Mutations in a putative zinc-binding domain inactivate the mitochondrial intermediate peptidase

Medicine & Life Sciences

• mitochondrial intermediate peptidase 100%
• Zinc 45%
• Mutation 26%
• Histidine 20%
• N,N-diethyl-2-(1-pyridyl)ethylamine 16%
• Glutamic Acid 16%
• Cysteine Proteases 11%
• Divalent Cations 11%
• Protein Stability 11%
• Mitochondrial Proteins 10%
• Sulfhydryl Compounds 10%
• Site-Directed Mutagenesis 10%
• Metalloproteases 10%
• Cysteine 8%
• Peptide Hydrolases 7%
• In Vitro Techniques 4%

Chemical Compounds

• Glutamic Acid 50%
• Histidine 44%
• Mutation 40%
• Cysteine Residue 24%
• Site-Directed Mutagenesis 24%
• Monoatomic Dication 24%
• Protein 19%