These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: eta(1)-N-succinimidato complexes of iron, molybdenum and tungsten as reversible inhibitors of papain.
    Author: Rudolf B, Salmain M, Martel A, Palusiak M, Zakrzewski J.
    Journal: J Inorg Biochem; 2009 Aug; 103(8):1162-8. PubMed ID: 19616302.
    Abstract:
    Recently we have found that the metallocarbonyl complexes (eta(5)-C(5)H(5))M(CO)(x)(eta(1)-N-maleimidato) (M=Fe, Mo, W; x=2 or 3) bearing a maleimide function were irreversible inhibitors of the enzyme papain. To get further insight into the binding mechanism of these compounds we synthesized the related complexes (eta(5)-C(5)H(5))M(CO)(x)(eta(1)-N-succinimidato) (M=Fe, Mo, W; x=2 or 3) that lacked the ethylenic bond responsible for alkylation of the cysteine 25 thiol group in the papain's catalytic pocket. We performed kinetic studies of the interaction of the synthesized complexes towards papain. We found that they act as reversible inhibitors of the enzyme with IC(50) values in the range 480-1700microM. Docking experiments confirmed binding of these complexes to the enzyme's catalytic pocket.
    [Abstract] [Full Text] [Related] [New Search]