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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Veröffentlicht in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2008-01, Vol.72 (1), p.155-162
Hauptverfasser: Hassan, M.(Tottori Univ. (Japan)), Okada, M, Ichiyanagi, T, Mori, N
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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.
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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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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. 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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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source J-STAGE Free; Oxford University Press Journals All Titles (1996-Current); MEDLINE; Freely Accessible Japanese Titles; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry
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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