Sensitivity to pH, product inhibition, and inhibition by NAD+ of 1,3-propanediol dehydrogenase purified from Enterobacter agglomerans CNCM 1210
Because of its key role in the metabolism of glycerol during fermentation, 1,3-propanediol dehydrogenase (EC 1.1.1.202) of Enterobacter agglomerans CNCM 1210 was purified to homogeneity and studied with respect to its sensitivity to pH and to nucleotide and 1,3-propanediol concentrations. Enzyme act...
Gespeichert in:
| Veröffentlicht in: | Archives of microbiology 1997-08, Vol.168 (2), p.160-163 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 163 |
|---|---|
| container_issue | 2 |
| container_start_page | 160 |
| container_title | Archives of microbiology |
| container_volume | 168 |
| creator | BARBIRATO, F LARGUIER, A CONTE, T ASTRUC, S BORIES, A |
| description | Because of its key role in the metabolism of glycerol during fermentation, 1,3-propanediol dehydrogenase (EC 1.1.1.202) of Enterobacter agglomerans CNCM 1210 was purified to homogeneity and studied with respect to its sensitivity to pH and to nucleotide and 1,3-propanediol concentrations. Enzyme activity was optimal at pH 7.8. The enzyme was competitively inhibited by NAD+ (Ki of 0.29 mM), and 1,3-propanediol exerted a strong inhibitory effect according to a mixed-type inhibition with a Ki of 13.7 mM and an a-factor of 9.0. It is proposed that these dehydrogenase properties be extended to the dehydrogenases of Citrobacter freundii and Klebsiella pneumoniae, which exhibited numerous similar physical properties. |
| doi_str_mv | 10.1007/s002030050482 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_hal_p</sourceid><recordid>TN_cdi_hal_primary_oai_HAL_hal_02695588v1</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>79164124</sourcerecordid><originalsourceid>FETCH-LOGICAL-c351t-921ab6c768cd20a588d416244438ec9c5aeb2f98c9d7bcc92e277f0bf3b445cd3</originalsourceid><addsrcrecordid>eNpVkUuP0zAUhS0EGsrAkiWSFwgJ0cD1I4m9rMpARyoziwGJXeRXWqMkztjJSP0V_GU8alUxqyvf8_lI5x6E3hL4TADqLwmAAgMogQv6DC0IZ7SAmv5-jhZ5TwshGXuJXqX0B4BQIcQFupCUCQJigf7euSH5yT_46YCngMfNEo8x2NlM2A97r7MWhiVWg_3vjfUB36y-fsKhxWTJivxjVIOzPnTYuv3BxrBzg0oOj3P0rXcWtzH0-GqYXAxamTyw2u260LuohoTXN-sfmFACr9GLVnXJvTnNS_Tr29XP9abY3n6_Xq-2hWElmQpJidKVqSthLAVVCmE5qSjnnAlnpCmV07SVwkhba2MkdbSuW9At05yXxrJL9PHou1ddM0bfq3hogvLNZrVtHndAK1lm3weS2Q9HNse8n12amt4n47ouRw5zampJKk4oz2BxBE0MKUXXnp0JNI9lNU_Kyvy7k_Gse2fP9KmdrL8_6SoZ1bX5VManM5YjSQ41-wc6lptC</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>79164124</pqid></control><display><type>article</type><title>Sensitivity to pH, product inhibition, and inhibition by NAD+ of 1,3-propanediol dehydrogenase purified from Enterobacter agglomerans CNCM 1210</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><creator>BARBIRATO, F ; LARGUIER, A ; CONTE, T ; ASTRUC, S ; BORIES, A</creator><creatorcontrib>BARBIRATO, F ; LARGUIER, A ; CONTE, T ; ASTRUC, S ; BORIES, A</creatorcontrib><description>Because of its key role in the metabolism of glycerol during fermentation, 1,3-propanediol dehydrogenase (EC 1.1.1.202) of Enterobacter agglomerans CNCM 1210 was purified to homogeneity and studied with respect to its sensitivity to pH and to nucleotide and 1,3-propanediol concentrations. Enzyme activity was optimal at pH 7.8. The enzyme was competitively inhibited by NAD+ (Ki of 0.29 mM), and 1,3-propanediol exerted a strong inhibitory effect according to a mixed-type inhibition with a Ki of 13.7 mM and an a-factor of 9.0. It is proposed that these dehydrogenase properties be extended to the dehydrogenases of Citrobacter freundii and Klebsiella pneumoniae, which exhibited numerous similar physical properties.</description><identifier>ISSN: 0302-8933</identifier><identifier>EISSN: 1432-072X</identifier><identifier>DOI: 10.1007/s002030050482</identifier><identifier>PMID: 9238108</identifier><identifier>CODEN: AMICCW</identifier><language>eng</language><publisher>Heidelberg: Springer</publisher><subject>Alcohol Dehydrogenase ; Alcohol Oxidoreductases - drug effects ; Alcohol Oxidoreductases - isolation & purification ; Alcohol Oxidoreductases - metabolism ; Aldehydes ; Amino Acid Sequence ; Bacteriology ; Biological and medical sciences ; Enterobacter - enzymology ; Environmental Sciences ; Enzyme Inhibitors ; Fundamental and applied biological sciences. Psychology ; Glyceraldehyde - analogs & derivatives ; Glyceraldehyde - metabolism ; Glycerol - metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Life Sciences ; Metabolism. Enzymes ; Microbiology ; Molecular Sequence Data ; NAD - pharmacology ; Propane ; Propylene Glycols - pharmacology ; Sequence Analysis ; Sequence Homology, Amino Acid</subject><ispartof>Archives of microbiology, 1997-08, Vol.168 (2), p.160-163</ispartof><rights>1997 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c351t-921ab6c768cd20a588d416244438ec9c5aeb2f98c9d7bcc92e277f0bf3b445cd3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2779407$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9238108$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02695588$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>BARBIRATO, F</creatorcontrib><creatorcontrib>LARGUIER, A</creatorcontrib><creatorcontrib>CONTE, T</creatorcontrib><creatorcontrib>ASTRUC, S</creatorcontrib><creatorcontrib>BORIES, A</creatorcontrib><title>Sensitivity to pH, product inhibition, and inhibition by NAD+ of 1,3-propanediol dehydrogenase purified from Enterobacter agglomerans CNCM 1210</title><title>Archives of microbiology</title><addtitle>Arch Microbiol</addtitle><description>Because of its key role in the metabolism of glycerol during fermentation, 1,3-propanediol dehydrogenase (EC 1.1.1.202) of Enterobacter agglomerans CNCM 1210 was purified to homogeneity and studied with respect to its sensitivity to pH and to nucleotide and 1,3-propanediol concentrations. Enzyme activity was optimal at pH 7.8. The enzyme was competitively inhibited by NAD+ (Ki of 0.29 mM), and 1,3-propanediol exerted a strong inhibitory effect according to a mixed-type inhibition with a Ki of 13.7 mM and an a-factor of 9.0. It is proposed that these dehydrogenase properties be extended to the dehydrogenases of Citrobacter freundii and Klebsiella pneumoniae, which exhibited numerous similar physical properties.</description><subject>Alcohol Dehydrogenase</subject><subject>Alcohol Oxidoreductases - drug effects</subject><subject>Alcohol Oxidoreductases - isolation & purification</subject><subject>Alcohol Oxidoreductases - metabolism</subject><subject>Aldehydes</subject><subject>Amino Acid Sequence</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Enterobacter - enzymology</subject><subject>Environmental Sciences</subject><subject>Enzyme Inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glyceraldehyde - analogs & derivatives</subject><subject>Glyceraldehyde - metabolism</subject><subject>Glycerol - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>NAD - pharmacology</subject><subject>Propane</subject><subject>Propylene Glycols - pharmacology</subject><subject>Sequence Analysis</subject><subject>Sequence Homology, Amino Acid</subject><issn>0302-8933</issn><issn>1432-072X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkUuP0zAUhS0EGsrAkiWSFwgJ0cD1I4m9rMpARyoziwGJXeRXWqMkztjJSP0V_GU8alUxqyvf8_lI5x6E3hL4TADqLwmAAgMogQv6DC0IZ7SAmv5-jhZ5TwshGXuJXqX0B4BQIcQFupCUCQJigf7euSH5yT_46YCngMfNEo8x2NlM2A97r7MWhiVWg_3vjfUB36y-fsKhxWTJivxjVIOzPnTYuv3BxrBzg0oOj3P0rXcWtzH0-GqYXAxamTyw2u260LuohoTXN-sfmFACr9GLVnXJvTnNS_Tr29XP9abY3n6_Xq-2hWElmQpJidKVqSthLAVVCmE5qSjnnAlnpCmV07SVwkhba2MkdbSuW9At05yXxrJL9PHou1ddM0bfq3hogvLNZrVtHndAK1lm3weS2Q9HNse8n12amt4n47ouRw5zampJKk4oz2BxBE0MKUXXnp0JNI9lNU_Kyvy7k_Gse2fP9KmdrL8_6SoZ1bX5VManM5YjSQ41-wc6lptC</recordid><startdate>19970801</startdate><enddate>19970801</enddate><creator>BARBIRATO, F</creator><creator>LARGUIER, A</creator><creator>CONTE, T</creator><creator>ASTRUC, S</creator><creator>BORIES, A</creator><general>Springer</general><general>Springer Verlag</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><scope>1XC</scope></search><sort><creationdate>19970801</creationdate><title>Sensitivity to pH, product inhibition, and inhibition by NAD+ of 1,3-propanediol dehydrogenase purified from Enterobacter agglomerans CNCM 1210</title><author>BARBIRATO, F ; LARGUIER, A ; CONTE, T ; ASTRUC, S ; BORIES, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c351t-921ab6c768cd20a588d416244438ec9c5aeb2f98c9d7bcc92e277f0bf3b445cd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Alcohol Dehydrogenase</topic><topic>Alcohol Oxidoreductases - drug effects</topic><topic>Alcohol Oxidoreductases - isolation & purification</topic><topic>Alcohol Oxidoreductases - metabolism</topic><topic>Aldehydes</topic><topic>Amino Acid Sequence</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Enterobacter - enzymology</topic><topic>Environmental Sciences</topic><topic>Enzyme Inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glyceraldehyde - analogs & derivatives</topic><topic>Glyceraldehyde - metabolism</topic><topic>Glycerol - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Metabolism. Enzymes</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>NAD - pharmacology</topic><topic>Propane</topic><topic>Propylene Glycols - pharmacology</topic><topic>Sequence Analysis</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BARBIRATO, F</creatorcontrib><creatorcontrib>LARGUIER, A</creatorcontrib><creatorcontrib>CONTE, T</creatorcontrib><creatorcontrib>ASTRUC, S</creatorcontrib><creatorcontrib>BORIES, A</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><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Archives of microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>BARBIRATO, F</au><au>LARGUIER, A</au><au>CONTE, T</au><au>ASTRUC, S</au><au>BORIES, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sensitivity to pH, product inhibition, and inhibition by NAD+ of 1,3-propanediol dehydrogenase purified from Enterobacter agglomerans CNCM 1210</atitle><jtitle>Archives of microbiology</jtitle><addtitle>Arch Microbiol</addtitle><date>1997-08-01</date><risdate>1997</risdate><volume>168</volume><issue>2</issue><spage>160</spage><epage>163</epage><pages>160-163</pages><issn>0302-8933</issn><eissn>1432-072X</eissn><coden>AMICCW</coden><abstract>Because of its key role in the metabolism of glycerol during fermentation, 1,3-propanediol dehydrogenase (EC 1.1.1.202) of Enterobacter agglomerans CNCM 1210 was purified to homogeneity and studied with respect to its sensitivity to pH and to nucleotide and 1,3-propanediol concentrations. Enzyme activity was optimal at pH 7.8. The enzyme was competitively inhibited by NAD+ (Ki of 0.29 mM), and 1,3-propanediol exerted a strong inhibitory effect according to a mixed-type inhibition with a Ki of 13.7 mM and an a-factor of 9.0. It is proposed that these dehydrogenase properties be extended to the dehydrogenases of Citrobacter freundii and Klebsiella pneumoniae, which exhibited numerous similar physical properties.</abstract><cop>Heidelberg</cop><cop>Berlin</cop><pub>Springer</pub><pmid>9238108</pmid><doi>10.1007/s002030050482</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0302-8933 |
| ispartof | Archives of microbiology, 1997-08, Vol.168 (2), p.160-163 |
| issn | 0302-8933 1432-072X |
| language | eng |
| recordid | cdi_hal_primary_oai_HAL_hal_02695588v1 |
| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Alcohol Dehydrogenase Alcohol Oxidoreductases - drug effects Alcohol Oxidoreductases - isolation & purification Alcohol Oxidoreductases - metabolism Aldehydes Amino Acid Sequence Bacteriology Biological and medical sciences Enterobacter - enzymology Environmental Sciences Enzyme Inhibitors Fundamental and applied biological sciences. Psychology Glyceraldehyde - analogs & derivatives Glyceraldehyde - metabolism Glycerol - metabolism Hydrogen-Ion Concentration Kinetics Life Sciences Metabolism. Enzymes Microbiology Molecular Sequence Data NAD - pharmacology Propane Propylene Glycols - pharmacology Sequence Analysis Sequence Homology, Amino Acid |
| title | Sensitivity to pH, product inhibition, and inhibition by NAD+ of 1,3-propanediol dehydrogenase purified from Enterobacter agglomerans CNCM 1210 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-22T10%3A49%3A26IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_hal_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Sensitivity%20to%20pH,%20product%20inhibition,%20and%20inhibition%20by%20NAD+%20of%201,3-propanediol%20dehydrogenase%20purified%20from%20Enterobacter%20agglomerans%20CNCM%201210&rft.jtitle=Archives%20of%20microbiology&rft.au=BARBIRATO,%20F&rft.date=1997-08-01&rft.volume=168&rft.issue=2&rft.spage=160&rft.epage=163&rft.pages=160-163&rft.issn=0302-8933&rft.eissn=1432-072X&rft.coden=AMICCW&rft_id=info:doi/10.1007/s002030050482&rft_dat=%3Cproquest_hal_p%3E79164124%3C/proquest_hal_p%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=79164124&rft_id=info:pmid/9238108&rfr_iscdi=true |