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Cleavage of nicotinamide adenine dinucleotide by the ribosome‐inactivating protein from Momordica charantia
Author(s) -
Vinkovic M.,
Dunn G.,
Wood G. E.,
Husain J.,
Wood S. P.,
Gill R.
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15013540
Subject(s) - momordica , nicotinamide adenine dinucleotide , chemistry , stereochemistry , ribose , nad+ kinase , cleavage (geology) , active site , ribosome , nicotinamide , ribosome inactivating protein , nicotinamide adenine dinucleotide phosphate , enzyme , nucleotide , biochemistry , rna , biology , oxidase test , medicine , paleontology , fracture (geology) , gene , traditional medicine
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.