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

Abstract

The catalytic properties of the type II phosphoinositide 5-phosphatases of Lowe's oculocerebrorenal 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 KM and VMax values. They also possessed an exclusive sensitivity towards fatty acid composition, head group phosphorylation and 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.

• Authors: Annette C Schmid, Helen M Wise, Christina A Mitchell, Robert Nussbaum, Rüdiger Woscholski
• Journal: FEBS letters (FEBS Lett) Vol. 576 Issue 1-2 Pg. 9-13 (Oct 08 2004) ISSN: 0014-5793 [Print] England
• PMID: 15474001 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright 2004 Federation of European Biochemical Societies

Chemical References

• Fatty Acids
• Nerve Tissue Proteins
• Phosphatidylinositols
• Recombinant Proteins
• synaptojanin
• Phosphoric Monoester Hydrolases

Topics

• Animals
• Catalysis
• Catalytic Domain
• Escherichia coli (genetics)
• Fatty Acids (chemistry)
• Humans
• Kinetics
• Mice
• Nerve Tissue Proteins (chemistry, genetics, metabolism)
• Oculocerebrorenal Syndrome (enzymology)
• Phosphatidylinositols (metabolism)
• Phosphoric Monoester Hydrolases (chemistry, classification, genetics, metabolism)
• Phosphorylation
• Protein Structure, Tertiary
• Recombinant Proteins (metabolism)
• Substrate Specificity