4-N-trimethylaminobutyraldehyde dehydrogenase: Purification and characterization of an enzyme from Pseudomonas sp. 13CM
4-N-trimethylaminobutyraldehyde dehydrogenase from Pseudomonas sp. 13CM was purified 14-fold to apparent homogeneity by hydrophobic chromatography on a Phenyl-Toyopearl, and affinity chromatography was done on a 5'-AMP Sepharose4B in the presence of dithiothreitol. The enzyme was found to be a...
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creator | Hassan, M.(Tottori Univ. (Japan)) Okada, M Ichiyanagi, T Mori, N |
description | 4-N-trimethylaminobutyraldehyde dehydrogenase from Pseudomonas sp. 13CM was purified 14-fold to apparent homogeneity by hydrophobic chromatography on a Phenyl-Toyopearl, and affinity chromatography was done on a 5'-AMP Sepharose4B in the presence of dithiothreitol. The enzyme was found to be a trimer with identical 55 kDa subunits. The isoeletric point was found to be 5.5. The optimum temperature and pH were 40 deg C and pH 10.0. The purified enzyme was further characterized with respect to substrate specificity, kinetic parameters, and analog inhibition. The Ksub(m) values for 4-N-trimethylaminobutyraldehyde, 4-dimethylaminobutyraldehyde, and NADsup(+) were 7.4, 51, and 125 micro M respectively. The enzyme was inhibited by SH reagents, and by heavy metal ions. |
doi_str_mv | 10.1271/bbb.70514 |
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(Japan)) ; Okada, M ; Ichiyanagi, T ; Mori, N</creator><creatorcontrib>Hassan, M.(Tottori Univ. (Japan)) ; Okada, M ; Ichiyanagi, T ; Mori, N</creatorcontrib><description>4-N-trimethylaminobutyraldehyde dehydrogenase from Pseudomonas sp. 13CM was purified 14-fold to apparent homogeneity by hydrophobic chromatography on a Phenyl-Toyopearl, and affinity chromatography was done on a 5'-AMP Sepharose4B in the presence of dithiothreitol. The enzyme was found to be a trimer with identical 55 kDa subunits. The isoeletric point was found to be 5.5. The optimum temperature and pH were 40 deg C and pH 10.0. The purified enzyme was further characterized with respect to substrate specificity, kinetic parameters, and analog inhibition. The Ksub(m) values for 4-N-trimethylaminobutyraldehyde, 4-dimethylaminobutyraldehyde, and NADsup(+) were 7.4, 51, and 125 micro M respectively. The enzyme was inhibited by SH reagents, and by heavy metal ions.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.70514</identifier><identifier>PMID: 18175913</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>aldehyde dehydrogenase ; Aldehyde Oxidoreductases - isolation & purification ; Aldehyde Oxidoreductases - metabolism ; analog inhibitor ; Bacterial Proteins - isolation & purification ; Bacterial Proteins - metabolism ; Biological and medical sciences ; biosynthesis ; CARNITINA ; CARNITINE ; CHEMICOPHYSICAL PROPERTIES ; Chromatography, Affinity ; Chromatography, Gel ; COMPOSE D'AMMONIUM QUATERNAIRE ; COMPUESTOS AMONICOS CUATERNARIOS ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Indicators and Reagents ; Isoelectric Focusing ; Kinetics ; METABOLITE ; METABOLITES ; METABOLITOS ; Molecular Weight ; OXIDOREDUCTASES ; OXIDORREDUCTASAS ; OXYDOREDUCTASE ; PROPIEDADES FISICOQUIMICAS ; PROPRIETE PHYSICOCHIMIQUE ; PSEUDOMONAS ; Pseudomonas - enzymology ; PURIFICACION ; PURIFICATION ; quaternary ammonium compound ; QUATERNARY AMMONIUM COMPOUNDS ; Sepharose</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2008-01, Vol.72 (1), p.155-162</ispartof><rights>2008 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 2008</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c534t-3cea618457d1b83152248e0dea3e0c353328adb4754c594db6e3ae371ab169113</citedby><cites>FETCH-LOGICAL-c534t-3cea618457d1b83152248e0dea3e0c353328adb4754c594db6e3ae371ab169113</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20157995$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18175913$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hassan, M.(Tottori Univ. (Japan))</creatorcontrib><creatorcontrib>Okada, M</creatorcontrib><creatorcontrib>Ichiyanagi, T</creatorcontrib><creatorcontrib>Mori, N</creatorcontrib><title>4-N-trimethylaminobutyraldehyde dehydrogenase: Purification and characterization of an enzyme from Pseudomonas sp. 13CM</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>4-N-trimethylaminobutyraldehyde dehydrogenase from Pseudomonas sp. 13CM was purified 14-fold to apparent homogeneity by hydrophobic chromatography on a Phenyl-Toyopearl, and affinity chromatography was done on a 5'-AMP Sepharose4B in the presence of dithiothreitol. The enzyme was found to be a trimer with identical 55 kDa subunits. The isoeletric point was found to be 5.5. The optimum temperature and pH were 40 deg C and pH 10.0. The purified enzyme was further characterized with respect to substrate specificity, kinetic parameters, and analog inhibition. The Ksub(m) values for 4-N-trimethylaminobutyraldehyde, 4-dimethylaminobutyraldehyde, and NADsup(+) were 7.4, 51, and 125 micro M respectively. The enzyme was inhibited by SH reagents, and by heavy metal ions.</description><subject>aldehyde dehydrogenase</subject><subject>Aldehyde Oxidoreductases - isolation & purification</subject><subject>Aldehyde Oxidoreductases - metabolism</subject><subject>analog inhibitor</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological and medical sciences</subject><subject>biosynthesis</subject><subject>CARNITINA</subject><subject>CARNITINE</subject><subject>CHEMICOPHYSICAL PROPERTIES</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, Gel</subject><subject>COMPOSE D'AMMONIUM QUATERNAIRE</subject><subject>COMPUESTOS AMONICOS CUATERNARIOS</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Indicators and Reagents</subject><subject>Isoelectric Focusing</subject><subject>Kinetics</subject><subject>METABOLITE</subject><subject>METABOLITES</subject><subject>METABOLITOS</subject><subject>Molecular Weight</subject><subject>OXIDOREDUCTASES</subject><subject>OXIDORREDUCTASAS</subject><subject>OXYDOREDUCTASE</subject><subject>PROPIEDADES FISICOQUIMICAS</subject><subject>PROPRIETE PHYSICOCHIMIQUE</subject><subject>PSEUDOMONAS</subject><subject>Pseudomonas - enzymology</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>quaternary ammonium compound</subject><subject>QUATERNARY AMMONIUM COMPOUNDS</subject><subject>Sepharose</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9v1DAQxS0EokvhwAcA5QIShyye2I4TbmjFXxXYA5yjiT3pGiXx1k5UpZ8et1nggsRppKffvNG8x9hT4FsoNLxu23aruQJ5j21ASJ2XtdT32YbXUOaVVHDGHsX4k_MkKHjIzqACrWoQG3Yt86_5FNxA02HpcXCjb-dpCdhbOiyWsrsR_CWNGOlNtp-D65zByfkxw9Fm5oABzUTB3ayi75Ke0XizDJR1wQ_ZPtJs_eCTQxaP2wzE7stj9qDDPtKT0zxnP96_-777mF98-_Bp9_YiN0rIKReGsIT0grbQVgJUUciKuCUUxI1QQhQV2lZqJY2qpW1LEkhCA7ZQ1gDinL1cfY_BX80Up2Zw0VDf40h-jo3mheBQ6v-CRcq31uWt46sVNMHHGKhrjik-DEsDvLmto0l1NHd1JPb5yXRuB7J_yVP-CXhxAjAa7LuAo3HxD1dwULquVeLkyrmx82HAax9620y49D78XhL_uv9sXevQN3gZEvV5X3BecS61KMQvUCqtvQ</recordid><startdate>20080101</startdate><enddate>20080101</enddate><creator>Hassan, M.(Tottori Univ. 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(Japan)) ; Okada, M ; Ichiyanagi, T ; Mori, N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c534t-3cea618457d1b83152248e0dea3e0c353328adb4754c594db6e3ae371ab169113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>aldehyde dehydrogenase</topic><topic>Aldehyde Oxidoreductases - isolation & purification</topic><topic>Aldehyde Oxidoreductases - metabolism</topic><topic>analog inhibitor</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biological and medical sciences</topic><topic>biosynthesis</topic><topic>CARNITINA</topic><topic>CARNITINE</topic><topic>CHEMICOPHYSICAL PROPERTIES</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, Gel</topic><topic>COMPOSE D'AMMONIUM QUATERNAIRE</topic><topic>COMPUESTOS AMONICOS CUATERNARIOS</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Indicators and Reagents</topic><topic>Isoelectric Focusing</topic><topic>Kinetics</topic><topic>METABOLITE</topic><topic>METABOLITES</topic><topic>METABOLITOS</topic><topic>Molecular Weight</topic><topic>OXIDOREDUCTASES</topic><topic>OXIDORREDUCTASAS</topic><topic>OXYDOREDUCTASE</topic><topic>PROPIEDADES FISICOQUIMICAS</topic><topic>PROPRIETE PHYSICOCHIMIQUE</topic><topic>PSEUDOMONAS</topic><topic>Pseudomonas - enzymology</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>quaternary ammonium compound</topic><topic>QUATERNARY AMMONIUM COMPOUNDS</topic><topic>Sepharose</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hassan, M.(Tottori Univ. (Japan))</creatorcontrib><creatorcontrib>Okada, M</creatorcontrib><creatorcontrib>Ichiyanagi, T</creatorcontrib><creatorcontrib>Mori, N</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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hassan, M.(Tottori Univ. (Japan))</au><au>Okada, M</au><au>Ichiyanagi, T</au><au>Mori, N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>4-N-trimethylaminobutyraldehyde dehydrogenase: Purification and characterization of an enzyme from Pseudomonas sp. 13CM</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2008-01-01</date><risdate>2008</risdate><volume>72</volume><issue>1</issue><spage>155</spage><epage>162</epage><pages>155-162</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>4-N-trimethylaminobutyraldehyde dehydrogenase from Pseudomonas sp. 13CM was purified 14-fold to apparent homogeneity by hydrophobic chromatography on a Phenyl-Toyopearl, and affinity chromatography was done on a 5'-AMP Sepharose4B in the presence of dithiothreitol. The enzyme was found to be a trimer with identical 55 kDa subunits. The isoeletric point was found to be 5.5. The optimum temperature and pH were 40 deg C and pH 10.0. The purified enzyme was further characterized with respect to substrate specificity, kinetic parameters, and analog inhibition. The Ksub(m) values for 4-N-trimethylaminobutyraldehyde, 4-dimethylaminobutyraldehyde, and NADsup(+) were 7.4, 51, and 125 micro M respectively. The enzyme was inhibited by SH reagents, and by heavy metal ions.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>18175913</pmid><doi>10.1271/bbb.70514</doi><tpages>8</tpages></addata></record> |
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subjects | aldehyde dehydrogenase Aldehyde Oxidoreductases - isolation & purification Aldehyde Oxidoreductases - metabolism analog inhibitor Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Biological and medical sciences biosynthesis CARNITINA CARNITINE CHEMICOPHYSICAL PROPERTIES Chromatography, Affinity Chromatography, Gel COMPOSE D'AMMONIUM QUATERNAIRE COMPUESTOS AMONICOS CUATERNARIOS Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Indicators and Reagents Isoelectric Focusing Kinetics METABOLITE METABOLITES METABOLITOS Molecular Weight OXIDOREDUCTASES OXIDORREDUCTASAS OXYDOREDUCTASE PROPIEDADES FISICOQUIMICAS PROPRIETE PHYSICOCHIMIQUE PSEUDOMONAS Pseudomonas - enzymology PURIFICACION PURIFICATION quaternary ammonium compound QUATERNARY AMMONIUM COMPOUNDS Sepharose |
title | 4-N-trimethylaminobutyraldehyde dehydrogenase: Purification and characterization of an enzyme from Pseudomonas sp. 13CM |
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