Adaptive alterations in Lactobacillus casei: II. Variation in the levels of aldolase in cells grown on glucose and ribose
The growth of homofermentative Laclobacillus casei on ribose caused reduction in aldol cleavage of fructose-1,6-diphosphate (FDP) while enhancing activities for condensation of triose phosphates and of fructose-1,6-diphosphatase. The purified preparation of aldolase from L. casei was not inhibited b...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1970-10, Vol.140 (2), p.334-340 |
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| creator | Kaklij, G.S. Nadkarni, G.B. |
| description | The growth of homofermentative
Laclobacillus casei on ribose caused reduction in aldol cleavage of fructose-1,6-diphosphate (FDP) while enhancing activities for condensation of triose phosphates and of fructose-1,6-diphosphatase. The purified preparation of aldolase from
L. casei was not inhibited by EDTA and was not affected by bivalent metal ions (Fe
2+ and Zn
2+). The inactivation of the enzyme by sodium borohydride only in presence of dihydroxyacetone phosphate (DHAP) suggested formation of a Schiff-base intermediate. The enzyme could be resolved into three active components on DEAE-cellulose chromatography. These fractions showed distinct differences in properties with respect to cleavage of FDP and condensation of triose phosphates. The fractions having high cleavage activity gave low condensation reaction. This component was also active for transaldolase reaction. The other two fractions gave higher rate of condensation and lower cleavage values. The profiles obtained for aldolase prepared from ribose-grown cells of
L. casei indicated that there was drastic reduction in the component having high cleavage activity. The results suggest that the equilibrium of the reaction toward cleavage or condensation was determined by isoenzymic composition of aldolase which appears to be adaptively altered by metabolic regulatory controls operative in glucose or ribose-grown cells of
L. casei. |
| doi_str_mv | 10.1016/0003-9861(70)90074-3 |
| format | Article |
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Laclobacillus casei on ribose caused reduction in aldol cleavage of fructose-1,6-diphosphate (FDP) while enhancing activities for condensation of triose phosphates and of fructose-1,6-diphosphatase. The purified preparation of aldolase from
L. casei was not inhibited by EDTA and was not affected by bivalent metal ions (Fe
2+ and Zn
2+). The inactivation of the enzyme by sodium borohydride only in presence of dihydroxyacetone phosphate (DHAP) suggested formation of a Schiff-base intermediate. The enzyme could be resolved into three active components on DEAE-cellulose chromatography. These fractions showed distinct differences in properties with respect to cleavage of FDP and condensation of triose phosphates. The fractions having high cleavage activity gave low condensation reaction. This component was also active for transaldolase reaction. The other two fractions gave higher rate of condensation and lower cleavage values. The profiles obtained for aldolase prepared from ribose-grown cells of
L. casei indicated that there was drastic reduction in the component having high cleavage activity. The results suggest that the equilibrium of the reaction toward cleavage or condensation was determined by isoenzymic composition of aldolase which appears to be adaptively altered by metabolic regulatory controls operative in glucose or ribose-grown cells of
L. casei.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(70)90074-3</identifier><identifier>PMID: 4319594</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acetone ; Amines ; Boron Compounds ; Chemical Phenomena ; Chemistry ; Chromatography, DEAE-Cellulose ; Culture Media ; Edetic Acid ; Fructose - metabolism ; Fructose-Bisphosphatase ; Fructose-Bisphosphate Aldolase - antagonists & inhibitors ; Fructose-Bisphosphate Aldolase - isolation & purification ; Fructose-Bisphosphate Aldolase - metabolism ; Gluconeogenesis ; Glucose - pharmacology ; Glycolysis ; Hexosephosphates - metabolism ; Iron ; Isoenzymes ; Lactobacillus - drug effects ; Lactobacillus - enzymology ; Lactobacillus - growth & development ; Phosphoric Acids - metabolism ; Ribose - pharmacology ; Transferases ; Trioses - metabolism ; Zinc</subject><ispartof>Archives of biochemistry and biophysics, 1970-10, Vol.140 (2), p.334-340</ispartof><rights>1970</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(70)90074-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4319594$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kaklij, G.S.</creatorcontrib><creatorcontrib>Nadkarni, G.B.</creatorcontrib><title>Adaptive alterations in Lactobacillus casei: II. Variation in the levels of aldolase in cells grown on glucose and ribose</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The growth of homofermentative
Laclobacillus casei on ribose caused reduction in aldol cleavage of fructose-1,6-diphosphate (FDP) while enhancing activities for condensation of triose phosphates and of fructose-1,6-diphosphatase. The purified preparation of aldolase from
L. casei was not inhibited by EDTA and was not affected by bivalent metal ions (Fe
2+ and Zn
2+). The inactivation of the enzyme by sodium borohydride only in presence of dihydroxyacetone phosphate (DHAP) suggested formation of a Schiff-base intermediate. The enzyme could be resolved into three active components on DEAE-cellulose chromatography. These fractions showed distinct differences in properties with respect to cleavage of FDP and condensation of triose phosphates. The fractions having high cleavage activity gave low condensation reaction. This component was also active for transaldolase reaction. The other two fractions gave higher rate of condensation and lower cleavage values. The profiles obtained for aldolase prepared from ribose-grown cells of
L. casei indicated that there was drastic reduction in the component having high cleavage activity. The results suggest that the equilibrium of the reaction toward cleavage or condensation was determined by isoenzymic composition of aldolase which appears to be adaptively altered by metabolic regulatory controls operative in glucose or ribose-grown cells of
L. casei.</description><subject>Acetone</subject><subject>Amines</subject><subject>Boron Compounds</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Chromatography, DEAE-Cellulose</subject><subject>Culture Media</subject><subject>Edetic Acid</subject><subject>Fructose - metabolism</subject><subject>Fructose-Bisphosphatase</subject><subject>Fructose-Bisphosphate Aldolase - antagonists & inhibitors</subject><subject>Fructose-Bisphosphate Aldolase - isolation & purification</subject><subject>Fructose-Bisphosphate Aldolase - metabolism</subject><subject>Gluconeogenesis</subject><subject>Glucose - pharmacology</subject><subject>Glycolysis</subject><subject>Hexosephosphates - metabolism</subject><subject>Iron</subject><subject>Isoenzymes</subject><subject>Lactobacillus - drug effects</subject><subject>Lactobacillus - enzymology</subject><subject>Lactobacillus - growth & development</subject><subject>Phosphoric Acids - metabolism</subject><subject>Ribose - pharmacology</subject><subject>Transferases</subject><subject>Trioses - metabolism</subject><subject>Zinc</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1970</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kV1L7DAQhoMoun78A4VciV5UJyZN23MhLOLHwoI36m1Ik6knh2yzJ2lX_PemuniVIc_DMPMOIacMrhgweQ0AvGhqyS4quGwAKlHwHTJj0MgCeC12yexXOSCHKf0DYEzIm32yLzhrykbMyOfc6vXgNki1HzDqwYU-UdfTpTZDaLVx3o-JGp3Q_aGLxRV909F9a5M1_EXqcYM-0dDlFjb4bE7EoM-f7zF89DS77340IRPdWxpdm8tjstdpn_Bk-x6R14f7l7unYvn8uLibLwtklRyKTpfcyI5JYDecCQHc5tl13VUldIIZiVbLsuWtaI2ddhctGJGZtbUtecuPyPlP33UM_0dMg1q5NE2newxjUrWQdc2hzOLZVhzbFVq1jm6l46faZpX57Q_P2-LGYVTJOOwNWhfRDMoGpxio6TZqCl5NwasK1PdtFOdfnC6AeA</recordid><startdate>197010</startdate><enddate>197010</enddate><creator>Kaklij, G.S.</creator><creator>Nadkarni, G.B.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>197010</creationdate><title>Adaptive alterations in Lactobacillus casei: II. Variation in the levels of aldolase in cells grown on glucose and ribose</title><author>Kaklij, G.S. ; Nadkarni, G.B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e176t-fa53c6f16012314403d319a8f750f41c6eda65b3b4bcd10964b0c450fdd8d53b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1970</creationdate><topic>Acetone</topic><topic>Amines</topic><topic>Boron Compounds</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Chromatography, DEAE-Cellulose</topic><topic>Culture Media</topic><topic>Edetic Acid</topic><topic>Fructose - metabolism</topic><topic>Fructose-Bisphosphatase</topic><topic>Fructose-Bisphosphate Aldolase - antagonists & inhibitors</topic><topic>Fructose-Bisphosphate Aldolase - isolation & purification</topic><topic>Fructose-Bisphosphate Aldolase - metabolism</topic><topic>Gluconeogenesis</topic><topic>Glucose - pharmacology</topic><topic>Glycolysis</topic><topic>Hexosephosphates - metabolism</topic><topic>Iron</topic><topic>Isoenzymes</topic><topic>Lactobacillus - drug effects</topic><topic>Lactobacillus - enzymology</topic><topic>Lactobacillus - growth & development</topic><topic>Phosphoric Acids - metabolism</topic><topic>Ribose - pharmacology</topic><topic>Transferases</topic><topic>Trioses - metabolism</topic><topic>Zinc</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kaklij, G.S.</creatorcontrib><creatorcontrib>Nadkarni, G.B.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kaklij, G.S.</au><au>Nadkarni, G.B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Adaptive alterations in Lactobacillus casei: II. Variation in the levels of aldolase in cells grown on glucose and ribose</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1970-10</date><risdate>1970</risdate><volume>140</volume><issue>2</issue><spage>334</spage><epage>340</epage><pages>334-340</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The growth of homofermentative
Laclobacillus casei on ribose caused reduction in aldol cleavage of fructose-1,6-diphosphate (FDP) while enhancing activities for condensation of triose phosphates and of fructose-1,6-diphosphatase. The purified preparation of aldolase from
L. casei was not inhibited by EDTA and was not affected by bivalent metal ions (Fe
2+ and Zn
2+). The inactivation of the enzyme by sodium borohydride only in presence of dihydroxyacetone phosphate (DHAP) suggested formation of a Schiff-base intermediate. The enzyme could be resolved into three active components on DEAE-cellulose chromatography. These fractions showed distinct differences in properties with respect to cleavage of FDP and condensation of triose phosphates. The fractions having high cleavage activity gave low condensation reaction. This component was also active for transaldolase reaction. The other two fractions gave higher rate of condensation and lower cleavage values. The profiles obtained for aldolase prepared from ribose-grown cells of
L. casei indicated that there was drastic reduction in the component having high cleavage activity. The results suggest that the equilibrium of the reaction toward cleavage or condensation was determined by isoenzymic composition of aldolase which appears to be adaptively altered by metabolic regulatory controls operative in glucose or ribose-grown cells of
L. casei.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4319594</pmid><doi>10.1016/0003-9861(70)90074-3</doi><tpages>7</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 1970-10, Vol.140 (2), p.334-340 |
| issn | 0003-9861 1096-0384 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Acetone Amines Boron Compounds Chemical Phenomena Chemistry Chromatography, DEAE-Cellulose Culture Media Edetic Acid Fructose - metabolism Fructose-Bisphosphatase Fructose-Bisphosphate Aldolase - antagonists & inhibitors Fructose-Bisphosphate Aldolase - isolation & purification Fructose-Bisphosphate Aldolase - metabolism Gluconeogenesis Glucose - pharmacology Glycolysis Hexosephosphates - metabolism Iron Isoenzymes Lactobacillus - drug effects Lactobacillus - enzymology Lactobacillus - growth & development Phosphoric Acids - metabolism Ribose - pharmacology Transferases Trioses - metabolism Zinc |
| title | Adaptive alterations in Lactobacillus casei: II. Variation in the levels of aldolase in cells grown on glucose and ribose |
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