Metal-dependent enzyme symmetry guides the biosynthetic flux of terpene precursors

Keyphrases

• Terpenes 100%
• Geranylgeranyl Pyrophosphate 100%
• Metal-dependent Enzyme 100%
• Farnesyl Pyrophosphate 66%
• Isopentenyl Diphosphate Isomerase 66%
• Metal Ions 33%
• Carbon Skeleton 33%
• Chain Length 33%
• Reaction Mechanism 33%
• Terpenoids 33%
• Bifunctional 33%
• Cooperative Effects 33%
• Functional Analysis 33%
• Binding Site 33%
• All-natural 33%
• Natural Products 33%
• Specific Binding 33%
• Homodimer 33%
• Physiological Development 33%
• Product Inhibition 33%
• Metal-dependent 33%
• Isoprenoids 33%
• Length Determination 33%
• Ligand Affinity 33%
• Metal Ion Concentration 33%
• Leaf Beetles 33%
• Phaedon Cochleariae 33%
• Human Farnesyl Pyrophosphate Synthase 33%
• Dynamic Potential 33%
• Biological Defense 33%

Biochemistry, Genetics and Molecular Biology

• Enzyme 100%
• Precursor 100%
• Pyrophosphate 100%
• Synthase 75%
• Farnesyl Pyrophosphate 75%
• Product Inhibition 25%
• Chrysomelidae 25%
• Binding Site 25%
• Phaedon cochleariae 25%