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 |
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| container_title | Biochemistry (Moscow) |
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| creator | Mikhailova, A. G. Khairullin, R. F. Kolomijtseva, G. Ya Rumsh, L. D. |
| description | 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. |
| doi_str_mv | 10.1134/S0006297912030091 |
| format | Article |
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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.</description><identifier>ISSN: 0006-2979</identifier><identifier>EISSN: 1608-3040</identifier><identifier>DOI: 10.1134/S0006297912030091</identifier><identifier>PMID: 22803948</identifier><language>eng</language><publisher>Dordrecht: SP MAIK Nauka/Interperiodica</publisher><subject>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</subject><ispartof>Biochemistry (Moscow), 2012-03, Vol.77 (3), p.300-306</ispartof><rights>Pleiades Publishing, Ltd. 2012</rights><rights>COPYRIGHT 2012 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-875aefb114fabb3cc9e4292fb82d7d2027804e017f0088ddda5338624b972d4a3</citedby><cites>FETCH-LOGICAL-c438t-875aefb114fabb3cc9e4292fb82d7d2027804e017f0088ddda5338624b972d4a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S0006297912030091$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S0006297912030091$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22803948$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mikhailova, A. G.</creatorcontrib><creatorcontrib>Khairullin, R. F.</creatorcontrib><creatorcontrib>Kolomijtseva, G. Ya</creatorcontrib><creatorcontrib>Rumsh, L. D.</creatorcontrib><title>Oligopeptidase B from Serratia proteamaculans. III. Inhibition analysis. Specific interactions with metalloproteinase inhibitors</title><title>Biochemistry (Moscow)</title><addtitle>Biochemistry Moscow</addtitle><addtitle>Biochemistry (Mosc)</addtitle><description>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.</description><subject>Analysis</subject><subject>Atomic absorption spectroscopy</subject><subject>Bacteria</subject><subject>Bacterial Proteins - antagonists & inhibitors</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bioorganic Chemistry</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Enzyme Inhibitors - metabolism</subject><subject>Enzymes</subject><subject>Hydrolysis</subject><subject>Ions</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Pancreas</subject><subject>Phenanthrolines - chemistry</subject><subject>Phenanthrolines - metabolism</subject><subject>Serine Endopeptidases - chemistry</subject><subject>Serine Endopeptidases - genetics</subject><subject>Serine Endopeptidases - metabolism</subject><subject>Serratia - chemistry</subject><subject>Serratia - enzymology</subject><subject>Serratia - genetics</subject><subject>Spectral analysis</subject><subject>Spectrometry</subject><subject>Zinc - chemistry</subject><subject>Zinc - metabolism</subject><issn>0006-2979</issn><issn>1608-3040</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1UUtv1DAQthCILoUfwAVFcOGSZfzIxjmWqoWVKvWwcI4cZ7x1ldjBdlT1xk_HIQXES5Zs2d_D880Q8pLCllIu3h0AYMeauqEMOEBDH5EN3YEsOQh4TDYLXC74CXkW422-Mmj4U3LCmATeCLkhX68He_QTTsn2KmLxvjDBj8UBQ1DJqmIKPqEalZ4H5eK22O_3eXM3trPJelcop4b7aDNymFBbY3VhXcKg9ALH4s6mm2LEpIbBf_eybvnGrg4-xOfkiVFDxBcP5yn5fHnx6fxjeXX9YX9-dlVqwWUqZV0pNB2lwqiu41o3KFjDTCdZX_cMWC1BINDaAEjZ972qOJc7JrqmZr1Q_JS8XX1zFV9mjKkdbdQ45Fjo59jSbJG7VnHI1Nd_UG_9HHLQ2Da5cbAT1UJ6s5KOasDWOuNTDr14tmdcVFLSSiys7T9YefU4Wu0dGpvffxPQVaCDjzGgaadgRxXuc4HtMvT2r6FnzauHeuduxP6n4seUM4GthJghd8TwK9D_Xb8Ba521wA</recordid><startdate>20120301</startdate><enddate>20120301</enddate><creator>Mikhailova, A. 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G.</au><au>Khairullin, R. F.</au><au>Kolomijtseva, G. Ya</au><au>Rumsh, L. D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Oligopeptidase B from Serratia proteamaculans. III. Inhibition analysis. Specific interactions with metalloproteinase inhibitors</atitle><jtitle>Biochemistry (Moscow)</jtitle><stitle>Biochemistry Moscow</stitle><addtitle>Biochemistry (Mosc)</addtitle><date>2012-03-01</date><risdate>2012</risdate><volume>77</volume><issue>3</issue><spage>300</spage><epage>306</epage><pages>300-306</pages><issn>0006-2979</issn><eissn>1608-3040</eissn><abstract>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.</abstract><cop>Dordrecht</cop><pub>SP MAIK Nauka/Interperiodica</pub><pmid>22803948</pmid><doi>10.1134/S0006297912030091</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-2979 |
| ispartof | Biochemistry (Moscow), 2012-03, Vol.77 (3), p.300-306 |
| issn | 0006-2979 1608-3040 |
| language | eng |
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| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | 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 |
| title | Oligopeptidase B from Serratia proteamaculans. III. Inhibition analysis. Specific interactions with metalloproteinase inhibitors |
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