Abstract
We synthesised analogues of diphosphoinositol polyphosphates (PP-InsPs) in which the diphosphate is replaced by an α-phosphonoacetic acid (PA) ester. Structural analysis revealed that 5-PA-InsP(5) mimics 5-PP-InsP(5) binding to the kinase domain of PPIP5K2; both molecules were phosphorylated by the enzyme. PA-InsPs are promising candidates for further studies into the biology of PP-InsPs.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
-
Binding Sites
-
Biocatalysis
-
Catalytic Domain
-
Crystallography, X-Ray
-
Humans
-
Inositol Phosphates / chemistry
-
Phosphotransferases (Phosphate Group Acceptor) / chemistry
-
Phosphotransferases (Phosphate Group Acceptor) / metabolism*
-
Polyphosphates / chemistry
-
Polyphosphates / metabolism*
-
Substrate Specificity
Substances
-
Inositol Phosphates
-
Polyphosphates
-
Phosphotransferases (Phosphate Group Acceptor)
-
diphosphoinositol pentakisphosphate kinase