ArticleThe Biochemical journal2002
A 13C-NMR study of the inhibition of papain by a dipeptide-glyoxal inhibitor.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 8 citations in OpenAlex.
- Quantifying tetrahedral adduct formation and stabilization in the cysteine and the serine proteases.Biochimica et biophysica acta · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Z-Phe-Ala-glyoxal (where Z is benzyloxycarbonyl) has been synthesized and shown to be a competitive inhibitor of papain with a K(i)=3.30+/-0.25 nM. (13)C-NMR has been used to show that in aqueous media, Z-Phe-[2-(13)C]Ala-glyoxal gives signals at 207.7 p.p.m. and 96.3 p.p.m. showing that both the alpha-keto carbon and its hydrate are present. When this inhibitor is bound to papain a single signal at 209.7 p.p.m. is observed due to the (13)C-enriched carbon. This demonstrates that the glyoxal alpha-keto carbon is not hydrated when it is bound to papain and that it does not form a thiohemiketal with the thiol group of Cys-25. Z-Phe-[1-(13)C]Ala-glyoxal has also been synthesized and its aldehyde carbon is fully hydrated in aqueous solution giving signals at 88.7 p.p.m. and 90.2 p.p.m. when the alpha-keto carbon and its hydrate are present respectively. When this inhibitor is bound to papain a single signal at 71.04 p.p.m. was observed due to the (13)C-enriched carbon showing that the (13)C-enriched aldehyde carbon forms a thiohemiacetal with Cys-25.
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