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Cleavage of nicotinamide adenine dinucleotide by the ribosome-inactivating protein fromMomordica charantia
journal contribution
posted on 2023-06-09, 04:36 authored by M Vinkovic, G Dunn, G E Wood, J Husain, S P Wood, R GillThe interaction of momordin, a type 1 ribosome-inactivating protein from Momordica charantia, with NADP(+) and NADPH has been investigated by X-ray diffraction analysis of complexes generated by co-crystallization and crystal soaking. It is known that the proteins of this family readily cleave the adenine-ribose bond of adenosine and related nucleotides in the crystal, leaving the product, adenine, bound to the enzyme active site. Surprisingly, the nicotinamide-ribose bond of oxidized NADP(+) is cleaved, leaving nicotinamide bound in the active site in the same position but in a slightly different orientation to that of the five-membered ring of adenine. No binding or cleavage of NADPH was observed at pH 7.4 in these experiments. These observations are in accord with current views of the enzyme mechanism and may contribute to ongoing searches for effective inhibitors.
History
Publication status
- Published
Journal
Acta Crystallographica Section F: Structural Biology CommunicationsISSN
2053-230XPublisher
International Union of CrystallographyExternal DOI
Issue
9Volume
71Page range
1152-1155Department affiliated with
- Chemistry Publications
Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2017-01-09Usage metrics
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