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Effect of NAD coenzyme on the inactivation of glyceraldehyde‐3‐phosphate dehydrogenase by anionic phospholipids
Author(s) -
Sidorowicz A.,
Modrzycka T.,
Gołebiowska J.,
Siemieniewski H.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81533-t
Subject(s) - nad+ kinase , glyceraldehyde 3 phosphate dehydrogenase , chemistry , cofactor , dehydrogenase , biochemistry , glyceraldehyde , coenzyme a , glycerol 3 phosphate dehydrogenase , phosphate , enzyme , reductase
The inactivation of bovine heart glyceraldehyde‐3‐phosphate dehydrogenase by phosphatidylinositol (PI) and phosphatidylserine (PS) in the form of liposomes was investigated in the presence and absence of NAD excess. In the absence of NAD, the enzyme activity decreased to about 50% of its initial value at 0.6 mM PI and 0.8 mM PS (lipid‐to‐protein molar ratio 600 and 800, respectively). In the same lipid concentration range almost full regainment of the activity was observed in the presence of 80 μM NAD. It was shown that the excess of NAD protects the enzyme against conformational change induced by the phospholipids. Centrifugation experiments showed that both PI and PS bind significant amounts of NAD.