Identification of an active-site residue in subunit S1 of pertussis toxin by photocrosslinking to NAD
- 5 June 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 249 (2), 329-332
- https://doi.org/10.1016/0014-5793(89)80652-0
Abstract
The site of interaction of NAD with the isolated S1 subunit of pertussis toxin was investigated by photoaffinity labelling. When S1 was irradiated at 254 nm in the presence of [carbonyl-14C]- or [adenine-14C]NAD, the uptake of radioactivity was equivalent to 0.75 and 0.1 mol/mol respectively, while the NAD glycohydrolase activity was abolished. Inactivation was thus accompanied by crosslinking of the nicotinamide portion of NAD to the protein. Sequence determination of purified radioactive peptides indicated that Glu-129 was a major site of labelling. This residue is therefore closely associated with either NAD binding or hydrolysisKeywords
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