Vitamin K-dependent oxygenase/carboxylase; Differential inactivation by sulfhydryl reagents
Inhibition of vitamin K-dependent carboxylase and oxygenase by sulfhydryl reagents was compared. Formation of vitamin K epoxide and vitamin K-dependent carboxylation are both strongly (>90%) inhibited by I mM p-hydroxymercuribenzoate, and this inhibition is reversed by dithiothrietol. Both activi...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1987-10, Vol.148 (1), p.184-191 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Canfield, Louise M. |
| description | Inhibition of vitamin K-dependent carboxylase and oxygenase by sulfhydryl reagents was compared. Formation of vitamin K epoxide and vitamin K-dependent carboxylation are both strongly (>90%) inhibited by I mM p-hydroxymercuribenzoate, and this inhibition is reversed by dithiothrietol. Both activities are also effectively inhibited by N-ethylmaleimide (NEM). Preincubation with vitamin K hydroquinone prevents NEM inhibition of epoxide formation but not of carboxylation. These data argue that separate active sites are required to support vitamin K-dependent epoxide formation and carboxylation and that the binding site for vitamin K oxygenase contains an active thiol group. |
| doi_str_mv | 10.1016/0006-291X(87)91093-X |
| format | Article |
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Formation of vitamin K epoxide and vitamin K-dependent carboxylation are both strongly (>90%) inhibited by I mM p-hydroxymercuribenzoate, and this inhibition is reversed by dithiothrietol. Both activities are also effectively inhibited by N-ethylmaleimide (NEM). Preincubation with vitamin K hydroquinone prevents NEM inhibition of epoxide formation but not of carboxylation. These data argue that separate active sites are required to support vitamin K-dependent epoxide formation and carboxylation and that the binding site for vitamin K oxygenase contains an active thiol group.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(87)91093-X</identifier><identifier>PMID: 3675572</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Applied sciences ; Carbon-Carbon Ligases ; Dithiothreitol - pharmacology ; Epoxy Compounds - analysis ; Ethylmaleimide - pharmacology ; Exact sciences and technology ; Intracellular Membranes - enzymology ; Iodoacetates - pharmacology ; Iodoacetic Acid ; Kinetics ; Ligases - antagonists & inhibitors ; Microsomes, Liver - enzymology ; Other techniques and industries ; Phenylmercury Compounds - pharmacology ; Sulfhydryl Reagents - pharmacology</subject><ispartof>Biochemical and biophysical research communications, 1987-10, Vol.148 (1), p.184-191</ispartof><rights>1987</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-8e2815882e997ae445fbe3ce3cea25cee550d190635a44adaa0f62e85fede58a3</citedby><cites>FETCH-LOGICAL-c386t-8e2815882e997ae445fbe3ce3cea25cee550d190635a44adaa0f62e85fede58a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006291X8791093X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7847385$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3675572$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Canfield, Louise M.</creatorcontrib><title>Vitamin K-dependent oxygenase/carboxylase; Differential inactivation by sulfhydryl reagents</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Inhibition of vitamin K-dependent carboxylase and oxygenase by sulfhydryl reagents was compared. Formation of vitamin K epoxide and vitamin K-dependent carboxylation are both strongly (>90%) inhibited by I mM p-hydroxymercuribenzoate, and this inhibition is reversed by dithiothrietol. Both activities are also effectively inhibited by N-ethylmaleimide (NEM). Preincubation with vitamin K hydroquinone prevents NEM inhibition of epoxide formation but not of carboxylation. These data argue that separate active sites are required to support vitamin K-dependent epoxide formation and carboxylation and that the binding site for vitamin K oxygenase contains an active thiol group.</description><subject>Applied sciences</subject><subject>Carbon-Carbon Ligases</subject><subject>Dithiothreitol - pharmacology</subject><subject>Epoxy Compounds - analysis</subject><subject>Ethylmaleimide - pharmacology</subject><subject>Exact sciences and technology</subject><subject>Intracellular Membranes - enzymology</subject><subject>Iodoacetates - pharmacology</subject><subject>Iodoacetic Acid</subject><subject>Kinetics</subject><subject>Ligases - antagonists & inhibitors</subject><subject>Microsomes, Liver - enzymology</subject><subject>Other techniques and industries</subject><subject>Phenylmercury Compounds - pharmacology</subject><subject>Sulfhydryl Reagents - pharmacology</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1rGzEQhkVpcJ20_6CFPZSQHDaWdldaLYFAyDcx9NIEQw9iLI0SlbXWkdYm--8rx8bHwsCMmOcdxEPId0bPGGViQikVedGw2YmsTxtGmzKffSLjNNC8YLT6TMZ75As5jPEvpYxVohmRUSlqzutiTP48ux4WzmePucEleoO-z7r34QU9RJxoCPP0atN8nl07azEkwEGbOQ-6d2voXeez-ZDFVWtfBxOGNgsIKd7Hr-TAQhvx264fkafbm99X9_n0193D1eU016UUfS6xkIxLWWDT1IBVxe0cS70pKLhG5Jwa1lBRcqgqMADUigIlt2iQSyiPyPH27jJ0byuMvVq4qLFtwWO3ikoyRoWgRQKrLahDF2NAq5bBLSAMilG1cao2wtRGmJK1-nCqZin2Y3d_NV-g2Yd2EtP-524PUUNrA3jt4h6rZVWXkifsYothcrF2GFTUDr1G4wLqXpnO_f8f_wCWhpWA</recordid><startdate>19871014</startdate><enddate>19871014</enddate><creator>Canfield, Louise M.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19871014</creationdate><title>Vitamin K-dependent oxygenase/carboxylase; Differential inactivation by sulfhydryl reagents</title><author>Canfield, Louise M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-8e2815882e997ae445fbe3ce3cea25cee550d190635a44adaa0f62e85fede58a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Applied sciences</topic><topic>Carbon-Carbon Ligases</topic><topic>Dithiothreitol - pharmacology</topic><topic>Epoxy Compounds - analysis</topic><topic>Ethylmaleimide - pharmacology</topic><topic>Exact sciences and technology</topic><topic>Intracellular Membranes - enzymology</topic><topic>Iodoacetates - pharmacology</topic><topic>Iodoacetic Acid</topic><topic>Kinetics</topic><topic>Ligases - antagonists & inhibitors</topic><topic>Microsomes, Liver - enzymology</topic><topic>Other techniques and industries</topic><topic>Phenylmercury Compounds - pharmacology</topic><topic>Sulfhydryl Reagents - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Canfield, Louise M.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Canfield, Louise M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Vitamin K-dependent oxygenase/carboxylase; Differential inactivation by sulfhydryl reagents</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1987-10-14</date><risdate>1987</risdate><volume>148</volume><issue>1</issue><spage>184</spage><epage>191</epage><pages>184-191</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>Inhibition of vitamin K-dependent carboxylase and oxygenase by sulfhydryl reagents was compared. Formation of vitamin K epoxide and vitamin K-dependent carboxylation are both strongly (>90%) inhibited by I mM p-hydroxymercuribenzoate, and this inhibition is reversed by dithiothrietol. Both activities are also effectively inhibited by N-ethylmaleimide (NEM). Preincubation with vitamin K hydroquinone prevents NEM inhibition of epoxide formation but not of carboxylation. These data argue that separate active sites are required to support vitamin K-dependent epoxide formation and carboxylation and that the binding site for vitamin K oxygenase contains an active thiol group.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3675572</pmid><doi>10.1016/0006-291X(87)91093-X</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biochemical and biophysical research communications, 1987-10, Vol.148 (1), p.184-191 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Applied sciences Carbon-Carbon Ligases Dithiothreitol - pharmacology Epoxy Compounds - analysis Ethylmaleimide - pharmacology Exact sciences and technology Intracellular Membranes - enzymology Iodoacetates - pharmacology Iodoacetic Acid Kinetics Ligases - antagonists & inhibitors Microsomes, Liver - enzymology Other techniques and industries Phenylmercury Compounds - pharmacology Sulfhydryl Reagents - pharmacology |
| title | Vitamin K-dependent oxygenase/carboxylase; Differential inactivation by sulfhydryl reagents |
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