Structural-functional relationships in pig heart AMP-deaminase in the presence of ATP, orthophosphate, and phosphatidate bilayers.

Autor: Tanfani F; Institute of Biochemistry, University of Ancona, Ancona, Via Ranieri, 60131, Italy. Tanfani@popcsi.unian.it, Kulawiak D, Kossowska E, Preis JP, Zydowo MM, Sarkissova E, Bertoli E, Wozniak M
Jazyk: angličtina
Zdroj: Molecular genetics and metabolism [Mol Genet Metab] 1998 Sep; Vol. 65 (1), pp. 51-8.
DOI: 10.1006/mgme.1998.2740
Abstrakt: The secondary structure of pig heart AMP-deaminase (AMP-d) in the absence and in the presence of orthophosphate or dioleoyl phosphatidic acid (DOPA) or ATP was investigated by FT-IR spectroscopy. While the latter substance activates the enzyme, orthophosphate is a well-known negative allosteric effector and DOPA exerts a noncompetitive inhibition on AMP-deaminase. Small changes in the secondary structure of AMP-d were induced by the above mentioned substances. Only DOPA reduced the thermal stability of AMP-d and avoided protein intermolecular interactions suggesting structural-functional relationships in AMP-d in the presence of the above substances and a possible role of phosphatidic acid in the subtle regulation of AMP-d activity by temporary binding of the enzyme to cellular membranes.
(Copyright 1998 Academic Press.)
Databáze: MEDLINE
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