Structure of malhamensilipin A, an inhibitor of protein tyrosine kinase, from the cultured chrysophyte Poterioochromonas malhamensis.
A new chlorosulfolipid, malhamensilpin A [1] was isolated from the cultured chrysophyte Poterioochromonas malhamensis. Malhamensilipin A was demonstrated to be a modest inhibitor of pp60v-src protein tyrosine kinase. The structure was determined by detailed spectral analysis to be a novel C24 hexachloro lipid containing a vinyl sulfate ester (2,11,12,13,15,16-hexachloro-14-hydroxy-n-tetracos-1E-enol-1-sulfa te).
Chen
J L
JL
College of Pharmacy, Oregon State University, Corvallis 97331.
Proteau
P J
PJ
Roberts
M A
MA
Gerwick
W H
WH
Slate
D L
DL
Lee
R H
RH
D001419:Bacteria / Q000187:drug effects; D002850:Chromatography, Gel; D056890:Eukaryota / Q000737:chemistry*; D008055:Lipids / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D009682:Magnetic Resonance Spectroscopy; D008826:Microbial Sensitivity Tests; D011505:Protein-Tyrosine Kinases / Q000037:antagonists & inhibitors*
D008055:Lipids; C088109:malhamensilipin A; D011505:Protein-Tyrosine Kinases