Site-Directed Mutagenesis and Functional Analysis of the Active-Site Residues of the E2 Component of Bovine Branched-Chain α-Keto Acid Dehydrogenase Complex

Medicine & Life Sciences

• 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 89%
• isovaleryl-coenzyme A 82%
• Site-Directed Mutagenesis 59%
• Acyl Coenzyme A 56%
• dihydrolipoamide 54%
• Catalytic Domain 50%
• Cattle 44%
• Acetyl Coenzyme A 36%
• Histidine 30%
• isobutyryl-coenzyme A 28%
• Serine 27%
• acetoacetyl CoA 25%
• Chloramphenicol O-Acetyltransferase 18%
• Benzene 17%
• Coenzyme A 17%
• Hydrogen Bonding 16%
• Valine 16%
• Carbon Monoxide 14%
• Alanine 14%
• Buffers 12%
• Electrons 11%
• Escherichia coli 9%
• Enzymes 7%

Chemical Compounds

• Isovaleryl-CoA 100%
• Acyl-CoA 72%
• Dihydrolipoamide 59%
• Site-Directed Mutagenesis 58%
• Acetyl-CoA 46%
• Histidine 35%
• Serine 35%
• Transfer Reaction 34%
• Isobutyryl-CoA 33%
• Isobutyl Group 29%
• Acetoacetyl-CoA 29%
• Chloramphenicol 22%
• Valine 20%
• Acid 19%
• Alanine 17%
• Transition State 15%
• Absorption Spectrum 13%
• Benzene 12%
• Buffer Solution 12%
• Substitution Reaction 11%
• Hydrogen Bond 11%
• Mixture 8%
• pH Value 7%