Zulfiqar Hasan

TL;DR: The catalytic effects suggest that fine tuning of residues Lys-353 and Phe-397, along with addition of negative charge or removal of positive charge near one of the vanadate oxygens, is very important in peroxide activation and halide binding.

TL;DR: The work reported in this manuscript is the first example of 51V solid-state NMR spectroscopy applied to probe the vanadium center in a protein directly, and is expected to be generally applicable for studies of diamagnetic vanadium sites in metalloproteins.

TL;DR: The kinetics of the phosphorylation and dephosphorylation reaction catalysed by the acid phosphatases from Shigella flexneri and Salmonella enterica are examined, likely that this class of enzyme is able to phosphorylate a wide range of hydroxy compounds.

TL;DR: Site-directed mutagenesis on two conserved active site residues of vanadium chloroperoxidase (VCPO) from the fungus Curvularia inaequalis resulted in the enhancement of bromination activity under certain conditions, however, inactivation of F397H by halide especially at low pH was observed during turnover.

TL;DR: The immunolocalization approach, using the anti-rAePO polyclonal antibody, has revealed that the Pxd peroxidase is selectively localized in the chorion structures and particularly in the endochorion and innermost chorionic layer (ICL).