EC Number |
Inhibitors |
Structure |
---|
2.7.1.127 | (2'S)-1D-1,2-O-[(2'-phosphoryloxy)propane-1',3'-diyl]-myo-inositol 4,5-bisphosphate |
synthetic bicyclic inositol trisphosphate S epimer, IC50 is 0.156 mM |
|
2.7.1.127 | 1D-myo-inositol 1,3,4,5-tetrakisphosphate |
marked product inhibition, isoforms A and B |
|
2.7.1.127 | 1D-myo-inositol 1,3,4,5-tetrakisphosphate |
product inhibition, IC50 is 0.013 mM |
|
2.7.1.127 | 1D-myo-inositol 1,4,5-trisphosphate |
recombinant, catalytically active fragment of isoform C, substrate inhibition by high concentrations |
|
2.7.1.127 | 1D-myo-inositol 1,4,5-trisphosphate |
substrate inhibition of the catalytic domain |
|
2.7.1.127 | 2,3-diphosphoglycerate |
- |
|
2.7.1.127 | 2-[3,5-dimethyl-1-(4-nitrophenyl)-1H-pyrazol-4-yl]-5,8-dinitro-1H-benzo[de]isoquinoline-1,3(2H)-dione |
BIP-4, BIP-4 is competitive to Ins(1,4,5)P3 and shows high selectivity for the Ins(1,4,5)P3 binding pocket, BIP-4 does not block the actin bundling activity of ITPKA |
|
2.7.1.127 | 3',4',7,8-tetrahydroxyflavone |
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate |
|
2.7.1.127 | 3',4',7,8-tetrahydroxyflavone |
inhibition of isozyme A, mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate |
|
2.7.1.127 | 3',4',7,8-tetrahydroxyflavone |
the point mutant K336Q reveals a drastically reduced inhibition by THF. Substitution of Lys336 leads to a 260fold increase in the IC50. On the other hand, kinetic parameters of the enzyme with respect to both substrates are nearly unchanged. This region shows high homology between IP3K isoforms. |
|