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Acylation of adenylyl cyclase catalyst is important for enzymic activity
Author(s) -
Stefan Mollner,
Krista Beck,
Thomas Pfeuffer
Publication year - 1995
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(95)00864-6
Subject(s) - adenylyl cyclase , chemistry , hydroxylamine , catalysis , adcy10 , adcy9 , biochemistry , gs alpha subunit , incubation , palmitic acid , enzyme , fatty acid
Incubation of human thrombocytes in the presence of [ 3 H]palmitic acid leads to incorporation of this fatty acid into the α subunit of G s as described [Linder et al., Proc. Natl. Acad. Sci. USA 90 (1993) 3675–3679; Degtyarev et al., Biochemistry 32 (1993) 8057–8061] but also into the catalyst of adenylyl cyclase which has not been recognized before. Treatment of labeled membranes with hydroxylamine released the label from both components. Label incorporated into the catalyst could be identified as [ 3 H]palmitate. At the same time chemical deacylation caused partial loss of adenylyl cyclase activity.