Oligopeptidase B from Serratia proteamaculans. III. Inhibition Analysis. Specific Interactions with Metalloproteinase Inhibitors

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A. G. Mikhailova^1*, R. F. Khairullin¹, G. Ya. Kolomijtseva², and L. D. Rumsh¹

¹Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia; fax: (495) 335-7103; E-mail: anna.mikhailova@ibch.ru

²Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia; fax: (495) 939-3181; E-mail: kolom@genebee.msu.ru

^* To whom correspondence should be addressed.

Received October 18, 2011; Revision received November 25, 2011

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Inhibition of the novel oligopeptidase B from Serratia proteamaculans (PSP) by basic pancreatic trypsin inhibitor, Zn²⁺ ions, and o- and m-phenanthroline was investigated. A pronounced effect of calcium ions on the interaction of PSP with inhibitors was demonstrated. Inversion voltamperometry and atomic absorption spectrometry revealed no zinc ions in the PSP molecule. Hydrophobic nature of the enzyme inhibition by o- and m-phenanthroline was established.

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KEY WORDS: oligopeptidase B, Serratia proteamaculans, inhibition analysis, zinc-dependent enzymes, atomic absorption spectrometry, inversion voltamperometry

DOI: 10.1134/S0006297912030091

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