Type II phosphoinositide 5-phosphatases have unique sensitivities towards fatty acid composition and head group phosphorylation

The catalytic properties of the type II phosphoinositide 5-phosphatases of Lowe's oculocercbrorenal syndrome, INPP5B, Synaptojanin1, Synaptojanin2 and SKIP were analysed with respect to their substrate specificity and enzymological properties. Our data reveal that all phosphatases have unique substrate specificities as judged by their corresponding K-M and V-Max values. They also possessed an exclusive sensitivity towards fatty acid composition, head group phosphorylation an micellar presentation. Thus, the biological function of these enzymes will not just be determined by their corresponding regulatory domains, but will be distinctly influenced by their catalytic properties as well. This suggests that the phosphatase domains fulfil a unique catalytic function that cannot be fully compensated by other: phosphatases. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.