Isolation of a Novel Tyrosine Kinase Inhibitor, Lavendustin A, from Streptomyces griseolavendus
- 1 November 1989
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of Natural Products
- Vol. 52 (6), 1252-1257
- https://doi.org/10.1021/np50066a009
Abstract
A potent tyrosine kinase inhibitor, lavendustin A [1], has been isolated from a butyl acetate extract of Streptomyces griseolavendus culture filtrate. It inhibits epidermal growth factor receptor-associated tyrosine kinase with an IC50 of 4.4 ng/ml, which is about 50 times more inhibitory than erbstatin. It does not inhibit protein kinase A or C. Its structure, determined by spectra data and total synthesis, is novel, having a tertiary amine in the center with substituted benzyl and phenyl groups. Lavendustin A competes with ATP and is noncompetitive with the peptide. Its structure-activity relationship is discussed.This publication has 4 references indexed in Scilit:
- INSITU INHIBITION OF TYROSINE PROTEIN-KINASE BY ERBSTATIN1987
- The kinetics of tyrosine phosphorylation by the purified epidermal growth factor receptor kinase of A-431 cells.Journal of Biological Chemistry, 1983
- Phosphorylation of synthetic peptides by a tyrosine protein kinase from the particulate fraction of a lymphoma cell line.Proceedings of the National Academy of Sciences of the United States of America, 1982
- Rapid isolation of plasma membranes in high yield from cultured fibroblastsBiochemical Journal, 1977