Testimony of the Correlation Between the Reactive Histidine Residue and the Arginase Catalytic Mechanism Using a Biochromatographic Concept and Mutagenesis Experiments

In a previous paper (Bagnost et al., J Chromatogr B Analyt Technol Biomed Life Sci 853:38–46, 2007), an arginase chromatographic support was developed to study the association mechanism of arginase (an enzyme which can reduce endothelial dysfunction and blood pressure rising in spontaneously hypertensive rats) with nor-NOHA a potential inhibitor of its activity. In this report mutagenesis experiments associated with this biochromatographic approach confirmed that the active-site residue Hist 141 is protonated as imidazolium cation. Hist 141 could function as a general acid to protonate the leaving amino group of l-ornithine during catalysis.