The crystal structure of palmitoyl protein thioesterase-2 (PPT2) reveals the basis for divergent substrate specificities of the two lysosomal thioesterases, PPT1 and PPT2

Keyphrases

• Substrate Specificity 100%
• Acyl Protein Thioesterase 100%
• Thioesterases 100%
• Fatty Acids 11%
• Neuronal Ceroid Lipofuscinosis 11%
• Palmitoyl-CoA 11%
• Lipid Binding 11%
• Palmitoylated Proteins 11%
• Palmitate 5%
• Structural Difference 5%
• Modified Proteins 5%
• Transgenic Mouse Model 5%
• Helix 5%
• Lysosomal Storage Disease 5%
• Lysosomal Acid Lipase 5%
• Biological Basis 5%
• Intellectual Disability 5%
• Thioester 5%
• Conformational Differences 5%
• Catabolism 5%
• Cortical Neurons 5%
• Granular Deposits 5%
• Protein Substrate 5%
• Architectural Features 5%
• Infantile Form 5%
• Head Group 5%
• Acid Modified 5%
• Fatty Acid Chain Length 5%
• Parallel Loops 5%
• Chain-Length Selectivity 5%

Biochemistry, Genetics and Molecular Biology

• Crystal Structure 100%
• Enzyme Specificity 100%
• Palmitoyl Protein Thioesterase 100%
• Enzymatic Hydrolysis 11%
• Lipid 11%
• Batten Disease 11%
• Neuronal Ceroid Lipofuscinosis 11%
• Palmitoyl-CoA 11%
• Mouse Model 5%
• Transgenic Mouse 5%
• Hydrolase 5%
• Thioester 5%
• Palmitic Acid 5%
• Deficiency 5%