The molecular basis of ornithine transcarbamylase deficiency: Modelling the human enzyme and the effects of mutations

Keyphrases

• Mutation Effect 100%
• Ornithine Transcarbamylase Deficiency 100%
• Human Enzymes 100%
• Binding Site 50%
• Aspartate Transcarbamoylase 50%
• Escherichia Coli 33%
• Catalytic Subunit 33%
• Predicted Effects 16%
• Conserved Residues 16%
• Side Chain 16%
• Trimer 16%
• Missense mutation 16%
• 3D Structure 16%
• Structural Domains 16%
• Ornithine 16%
• Phosphate 16%
• Late-onset 16%
• In-frame Deletion 16%
• Hydrophobic Region 16%
• Charged Residue 16%
• Active Sites 16%
• Positively Charged 16%
• Negatively Charged 16%
• Three Dimensional Model 16%
• Functional Domain 16%
• Amino Acid Sequence Homology 16%
• Holoenzyme 16%
• Predictive Distribution 16%
• Hyperammonemia 16%
• Secondary Structure Prediction 16%
• L-aspartate 16%

Biochemistry, Genetics and Molecular Biology

• Enzyme 100%
• Ornithine Transcarbamylase 100%
• Ornithine Transcarbamylase Deficiency 100%
• Binding Site 60%
• Aspartate Carbamoyltransferase 60%
• Enzyme Active Site 40%
• Crystal Structure 20%
• Protein Secondary Structure 20%
• Missense Mutation 20%
• Sequence Homology 20%
• Active Site 20%
• Aspartic Acid 20%
• Ornithine 20%