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J Enzyme Inhib Med Chem. 2011 Apr;26(2):155-61. doi: 10.3109/14756366.2010.482047. Epub 2010 Jun 28.

Unusual activity pattern of leucine aminopeptidase inhibitors based on phosphorus containing derivatives of methionine and norleucine.

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Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, V.V.I., Flemingovo Nám., Praha, Czech Republic.


Ligands containing bulky aliphatic P1 residues exhibit a high affinity towards cytosolic leucine aminopeptidase, a bizinc protease of biomedical significance. According to this specificity, a series of phosphonic and phosphinic compounds have been put forward as novel putative inhibitors of the enzyme. These phosphonic and phosphinic compounds were derivatives of methionine and norleucine as both single amino acids and dipeptides. The designed inhibitors were synthesised and tested towards the peptidase isolated from porcine kidneys using an improved separation procedure affording superior homogeneity. Unexpectedly, organophosphorus derivatives of methionine and norleucine exhibited moderate activity with K(i) values in the micromolar range.

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