ISSN:
1432-072X
Keywords:
Saccharomyces cerevisiae
;
Yeast
;
Phospholipase B
;
Lysophospholipase
;
Enzyme inhibition
;
AMP
;
Unesterified fatty acids
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
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 μM. The inhibition by nucleotides in low concentrations is enhanced by divalent cations.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00414431
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