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    Cleavage of nicotinamide adenine dinucleotide by the ribosome-inactivating protein fromMomordica charantia

    Vinkovic, M. and Dunn, G. and Wood, G.E. and Husain, Jasmine and Wood, S.P. and Gill, R. (2015) Cleavage of nicotinamide adenine dinucleotide by the ribosome-inactivating protein fromMomordica charantia. Acta Crystallographica Section F: Structural Biology Communications 71 (9), pp. 1152-1155. ISSN 1744-3091.

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    Abstract

    The 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.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): ribosome-inactivating protein, N-glycosidase, nicotinamide, crystal structure, momordin
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 10 Sep 2015 09:05
    Last Modified: 10 Sep 2015 09:05
    URI: http://eprints.bbk.ac.uk/id/eprint/12937

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