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Structure-activity relationships of the nikkomycins.

Journal of general microbiology (1991-08-01)
H Decker, H Zähner, H Heitsch, W A König, H P Fiedler
ANOTACE

The structure-activity relationships of different nikkomycins were studied to evaluate the structural requirements for a potent chitin synthase inhibitor. We investigated the transport of the nikkomycins via the peptide transport system of the yeast Yarrowia lipolytica and determined the kinetic parameters for nikkomycin Z uptake [Km = 24 microM, Vmax = 2.2 nmol min-1 (mg dry wt)-1]. We demonstrated that the beta-methyl group of the N-terminal amino acid of dipeptide nikkomycins protects the molecule against peptidase activity in crude cell-extracts of different fungi. Furthermore, the relationship between inhibition constants for chitin synthase, transport of the nikkomycins via the peptide transport system, susceptibility to degradation by cellular proteases and whole-cell activity of the nikkomycins are discussed.

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Sigma-Aldrich
Nikkomycin Z from Streptomyces tendae, ≥90% (HPLC)