Oligopeptidase B from Serratia proteamaculans. III. Inhibition analysis. Specific interactions with metalloproteinase inhibitors

Oligopeptidase B from Serratia proteamaculans. III. Inhibition analysis. Specific interactions with metalloproteinase inhibitors

Inhibition of the novel oligopeptidase B from Serratia proteamaculans (PSP) by basic pancreatic trypsin inhibitor, Zn 2+ 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...

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Veröffentlicht in:Biochemistry (Moscow) 2012-03, Vol.77 (3), p.300-306
Hauptverfasser: Mikhailova, A. G., Khairullin, R. F., Kolomijtseva, G. Ya, Rumsh, L. D.
Format: Artikel
Sprache:eng
Schlagworte:
Analysis
Atomic absorption spectroscopy
Bacteria
Bacterial Proteins - antagonists & inhibitors
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Binding Sites
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - metabolism
Enzymes
Hydrolysis
Ions
Kinetics
Life Sciences
Microbiology
Pancreas
Phenanthrolines - chemistry
Phenanthrolines - metabolism
Serine Endopeptidases - chemistry
Serine Endopeptidases - genetics
Serine Endopeptidases - metabolism
Serratia - chemistry
Serratia - enzymology
Serratia - genetics
Spectral analysis
Spectrometry
Zinc - chemistry
Zinc - metabolism
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Zusammenfassung:Inhibition of the novel oligopeptidase B from Serratia proteamaculans (PSP) by basic pancreatic trypsin inhibitor, Zn 2+ 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.
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297912030091