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pubmed:abstractText |
New data on proteolytic enzyme inhibitors and mechanisms of their interaction with the enzymes are reviewed. In recent years, a number of new inhibitors comprising families earlier unknown have been described such as proteins from the parasitic nematode Ascaris lumbricoides, ecotin from the periplasm of Escherichia coli, proteins PMP-C and PMP-D from locust Locusta migratoria, and hirustasin from the medicinal leech Hirudo medicinalis. At the same time, some proteins that may be assigned to inhibitors on the basis of their structures were found to perform other (not inhibitory) functions. Thus, the family of the Kunitz soybean trypsin inhibitor includes plant storage proteins and proteins whose synthesis is induced by stress factors. Numerous inhibitors interacting with the enzymes by mechanisms other than the substrate-like ones were identified, such as ornithodorin and anticoagulant peptide from tick Ornithodoros moubata (inhibitors of the blood clotting system proteases), an inhibitor from snake (Bothrops jararaca) venom, and ecotin, an inhibitor of serine proteases with an unusually broad specificity range. Special emphasis is placed on enzyme inhibition with propeptides and the mechanism of this process.
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