Molecular basis of cysteine biosynthesis in plants: Structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana

Keyphrases

• Functional Analysis 100%
• Arabidopsis Thaliana 100%
• O-acetylserine Sulfhydrylase 100%
• Cysteine Biosynthesis 100%
• Pyridoxal 5′-phosphate 60%
• Methionine 60%
• Cysteine 40%
• O-acetylserine 40%
• Protein-protein Interaction 20%
• Amino Acids 20%
• Active Sites 20%
• Ligand Binding 20%
• Glutathione 20%
• Site-directed mutagenesis 20%
• Titration 20%
• Metabolic 20%
• Kinetic Analysis 20%
• Functional Role 20%
• Binding Residues 20%
• Vitamins 20%
• Sulfur Incorporation 20%
• Iron-sulfur Cluster 20%
• Bacterial Enzymes 20%
• Inorganic Sulfur 20%
• Key Amino Acids 20%
• Secondary Metabolites 20%
• Conserved Set 20%
• Active Loop 20%
• Phytochelatins 20%
• Serine Acetyltransferase 20%
• External Aldimine 20%
• Phosphate Binding 20%
• CRISTAL 20%
• Interaction Experiment 20%
• Surface Loops 20%
• Sulfide Donors 20%

Biochemistry, Genetics and Molecular Biology

• Anabolism 100%
• Arabidopsis thaliana 100%
• Cysteine 100%
• Active Site 50%
• Methionine 50%
• Pyridoxal Phosphate 50%
• Enzyme 33%
• Amino Acids 33%
• Crystal Structure 16%
• Protein-Protein Interaction 16%
• Ligand Binding 16%
• Site-Directed Mutagenesis 16%
• N-Acetyltransferase 16%
• Iron-Sulfur Cluster 16%
• Secondary Metabolite 16%
• Sulfide 16%
• Thioether 16%
• Serine 16%
• Glutathione 16%
• Phytochelatin 16%