.346 for improving production of (13R,17S)-ethyl secol

doi: 10.1016/j.synbio.2025.04.016

Figure Lengend Snippet: Identification, characterization of AsSDR1 and AsSDR2. (a) Saccharomyces cerevisiae AS2.346 transformation reaction; (b) Phylogenetic analysis of carbonyl reductases. The phylogenetic tree was constructed based on the alignment of full amino acid sequences. All analyzed sequences of reductase enzymes were retrieved from GenBank and SGD; (c) Biotransformation reaction of recombination E. coli .

Article Snippet: Molecular Dynamics Simulation Results of AsSDR1 and AsSDR2. (a) Protein-substrate MD distance of AsSDR1 and AsSDR2; (b) diagram of the protein-substrate binding patterns of AsSDR1; (c) diagram of the protein-substrate binding patterns of AsSDR2.

Techniques: Transformation Assay, Construct

Journal: Synthetic and Systems Biotechnology

Article Title: Identification, characterization, and application of an NADPH-dependent carbonyl reductase in Saccharomyces cerevisiae AS2.346 for improving production of (13R,17S)-ethyl secol

doi: 10.1016/j.synbio.2025.04.016

Figure Lengend Snippet: Molecular Dynamics Simulation Results of AsSDR1 and AsSDR2. (a) Protein-substrate MD distance of AsSDR1 and AsSDR2; (b) diagram of the protein-substrate binding patterns of AsSDR1; (c) diagram of the protein-substrate binding patterns of AsSDR2.

Article Snippet: Molecular Dynamics Simulation Results of AsSDR1 and AsSDR2. (a) Protein-substrate MD distance of AsSDR1 and AsSDR2; (b) diagram of the protein-substrate binding patterns of AsSDR1; (c) diagram of the protein-substrate binding patterns of AsSDR2.

Techniques: Binding Assay

Journal: Synthetic and Systems Biotechnology

Article Title: Identification, characterization, and application of an NADPH-dependent carbonyl reductase in Saccharomyces cerevisiae AS2.346 for improving production of (13R,17S)-ethyl secol

doi: 10.1016/j.synbio.2025.04.016

Figure Lengend Snippet: Optimal Reaction Conditions for AsSDR1 and AsSDR2. (a) Purifed enzymes were reacted at different temperatures and assayed at various temperatures from 20 to 50 °C; (b) Purified enzymes were mixed with different buffers and assayed at various pH values, from 3.0 to 10.0. The values provided are the means of three independent replicates.

Article Snippet: Molecular Dynamics Simulation Results of AsSDR1 and AsSDR2. (a) Protein-substrate MD distance of AsSDR1 and AsSDR2; (b) diagram of the protein-substrate binding patterns of AsSDR1; (c) diagram of the protein-substrate binding patterns of AsSDR2.

Techniques: Purification

Journal: Scientific Reports

Article Title: Urolithin A suppressed osteosarcoma cell migration and invasion via targeting MMPs and AKT1

doi: 10.1038/s41598-025-11804-2

Figure Lengend Snippet: Stable interaction of UA with the kinase domain of AKT1. Plots generated from 100 ns molecular dynamics simulations, demonstrating structural and energetic properties of the UA-AKT1 complex: RMSD ( A ), RMSF ( B ), Rg ( C ), and SASA ( D ), short-range Coulombic potential ( E ) and short-range Lennard-Jones potential ( F ).

Article Snippet: Plots generated from 100 ns molecular dynamics simulations, demonstrating structural and energetic properties of the UA-AKT1 complex: RMSD ( A ), RMSF ( B ), Rg ( C ), and SASA ( D ), short-range Coulombic potential ( E ) and short-range Lennard-Jones potential ( F ).

Techniques: Generated