| Literature DB >> 2655549 |
W Witt1, P Hampel, K Böcker, A Mertsching.
Abstract
Divalent cations activate the lysophospholipase and transacylase reactions catalyzed by the same enzymes in the yeast Saccharomyces cerevisiae. The activation was observed at neutral pH, but not at the pH optimum of lysophospholipase/transacylase, near 3.5. Adenine nucleotides, especially AMP and ADP, are strong inhibitors of the same group of enzymes. Half maximal inhibition by AMP was found at a concentration of about 20 microM. The inhibition by nucleotides in low concentrations is enhanced by divalent cations.Entities:
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Year: 1989 PMID: 2655549 DOI: 10.1007/bf00414431
Source DB: PubMed Journal: Arch Microbiol ISSN: 0302-8933 Impact factor: 2.552