Characterization of glycerol kinase and NAD-independent glycerol-3-phosphate dehydrogenase from Pediococcus pentosaceus N5p
The pathway involved in glycerol dissimilation in Pediococcus pentosaceus N5p, a strain isolated from wine, includes glycerol kinase and NAD‐independent glycerol‐3P dehydrogenase. The properties of these enzymes were studied. Glycerol kinase activity was maximal at 28 °C and pH 7·5 in 50 mmol l−1 Tr...
Gespeichert in:
| Veröffentlicht in: | Letters in applied microbiology 1998-08, Vol.27 (2), p.93-97 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 97 |
|---|---|
| container_issue | 2 |
| container_start_page | 93 |
| container_title | Letters in applied microbiology |
| container_volume | 27 |
| creator | Pasteris, S.E Saad, A.M.S. de |
| description | The pathway involved in glycerol dissimilation in Pediococcus pentosaceus N5p, a strain isolated from wine, includes glycerol kinase and NAD‐independent glycerol‐3P dehydrogenase. The properties of these enzymes were studied. Glycerol kinase activity was maximal at 28 °C and pH 7·5 in 50 mmol l−1 Tris‐HCl buffer. The end‐products of the reaction acted as competitive inhibitors while fructose‐1,6‐diphosphate was a non‐competitive inhibitor. Mg2+ was required for optimal enzyme activity. The Km values for both substrates were 0·11 and 0·37 mmol l−1 for glycerol and ATP, respectively. NAD‐independent glycerol‐3P dehydrogenase activity was maximal at 37 °C and pH 7·5 in 100 mmol l−1 Tris‐HCl buffer. The enzymatic activity was activated by KCN and bivalent cations as Mg2+ and Ca2+, but it was strongly inhibited by others. Dihydroxyacetone phosphate acted as competitive inhibitor while ATP and phosphenolpyruvate were non‐competitive inhibitors. |
| doi_str_mv | 10.1046/j.1472-765X.1998.00391.x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_17110910</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>17110910</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3461-4934ec325cb867d93704308f8ec1926400396ae98fef282ac5f80dde8af149053</originalsourceid><addsrcrecordid>eNqNkE1vEzEQhi1EJULhN-AD4raLv9ZrS1yiUD6k0FaCStws4x0nDpv1Ym9EQ_883qYqVy4zI_l5ZuQXIUxJTYmQb3c1FS2rWtl8r6nWqiaEa1rfPkGLx4enaEGYlJVijXiGnue8I4QoyvQC3a22Nlk3QQp_7BTigKPHm_7oIMUe_wyDzYDt0OHL5fsqDB2MUMowPTIVr8ZtzOPWToA72B67FDdwr_kU9_gauhBddO6QcXGnmK2DMl824wt05m2f4eVDP0c3Hy6-rT5V66uPn1fLdeW4kLQSmgtwnDXuh5Jtp3lLBCfKK3BUMynmD0sLWnnwTDHrGq9I14GyngpNGn6O3pz2jin-OkCezD5kB31vB4iHbGhLKdGUFFCdQJdizgm8GVPY23Q0lJg5bbMzc6hmDtXMaZv7tM1tUV8_3LDZ2d4nO7iQ__mSSqF0wd6dsN-hh-N_rzfr5ZcyFP3VSfc2GrtJ5cLNV0YoJ0w3lKmW_wVX4J3Z</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17110910</pqid></control><display><type>article</type><title>Characterization of glycerol kinase and NAD-independent glycerol-3-phosphate dehydrogenase from Pediococcus pentosaceus N5p</title><source>Oxford University Press Journals All Titles (1996-Current)</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Pasteris, S.E ; Saad, A.M.S. de</creator><creatorcontrib>Pasteris, S.E ; Saad, A.M.S. de</creatorcontrib><description>The pathway involved in glycerol dissimilation in Pediococcus pentosaceus N5p, a strain isolated from wine, includes glycerol kinase and NAD‐independent glycerol‐3P dehydrogenase. The properties of these enzymes were studied. Glycerol kinase activity was maximal at 28 °C and pH 7·5 in 50 mmol l−1 Tris‐HCl buffer. The end‐products of the reaction acted as competitive inhibitors while fructose‐1,6‐diphosphate was a non‐competitive inhibitor. Mg2+ was required for optimal enzyme activity. The Km values for both substrates were 0·11 and 0·37 mmol l−1 for glycerol and ATP, respectively. NAD‐independent glycerol‐3P dehydrogenase activity was maximal at 37 °C and pH 7·5 in 100 mmol l−1 Tris‐HCl buffer. The enzymatic activity was activated by KCN and bivalent cations as Mg2+ and Ca2+, but it was strongly inhibited by others. Dihydroxyacetone phosphate acted as competitive inhibitor while ATP and phosphenolpyruvate were non‐competitive inhibitors.</description><identifier>ISSN: 0266-8254</identifier><identifier>EISSN: 1472-765X</identifier><identifier>EISSN: 1365-2673</identifier><identifier>DOI: 10.1046/j.1472-765X.1998.00391.x</identifier><identifier>CODEN: LAMIE7</identifier><language>eng</language><publisher>Edinburgh, UK: Blackwell Science Ltd</publisher><subject>Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; Fermented food industries ; food contamination ; Food industries ; Fundamental and applied biological sciences. Psychology ; horticultural crops ; Mission oriented research ; Pediococcus pentosaceus ; Physiology and metabolism ; Wines and vinegars</subject><ispartof>Letters in applied microbiology, 1998-08, Vol.27 (2), p.93-97</ispartof><rights>The Society for Applied Bacteriology, 1997</rights><rights>1999 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3461-4934ec325cb867d93704308f8ec1926400396ae98fef282ac5f80dde8af149053</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.1472-765X.1998.00391.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1472-765X.1998.00391.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1616489$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Pasteris, S.E</creatorcontrib><creatorcontrib>Saad, A.M.S. de</creatorcontrib><title>Characterization of glycerol kinase and NAD-independent glycerol-3-phosphate dehydrogenase from Pediococcus pentosaceus N5p</title><title>Letters in applied microbiology</title><description>The pathway involved in glycerol dissimilation in Pediococcus pentosaceus N5p, a strain isolated from wine, includes glycerol kinase and NAD‐independent glycerol‐3P dehydrogenase. The properties of these enzymes were studied. Glycerol kinase activity was maximal at 28 °C and pH 7·5 in 50 mmol l−1 Tris‐HCl buffer. The end‐products of the reaction acted as competitive inhibitors while fructose‐1,6‐diphosphate was a non‐competitive inhibitor. Mg2+ was required for optimal enzyme activity. The Km values for both substrates were 0·11 and 0·37 mmol l−1 for glycerol and ATP, respectively. NAD‐independent glycerol‐3P dehydrogenase activity was maximal at 37 °C and pH 7·5 in 100 mmol l−1 Tris‐HCl buffer. The enzymatic activity was activated by KCN and bivalent cations as Mg2+ and Ca2+, but it was strongly inhibited by others. Dihydroxyacetone phosphate acted as competitive inhibitor while ATP and phosphenolpyruvate were non‐competitive inhibitors.</description><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>Fermented food industries</subject><subject>food contamination</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>horticultural crops</subject><subject>Mission oriented research</subject><subject>Pediococcus pentosaceus</subject><subject>Physiology and metabolism</subject><subject>Wines and vinegars</subject><issn>0266-8254</issn><issn>1472-765X</issn><issn>1365-2673</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNqNkE1vEzEQhi1EJULhN-AD4raLv9ZrS1yiUD6k0FaCStws4x0nDpv1Ym9EQ_883qYqVy4zI_l5ZuQXIUxJTYmQb3c1FS2rWtl8r6nWqiaEa1rfPkGLx4enaEGYlJVijXiGnue8I4QoyvQC3a22Nlk3QQp_7BTigKPHm_7oIMUe_wyDzYDt0OHL5fsqDB2MUMowPTIVr8ZtzOPWToA72B67FDdwr_kU9_gauhBddO6QcXGnmK2DMl824wt05m2f4eVDP0c3Hy6-rT5V66uPn1fLdeW4kLQSmgtwnDXuh5Jtp3lLBCfKK3BUMynmD0sLWnnwTDHrGq9I14GyngpNGn6O3pz2jin-OkCezD5kB31vB4iHbGhLKdGUFFCdQJdizgm8GVPY23Q0lJg5bbMzc6hmDtXMaZv7tM1tUV8_3LDZ2d4nO7iQ__mSSqF0wd6dsN-hh-N_rzfr5ZcyFP3VSfc2GrtJ5cLNV0YoJ0w3lKmW_wVX4J3Z</recordid><startdate>199808</startdate><enddate>199808</enddate><creator>Pasteris, S.E</creator><creator>Saad, A.M.S. de</creator><general>Blackwell Science Ltd</general><general>Blackwell Science</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>199808</creationdate><title>Characterization of glycerol kinase and NAD-independent glycerol-3-phosphate dehydrogenase from Pediococcus pentosaceus N5p</title><author>Pasteris, S.E ; Saad, A.M.S. de</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3461-4934ec325cb867d93704308f8ec1926400396ae98fef282ac5f80dde8af149053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Biological and medical sciences</topic><topic>Biology of microorganisms of confirmed or potential industrial interest</topic><topic>Biotechnology</topic><topic>Fermented food industries</topic><topic>food contamination</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>horticultural crops</topic><topic>Mission oriented research</topic><topic>Pediococcus pentosaceus</topic><topic>Physiology and metabolism</topic><topic>Wines and vinegars</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pasteris, S.E</creatorcontrib><creatorcontrib>Saad, A.M.S. de</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Letters in applied microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pasteris, S.E</au><au>Saad, A.M.S. de</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of glycerol kinase and NAD-independent glycerol-3-phosphate dehydrogenase from Pediococcus pentosaceus N5p</atitle><jtitle>Letters in applied microbiology</jtitle><date>1998-08</date><risdate>1998</risdate><volume>27</volume><issue>2</issue><spage>93</spage><epage>97</epage><pages>93-97</pages><issn>0266-8254</issn><eissn>1472-765X</eissn><eissn>1365-2673</eissn><coden>LAMIE7</coden><abstract>The pathway involved in glycerol dissimilation in Pediococcus pentosaceus N5p, a strain isolated from wine, includes glycerol kinase and NAD‐independent glycerol‐3P dehydrogenase. The properties of these enzymes were studied. Glycerol kinase activity was maximal at 28 °C and pH 7·5 in 50 mmol l−1 Tris‐HCl buffer. The end‐products of the reaction acted as competitive inhibitors while fructose‐1,6‐diphosphate was a non‐competitive inhibitor. Mg2+ was required for optimal enzyme activity. The Km values for both substrates were 0·11 and 0·37 mmol l−1 for glycerol and ATP, respectively. NAD‐independent glycerol‐3P dehydrogenase activity was maximal at 37 °C and pH 7·5 in 100 mmol l−1 Tris‐HCl buffer. The enzymatic activity was activated by KCN and bivalent cations as Mg2+ and Ca2+, but it was strongly inhibited by others. Dihydroxyacetone phosphate acted as competitive inhibitor while ATP and phosphenolpyruvate were non‐competitive inhibitors.</abstract><cop>Edinburgh, UK</cop><pub>Blackwell Science Ltd</pub><doi>10.1046/j.1472-765X.1998.00391.x</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0266-8254 |
| ispartof | Letters in applied microbiology, 1998-08, Vol.27 (2), p.93-97 |
| issn | 0266-8254 1472-765X 1365-2673 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_17110910 |
| source | Oxford University Press Journals All Titles (1996-Current); Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Fermented food industries food contamination Food industries Fundamental and applied biological sciences. Psychology horticultural crops Mission oriented research Pediococcus pentosaceus Physiology and metabolism Wines and vinegars |
| title | Characterization of glycerol kinase and NAD-independent glycerol-3-phosphate dehydrogenase from Pediococcus pentosaceus N5p |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-13T20%3A01%3A22IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Characterization%20of%20glycerol%20kinase%20and%20NAD-independent%20glycerol-3-phosphate%20dehydrogenase%20from%20Pediococcus%20pentosaceus%20N5p&rft.jtitle=Letters%20in%20applied%20microbiology&rft.au=Pasteris,%20S.E&rft.date=1998-08&rft.volume=27&rft.issue=2&rft.spage=93&rft.epage=97&rft.pages=93-97&rft.issn=0266-8254&rft.eissn=1472-765X&rft.coden=LAMIE7&rft_id=info:doi/10.1046/j.1472-765X.1998.00391.x&rft_dat=%3Cproquest_cross%3E17110910%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17110910&rft_id=info:pmid/&rfr_iscdi=true |