... consist of two domains, a large a ⁄ bdomain and a small a domain with the catalytic site at the interface of the two domains [4,5]. HAPs can initi-ate hydrolysis of phytate at either the C3(EC ... smaller than for AppA, showing that binding is favored by the preformed site. By con-trast, catalysis by AppA is faster, as reflected in the values for kcat⁄ Km, indicating that a conformationallyflexible ... December2009)doi:10.1111/j.1742-4658.2010.07559.x The extracellular phytase of the plant-associated Klebsiella sp. ASR1 is a member of the histidine-acid-phosphatase family and acts primarily as a scavenger of phosphate groups locked in the...