Ascorbate peroxidase, a haem protein （EC 1.11.1.11）, efficiently scavenges hydrogen peroxide （H2O2） in cytosol and chloroplasts of plants. In this study, a fulllength coding sequence of thylakoid-bound ascorbate p...Ascorbate peroxidase, a haem protein （EC 1.11.1.11）, efficiently scavenges hydrogen peroxide （H2O2） in cytosol and chloroplasts of plants. In this study, a fulllength coding sequence of thylakoid-bound ascorbate peroxidase cDNA （TatAPX） was cloned from a drought tolerant wheat cultivar C306. Homology modeling of the TatAPX protein was performed by using the template crystal structure of chloroplastic ascorbate peroxidase from tobacco plant （PDB： IIYN）. The model structure was further refined by molecular mechanics and dynamic methods using various tools such as PROCHECK, ProSA and Verify3D. The predicted model was then tested for docking with H2O2, the substrate for TatAPX enzyme. The results revealed that Arg233 and Glu255 in the predicted active site of the enzyme are two important amino acid residues responsible for strong hydrogen bonding affinity with H2O2, which might play an important role in scavenging of H2O2 from the plant system.展开更多
基金supported by the Indian Council of Agricultural Research (ICAR)sponsored Network Project on Transgenics in Crops (NPTC)
文摘Ascorbate peroxidase, a haem protein （EC 1.11.1.11）, efficiently scavenges hydrogen peroxide （H2O2） in cytosol and chloroplasts of plants. In this study, a fulllength coding sequence of thylakoid-bound ascorbate peroxidase cDNA （TatAPX） was cloned from a drought tolerant wheat cultivar C306. Homology modeling of the TatAPX protein was performed by using the template crystal structure of chloroplastic ascorbate peroxidase from tobacco plant （PDB： IIYN）. The model structure was further refined by molecular mechanics and dynamic methods using various tools such as PROCHECK, ProSA and Verify3D. The predicted model was then tested for docking with H2O2, the substrate for TatAPX enzyme. The results revealed that Arg233 and Glu255 in the predicted active site of the enzyme are two important amino acid residues responsible for strong hydrogen bonding affinity with H2O2, which might play an important role in scavenging of H2O2 from the plant system.
