Activity of the enzymes involved in the synthesis of exopolysaccharide precursors in an overproducing mutant ropy strain of Streptococcus thermophilus
Abstract The activities of some enzymes belonging to the Leloir pathway, phosphoglucomutase, UDP-glucose pyrophosphorylase, UDP-galactose 4-epimerase and galactose 1-P uridyl transferase, were studied in a wild ropy, a non-ropy and an overproducing mutant ropy strain of Streptococcus thermophilus. T...
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| Veröffentlicht in: | FEMS microbiology letters 2002-04, Vol.209 (2), p.289-293 |
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| creator | Escalante, Adelfo Villegas, Jesús Wacher, Carmen Garcı́a-Garibay, Mariano Farrés, Amelia |
| description | Abstract
The activities of some enzymes belonging to the Leloir pathway, phosphoglucomutase, UDP-glucose pyrophosphorylase, UDP-galactose 4-epimerase and galactose 1-P uridyl transferase, were studied in a wild ropy, a non-ropy and an overproducing mutant ropy strain of Streptococcus thermophilus. These activities were assayed over successive culture transfers along with exocellular polysaccharide (EPS) production. The overproducing mutant ropy strain showed increments in polysaccharide production over successive culture transfers, as opposed to reductions in production by the wild ropy strain. The observed variations among strains in the enzyme activities that were analysed in relation to EPS production suggest their involvement in the synthesis of sugar-nucleotide EPS precursors. |
| doi_str_mv | 10.1111/j.1574-6968.2002.tb11146.x |
| format | Article |
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The activities of some enzymes belonging to the Leloir pathway, phosphoglucomutase, UDP-glucose pyrophosphorylase, UDP-galactose 4-epimerase and galactose 1-P uridyl transferase, were studied in a wild ropy, a non-ropy and an overproducing mutant ropy strain of Streptococcus thermophilus. These activities were assayed over successive culture transfers along with exocellular polysaccharide (EPS) production. The overproducing mutant ropy strain showed increments in polysaccharide production over successive culture transfers, as opposed to reductions in production by the wild ropy strain. The observed variations among strains in the enzyme activities that were analysed in relation to EPS production suggest their involvement in the synthesis of sugar-nucleotide EPS precursors.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2002.tb11146.x</identifier><identifier>PMID: 12007820</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Bacteriology ; Biological and medical sciences ; Culture ; Enzymatic activity ; Enzymes ; Epimerase ; Exocellular polysaccharide ; Exopolysaccharides ; Fundamental and applied biological sciences. Psychology ; Galactose ; Gene Expression Regulation, Bacterial ; Gene Expression Regulation, Enzymologic ; Genetics ; Metabolism. Enzymes ; Microbiology ; Mutant strain ; Mutation - physiology ; Nucleotides ; Phenotype ; Phosphoglucomutase ; Phosphoglucomutase - genetics ; Phosphoglucomutase - metabolism ; Polysaccharides ; Polysaccharides, Bacterial - biosynthesis ; Precursor synthesizing enzyme ; Precursors ; Streptococcus - enzymology ; Streptococcus - genetics ; Streptococcus thermophilus ; Synthesis ; UDPglucose 4-Epimerase - genetics ; UDPglucose 4-Epimerase - metabolism ; UTP-Glucose-1-Phosphate Uridylyltransferase - genetics ; UTP-Glucose-1-Phosphate Uridylyltransferase - metabolism ; UTP-Hexose-1-Phosphate Uridylyltransferase - genetics ; UTP-Hexose-1-Phosphate Uridylyltransferase - metabolism ; Yogurt</subject><ispartof>FEMS microbiology letters, 2002-04, Vol.209 (2), p.289-293</ispartof><rights>2002 Federation of European Microbiological Societies 2002</rights><rights>2002 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4379-acbbecf8dd899a25611fd051fe4a2f77c7883d62dfed1954636789e7d6b49d443</citedby><cites>FETCH-LOGICAL-c4379-acbbecf8dd899a25611fd051fe4a2f77c7883d62dfed1954636789e7d6b49d443</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.2002.tb11146.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2002.tb11146.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,778,782,1414,27907,27908,45557,45558</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14275472$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12007820$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Escalante, Adelfo</creatorcontrib><creatorcontrib>Villegas, Jesús</creatorcontrib><creatorcontrib>Wacher, Carmen</creatorcontrib><creatorcontrib>Garcı́a-Garibay, Mariano</creatorcontrib><creatorcontrib>Farrés, Amelia</creatorcontrib><title>Activity of the enzymes involved in the synthesis of exopolysaccharide precursors in an overproducing mutant ropy strain of Streptococcus thermophilus</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
The activities of some enzymes belonging to the Leloir pathway, phosphoglucomutase, UDP-glucose pyrophosphorylase, UDP-galactose 4-epimerase and galactose 1-P uridyl transferase, were studied in a wild ropy, a non-ropy and an overproducing mutant ropy strain of Streptococcus thermophilus. These activities were assayed over successive culture transfers along with exocellular polysaccharide (EPS) production. The overproducing mutant ropy strain showed increments in polysaccharide production over successive culture transfers, as opposed to reductions in production by the wild ropy strain. The observed variations among strains in the enzyme activities that were analysed in relation to EPS production suggest their involvement in the synthesis of sugar-nucleotide EPS precursors.</description><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Culture</subject><subject>Enzymatic activity</subject><subject>Enzymes</subject><subject>Epimerase</subject><subject>Exocellular polysaccharide</subject><subject>Exopolysaccharides</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Galactose</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Genetics</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>Mutant strain</subject><subject>Mutation - physiology</subject><subject>Nucleotides</subject><subject>Phenotype</subject><subject>Phosphoglucomutase</subject><subject>Phosphoglucomutase - genetics</subject><subject>Phosphoglucomutase - metabolism</subject><subject>Polysaccharides</subject><subject>Polysaccharides, Bacterial - biosynthesis</subject><subject>Precursor synthesizing enzyme</subject><subject>Precursors</subject><subject>Streptococcus - enzymology</subject><subject>Streptococcus - genetics</subject><subject>Streptococcus thermophilus</subject><subject>Synthesis</subject><subject>UDPglucose 4-Epimerase - genetics</subject><subject>UDPglucose 4-Epimerase - metabolism</subject><subject>UTP-Glucose-1-Phosphate Uridylyltransferase - genetics</subject><subject>UTP-Glucose-1-Phosphate Uridylyltransferase - metabolism</subject><subject>UTP-Hexose-1-Phosphate Uridylyltransferase - genetics</subject><subject>UTP-Hexose-1-Phosphate Uridylyltransferase - metabolism</subject><subject>Yogurt</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqVkd-K1DAUxoso7uzqK0hR3LvWJE3zx4uFZXFVGPFCvQ5pkjoZ2qYmzTj1QXxeU6e4IIqYm4ST3_edc_iy7CkEJUznxb6ENcUF4YSVCABUTk0qY1Ie72WbX1_3sw2oKCsg4PQsOw9hDwDACJCH2RlMMsoQ2GTfr9VkD3aac9fm087kZvg29ybkdji47mB0evysh3lIV7BhAc3Rja6bg1RqJ73VJh-9UdEH5xdlLofcHYwfvdNR2eFz3sdJDlPu3TjnYfIyMcnmw-TNODnllIph6eJ7N-5sF8Oj7EEru2Aer_dF9un21cebN8X2_eu3N9fbQuGK8kKqpjGqZVozziWqCYStBjVsDZaopVRRxipNkG6NhrzGpCKUcUM1aTDXGFcX2eXJN436JZowid4GZbpODsbFICgkjLMK_hOErOKQAZbAZ7-Bexf9kJYQqIKAkBqzOlEvT5TyLgRvWjF620s_CwjEErLYiyVJsSQplpDFGrI4JvGTtUVseqPvpGuqCXi-AjIo2bVeDsqGOw4jWmOKEnd14r7azsz_MYK4fbdFjCeD-mTg4vgXefGnDX4AKJbYCg</recordid><startdate>20020409</startdate><enddate>20020409</enddate><creator>Escalante, Adelfo</creator><creator>Villegas, Jesús</creator><creator>Wacher, Carmen</creator><creator>Garcı́a-Garibay, Mariano</creator><creator>Farrés, Amelia</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20020409</creationdate><title>Activity of the enzymes involved in the synthesis of exopolysaccharide precursors in an overproducing mutant ropy strain of Streptococcus thermophilus</title><author>Escalante, Adelfo ; Villegas, Jesús ; Wacher, Carmen ; Garcı́a-Garibay, Mariano ; Farrés, Amelia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4379-acbbecf8dd899a25611fd051fe4a2f77c7883d62dfed1954636789e7d6b49d443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Culture</topic><topic>Enzymatic activity</topic><topic>Enzymes</topic><topic>Epimerase</topic><topic>Exocellular polysaccharide</topic><topic>Exopolysaccharides</topic><topic>Fundamental and applied biological sciences. 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Enzymes</topic><topic>Microbiology</topic><topic>Mutant strain</topic><topic>Mutation - physiology</topic><topic>Nucleotides</topic><topic>Phenotype</topic><topic>Phosphoglucomutase</topic><topic>Phosphoglucomutase - genetics</topic><topic>Phosphoglucomutase - metabolism</topic><topic>Polysaccharides</topic><topic>Polysaccharides, Bacterial - biosynthesis</topic><topic>Precursor synthesizing enzyme</topic><topic>Precursors</topic><topic>Streptococcus - enzymology</topic><topic>Streptococcus - genetics</topic><topic>Streptococcus thermophilus</topic><topic>Synthesis</topic><topic>UDPglucose 4-Epimerase - genetics</topic><topic>UDPglucose 4-Epimerase - metabolism</topic><topic>UTP-Glucose-1-Phosphate Uridylyltransferase - genetics</topic><topic>UTP-Glucose-1-Phosphate Uridylyltransferase - metabolism</topic><topic>UTP-Hexose-1-Phosphate Uridylyltransferase - genetics</topic><topic>UTP-Hexose-1-Phosphate Uridylyltransferase - metabolism</topic><topic>Yogurt</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Escalante, Adelfo</creatorcontrib><creatorcontrib>Villegas, Jesús</creatorcontrib><creatorcontrib>Wacher, Carmen</creatorcontrib><creatorcontrib>Garcı́a-Garibay, Mariano</creatorcontrib><creatorcontrib>Farrés, Amelia</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>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection (ProQuest)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Escalante, Adelfo</au><au>Villegas, Jesús</au><au>Wacher, Carmen</au><au>Garcı́a-Garibay, Mariano</au><au>Farrés, Amelia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activity of the enzymes involved in the synthesis of exopolysaccharide precursors in an overproducing mutant ropy strain of Streptococcus thermophilus</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2002-04-09</date><risdate>2002</risdate><volume>209</volume><issue>2</issue><spage>289</spage><epage>293</epage><pages>289-293</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Abstract
The activities of some enzymes belonging to the Leloir pathway, phosphoglucomutase, UDP-glucose pyrophosphorylase, UDP-galactose 4-epimerase and galactose 1-P uridyl transferase, were studied in a wild ropy, a non-ropy and an overproducing mutant ropy strain of Streptococcus thermophilus. These activities were assayed over successive culture transfers along with exocellular polysaccharide (EPS) production. The overproducing mutant ropy strain showed increments in polysaccharide production over successive culture transfers, as opposed to reductions in production by the wild ropy strain. The observed variations among strains in the enzyme activities that were analysed in relation to EPS production suggest their involvement in the synthesis of sugar-nucleotide EPS precursors.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>12007820</pmid><doi>10.1111/j.1574-6968.2002.tb11146.x</doi><tpages>5</tpages></addata></record> |
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| ispartof | FEMS microbiology letters, 2002-04, Vol.209 (2), p.289-293 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Bacteriology Biological and medical sciences Culture Enzymatic activity Enzymes Epimerase Exocellular polysaccharide Exopolysaccharides Fundamental and applied biological sciences. Psychology Galactose Gene Expression Regulation, Bacterial Gene Expression Regulation, Enzymologic Genetics Metabolism. Enzymes Microbiology Mutant strain Mutation - physiology Nucleotides Phenotype Phosphoglucomutase Phosphoglucomutase - genetics Phosphoglucomutase - metabolism Polysaccharides Polysaccharides, Bacterial - biosynthesis Precursor synthesizing enzyme Precursors Streptococcus - enzymology Streptococcus - genetics Streptococcus thermophilus Synthesis UDPglucose 4-Epimerase - genetics UDPglucose 4-Epimerase - metabolism UTP-Glucose-1-Phosphate Uridylyltransferase - genetics UTP-Glucose-1-Phosphate Uridylyltransferase - metabolism UTP-Hexose-1-Phosphate Uridylyltransferase - genetics UTP-Hexose-1-Phosphate Uridylyltransferase - metabolism Yogurt |
| title | Activity of the enzymes involved in the synthesis of exopolysaccharide precursors in an overproducing mutant ropy strain of Streptococcus thermophilus |
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