Purification and characterization of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes
Oxalyl-coenzyme A (oxalyl-CoA) decarboxylase was purified from Oxalobacter formigenes by high-pressure liquid chromatography with hydrophobic interaction chromatography, DEAE anion-exchange chromatography, and gel permeation chromatography. The enzyme is made up of four identical subunits (M(r), 65,...
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| Veröffentlicht in: | Journal of Bacteriology 1989-05, Vol.171 (5), p.2605-2608 |
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| container_title | Journal of Bacteriology |
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| creator | Baetz, A.L. (National Animal Disease Center, ARS, USDA, Ames, IA) Allison, M.J |
| description | Oxalyl-coenzyme A (oxalyl-CoA) decarboxylase was purified from Oxalobacter formigenes by high-pressure liquid chromatography with hydrophobic interaction chromatography, DEAE anion-exchange chromatography, and gel permeation chromatography. The enzyme is made up of four identical subunits (M(r), 65,000) to give the active enzyme (M(r), 260,000). The enzyme catalyzed the thiamine PP(i)-dependent decarboxylation of oxalyl-CoA to formate and carbon dioxide. Apparent K(m) and V(max) values, respectively, were 0.24 mM and 0.25 micromole/min for oxalyl-CoA and 1.1 pM and 0.14 micromole/min for thiamine pyrophosphate. The maximum specific activity was 13.5 microM oxalyl-CoA decarboxylated per min per mg of protein |
| doi_str_mv | 10.1128/jb.171.5.2605-2608.1989 |
| format | Article |
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(National Animal Disease Center, ARS, USDA, Ames, IA) ; Allison, M.J</creator><creatorcontrib>Baetz, A.L. (National Animal Disease Center, ARS, USDA, Ames, IA) ; Allison, M.J</creatorcontrib><description>Oxalyl-coenzyme A (oxalyl-CoA) decarboxylase was purified from Oxalobacter formigenes by high-pressure liquid chromatography with hydrophobic interaction chromatography, DEAE anion-exchange chromatography, and gel permeation chromatography. The enzyme is made up of four identical subunits (M(r), 65,000) to give the active enzyme (M(r), 260,000). The enzyme catalyzed the thiamine PP(i)-dependent decarboxylation of oxalyl-CoA to formate and carbon dioxide. Apparent K(m) and V(max) values, respectively, were 0.24 mM and 0.25 micromole/min for oxalyl-CoA and 1.1 pM and 0.14 micromole/min for thiamine pyrophosphate. The maximum specific activity was 13.5 microM oxalyl-CoA decarboxylated per min per mg of protein</description><identifier>ISSN: 0021-9193</identifier><identifier>EISSN: 1098-5530</identifier><identifier>EISSN: 1067-8832</identifier><identifier>DOI: 10.1128/jb.171.5.2605-2608.1989</identifier><identifier>PMID: 2708315</identifier><identifier>CODEN: JOBAAY</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Acyl Coenzyme A - metabolism ; BACTERIA ; BACTERIE ; Bacteriology ; Biological and medical sciences ; Carboxy-Lyases - isolation & purification ; Carboxy-Lyases - metabolism ; COENZIMAS ; COENZYME ; EPURATION ; Fundamental and applied biological sciences. Psychology ; Gram-Negative Anaerobic Bacteria - enzymology ; Kinetics ; LIASAS ; LYASE ; Metabolism. Enzymes ; Microbiology ; Molecular Weight ; Oxalates - metabolism ; Oxalic Acid ; Oxalobacter formigenes ; PROPIEDADES FISICO-QUIMICAS ; PROPRIETE PHYSICO-CHIMIQUE ; PURIFICACION ; RUMEN ; Spectrum Analysis ; Substrate Specificity</subject><ispartof>Journal of Bacteriology, 1989-05, Vol.171 (5), p.2605-2608</ispartof><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c516t-f29f09b30a20fcced07c44578ab3beef141ee442cc5bf1ad534b5ca81ea5c7023</citedby><cites>FETCH-LOGICAL-c516t-f29f09b30a20fcced07c44578ab3beef141ee442cc5bf1ad534b5ca81ea5c7023</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC209940/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC209940/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6926203$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2708315$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Baetz, A.L. (National Animal Disease Center, ARS, USDA, Ames, IA)</creatorcontrib><creatorcontrib>Allison, M.J</creatorcontrib><title>Purification and characterization of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes</title><title>Journal of Bacteriology</title><addtitle>J Bacteriol</addtitle><description>Oxalyl-coenzyme A (oxalyl-CoA) decarboxylase was purified from Oxalobacter formigenes by high-pressure liquid chromatography with hydrophobic interaction chromatography, DEAE anion-exchange chromatography, and gel permeation chromatography. The enzyme is made up of four identical subunits (M(r), 65,000) to give the active enzyme (M(r), 260,000). The enzyme catalyzed the thiamine PP(i)-dependent decarboxylation of oxalyl-CoA to formate and carbon dioxide. Apparent K(m) and V(max) values, respectively, were 0.24 mM and 0.25 micromole/min for oxalyl-CoA and 1.1 pM and 0.14 micromole/min for thiamine pyrophosphate. The maximum specific activity was 13.5 microM oxalyl-CoA decarboxylated per min per mg of protein</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Acyl Coenzyme A - metabolism</subject><subject>BACTERIA</subject><subject>BACTERIE</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Carboxy-Lyases - isolation & purification</subject><subject>Carboxy-Lyases - metabolism</subject><subject>COENZIMAS</subject><subject>COENZYME</subject><subject>EPURATION</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gram-Negative Anaerobic Bacteria - enzymology</subject><subject>Kinetics</subject><subject>LIASAS</subject><subject>LYASE</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>Molecular Weight</subject><subject>Oxalates - metabolism</subject><subject>Oxalic Acid</subject><subject>Oxalobacter formigenes</subject><subject>PROPIEDADES FISICO-QUIMICAS</subject><subject>PROPRIETE PHYSICO-CHIMIQUE</subject><subject>PURIFICACION</subject><subject>RUMEN</subject><subject>Spectrum Analysis</subject><subject>Substrate Specificity</subject><issn>0021-9193</issn><issn>1098-5530</issn><issn>1067-8832</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhSMEKtPCCyAhglSxS7CdOLEXXVQVf1KlIkHX5tq5nvEoiYudgU6fHoeMRnTF5lry-c71sU6WvaGkpJSJ91td0paWvGQN4UUaoqRSyCfZihIpCs4r8jRbEcJoIamsnmenMW4JoXXN2Ul2wloiKspX2Y-vu-CsMzA5P-YwdrnZQAAzYXAPy6W3ub-Hft8XxuP4sB8wv8w7NBC0v9_3EDG3wQ_5TYK8_mvNrQ-DW-OI8UX2zEIf8eXhPMtuP374fvW5uL759OXq8rownDZTYZm0ROqKACPWGOxIa1LWVoCuNKKlNUWsa2YM15ZCx6tacwOCInDTEladZRfL3rudHrAzOE4BenUX3ABhrzw49VgZ3Uat_S_FiJQ1Sf53B3_wP3cYJzW4aLDvYUS_i6oVkjEu-X9ByhlrhJjBdgFN8DEGtMcwlKi5RLXVKpWouJpLnIdQc4nJ-frfvxx9h9aSfn7QIRrobYDRuHjEGskaRqqEvV2wjVtvfruACuLw-NHEvFoYC17BOqQ1t99SBNZwVv0BdoG8ZQ</recordid><startdate>19890501</startdate><enddate>19890501</enddate><creator>Baetz, A.L. (National Animal Disease Center, ARS, USDA, Ames, IA)</creator><creator>Allison, M.J</creator><general>American Society for Microbiology</general><scope>FBQ</scope><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19890501</creationdate><title>Purification and characterization of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes</title><author>Baetz, A.L. (National Animal Disease Center, ARS, USDA, Ames, IA) ; Allison, M.J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c516t-f29f09b30a20fcced07c44578ab3beef141ee442cc5bf1ad534b5ca81ea5c7023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Acyl Coenzyme A - metabolism</topic><topic>BACTERIA</topic><topic>BACTERIE</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Carboxy-Lyases - isolation & purification</topic><topic>Carboxy-Lyases - metabolism</topic><topic>COENZIMAS</topic><topic>COENZYME</topic><topic>EPURATION</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gram-Negative Anaerobic Bacteria - enzymology</topic><topic>Kinetics</topic><topic>LIASAS</topic><topic>LYASE</topic><topic>Metabolism. Enzymes</topic><topic>Microbiology</topic><topic>Molecular Weight</topic><topic>Oxalates - metabolism</topic><topic>Oxalic Acid</topic><topic>Oxalobacter formigenes</topic><topic>PROPIEDADES FISICO-QUIMICAS</topic><topic>PROPRIETE PHYSICO-CHIMIQUE</topic><topic>PURIFICACION</topic><topic>RUMEN</topic><topic>Spectrum Analysis</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Baetz, A.L. (National Animal Disease Center, ARS, USDA, Ames, IA)</creatorcontrib><creatorcontrib>Allison, M.J</creatorcontrib><collection>AGRIS</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of Bacteriology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Baetz, A.L. (National Animal Disease Center, ARS, USDA, Ames, IA)</au><au>Allison, M.J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes</atitle><jtitle>Journal of Bacteriology</jtitle><addtitle>J Bacteriol</addtitle><date>1989-05-01</date><risdate>1989</risdate><volume>171</volume><issue>5</issue><spage>2605</spage><epage>2608</epage><pages>2605-2608</pages><issn>0021-9193</issn><eissn>1098-5530</eissn><eissn>1067-8832</eissn><coden>JOBAAY</coden><abstract>Oxalyl-coenzyme A (oxalyl-CoA) decarboxylase was purified from Oxalobacter formigenes by high-pressure liquid chromatography with hydrophobic interaction chromatography, DEAE anion-exchange chromatography, and gel permeation chromatography. The enzyme is made up of four identical subunits (M(r), 65,000) to give the active enzyme (M(r), 260,000). The enzyme catalyzed the thiamine PP(i)-dependent decarboxylation of oxalyl-CoA to formate and carbon dioxide. Apparent K(m) and V(max) values, respectively, were 0.24 mM and 0.25 micromole/min for oxalyl-CoA and 1.1 pM and 0.14 micromole/min for thiamine pyrophosphate. The maximum specific activity was 13.5 microM oxalyl-CoA decarboxylated per min per mg of protein</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>2708315</pmid><doi>10.1128/jb.171.5.2605-2608.1989</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of Bacteriology, 1989-05, Vol.171 (5), p.2605-2608 |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Acyl Coenzyme A - metabolism BACTERIA BACTERIE Bacteriology Biological and medical sciences Carboxy-Lyases - isolation & purification Carboxy-Lyases - metabolism COENZIMAS COENZYME EPURATION Fundamental and applied biological sciences. Psychology Gram-Negative Anaerobic Bacteria - enzymology Kinetics LIASAS LYASE Metabolism. Enzymes Microbiology Molecular Weight Oxalates - metabolism Oxalic Acid Oxalobacter formigenes PROPIEDADES FISICO-QUIMICAS PROPRIETE PHYSICO-CHIMIQUE PURIFICACION RUMEN Spectrum Analysis Substrate Specificity |
| title | Purification and characterization of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes |
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