Article
Role of conserved active site tryptophan-101 in functional activity and stability of phosphoserine aminotransferase from an enteric human parasite.
Amino acids - 1 Jul 2012
Mishra Vibhor, Kumar Ashutosh, Ali Vahab, Nozaki Tomoyoshi, Zhang Kam Y J, Bhakuni Vinod
Abstract excerpt
Site-directed mutagenesis study was performed to elucidate the role of conserved tryptophan-101 present at the active site of phosphoserine aminotransferase from an enteric human parasite Entamoeba histolytica. Fluorescence resonance energy transfer and molecular dynamic simulation show that the indole ring of Trp101 stacks with the cofactor PLP. Loss of enzymatic activity and PLP...
Topics
- Amino Acid Sequence
- Catalytic Domain
- Entamoeba histolytica
- Enzyme Stability
- Fluorescence Resonance Energy Transfer
- Humans
- Models, Molecular
- Molecular Dynamics Simulation
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Protein Conformation