Title : The antiproliferative agent didemnin B uncompetitively inhibits palmitoyl protein thioesterase.

Pub. Date : 1998 Jul 21

PMID : 9671519






5 Functional Relationships(s)
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1 While the palmitoyl protein thioesterase(s) responsible for depalmitoylation of plasma membrane-associated signaling proteins has (have) not been identified, the lysosomal palmitoyl protein thioesterase 1 (PPT1) has proven useful in in vitro studies of membrane localization requirements of GTP-binding proteins. Guanosine Triphosphate palmitoyl-protein thioesterase 1 Homo sapiens
2 While the palmitoyl protein thioesterase(s) responsible for depalmitoylation of plasma membrane-associated signaling proteins has (have) not been identified, the lysosomal palmitoyl protein thioesterase 1 (PPT1) has proven useful in in vitro studies of membrane localization requirements of GTP-binding proteins. Guanosine Triphosphate palmitoyl-protein thioesterase 1 Homo sapiens
3 Didemnin B was shown to inhibit recombinant human PPT1 with a Ki of 92 nM. didemnins palmitoyl-protein thioesterase 1 Homo sapiens
4 Kinetic analysis of this inhibition revealed that didemnin B inhibits PPT1 uncompetitively. didemnins palmitoyl-protein thioesterase 1 Homo sapiens
5 As the first described inhibitor of PPT1, didemnin B may prove to be a useful tool in the investigation of protein palmitoylation regulation. didemnins palmitoyl-protein thioesterase 1 Homo sapiens