Fructose 1,6-Bisphosphatase: The Role of Lysosomal Enzymes in the Modification of Catalytic and Structural Properties
Seasonal variations in the properties of rabbit-liver fructose 1,6-bisphosphatase have now been linked to corresponding changes in the levels of proteolytic activity in the liver extracts. Incubation of native fructose 1,6-bisphosphatase with purified liver lysosomes causes a 3-fold increase in cata...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1973-02, Vol.70 (2), p.303-305 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Pontremoli, S. Melloni, E. Balestrero, F. Franzi, A. T. De Flora, A. Horecker, B. L. |
| description | Seasonal variations in the properties of rabbit-liver fructose 1,6-bisphosphatase have now been linked to corresponding changes in the levels of proteolytic activity in the liver extracts. Incubation of native fructose 1,6-bisphosphatase with purified liver lysosomes causes a 3-fold increase in catalytic activity at pH 9.2, with a smaller, and variable, decrease in activity tested at pH 7.5. These changes in catalytic properties are accompanied by the appearance of a smaller subunit, as was previously reported for the enzyme treated with subtilisin. AMP, a negative modulator of fructose bisphosphatase activity, protects against this action of lysosomes. This proteolytic modification of fructose bisphosphatase by lysosomal enzymes may play a role in the modulation of gluconeogenesis. |
| doi_str_mv | 10.1073/pnas.70.2.303 |
| format | Article |
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This proteolytic modification of fructose bisphosphatase by lysosomal enzymes may play a role in the modulation of gluconeogenesis.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.70.2.303</identifier><identifier>PMID: 4346880</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Animals ; Biological Sciences: Biochemistry ; Catalysis ; Catalytic activity ; Electrophoresis ; Electrophoresis, Polyacrylamide Gel ; Enzymes ; Fructose-Bisphosphatase - analysis ; Fructose-Bisphosphatase - metabolism ; Gels ; Hydrogen-Ion Concentration ; Liver ; Liver - cytology ; Liver - enzymology ; Liver extracts ; Lysosomes ; Lysosomes - enzymology ; Mice ; Microsomes, Liver - enzymology ; Mitochondria, Liver - enzymology ; Molecular Conformation ; Peptide Hydrolases - metabolism ; Peptide Hydrolases - physiology ; Periodicity ; Rabbits ; Seasons ; Subtilisins - metabolism ; Subtilisins - pharmacology ; Sulfates ; Summer ; Winter</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1973-02, Vol.70 (2), p.303-305</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c451t-16c39bc09e795121b91e01782d183fd4332fa443198eee8184a85571f13acfa03</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/70/2.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/62482$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/62482$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53769,53771,57995,58228</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4346880$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pontremoli, S.</creatorcontrib><creatorcontrib>Melloni, E.</creatorcontrib><creatorcontrib>Balestrero, F.</creatorcontrib><creatorcontrib>Franzi, A. T.</creatorcontrib><creatorcontrib>De Flora, A.</creatorcontrib><creatorcontrib>Horecker, B. L.</creatorcontrib><title>Fructose 1,6-Bisphosphatase: The Role of Lysosomal Enzymes in the Modification of Catalytic and Structural Properties</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Seasonal variations in the properties of rabbit-liver fructose 1,6-bisphosphatase have now been linked to corresponding changes in the levels of proteolytic activity in the liver extracts. Incubation of native fructose 1,6-bisphosphatase with purified liver lysosomes causes a 3-fold increase in catalytic activity at pH 9.2, with a smaller, and variable, decrease in activity tested at pH 7.5. These changes in catalytic properties are accompanied by the appearance of a smaller subunit, as was previously reported for the enzyme treated with subtilisin. AMP, a negative modulator of fructose bisphosphatase activity, protects against this action of lysosomes. This proteolytic modification of fructose bisphosphatase by lysosomal enzymes may play a role in the modulation of gluconeogenesis.</description><subject>Animals</subject><subject>Biological Sciences: Biochemistry</subject><subject>Catalysis</subject><subject>Catalytic activity</subject><subject>Electrophoresis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes</subject><subject>Fructose-Bisphosphatase - analysis</subject><subject>Fructose-Bisphosphatase - metabolism</subject><subject>Gels</subject><subject>Hydrogen-Ion Concentration</subject><subject>Liver</subject><subject>Liver - cytology</subject><subject>Liver - enzymology</subject><subject>Liver extracts</subject><subject>Lysosomes</subject><subject>Lysosomes - enzymology</subject><subject>Mice</subject><subject>Microsomes, Liver - enzymology</subject><subject>Mitochondria, Liver - enzymology</subject><subject>Molecular Conformation</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Peptide Hydrolases - physiology</subject><subject>Periodicity</subject><subject>Rabbits</subject><subject>Seasons</subject><subject>Subtilisins - metabolism</subject><subject>Subtilisins - pharmacology</subject><subject>Sulfates</subject><subject>Summer</subject><subject>Winter</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUGP0zAUhC0EWrqFIxcEki_LiZTn2EkcJA5Q7QJSEQiWs-U6L9SrJA62gyi_HoeWarlwsHyYb2aeNIQ8YrBiUPEX46DDqoJVvuLA75AFg5plpajhLlkA5FUmRS7uk_MQbgCgLiSckTPBRSklLMh05ScTXUDKnpfZGxvGnUtPRx3wJb3eIf3sOqSupZt9cMH1uqOXw699j4HagcYEfHCNba3R0bphBtfJ3O2jNVQPDf0S54LJJ98n70b00WJ4QO61ugv48Pgvydery-v1u2zz8e379etNZkTBYsZKw-utgRqrumA529YMgVUyb5jkbSM4z1stBGe1RETJpNCyKCrWMq5Nq4EvyatD7jhte2wMDjEdokZve-33ymmr_lUGu1Pf3A81R6fgJXl29Hv3fcIQVW-Dwa7TA7opqFTJixp4ArMDaLwLwWN76mCg5pnUPJOqQOWK_-Gf3j7sRB93SfqToz7b_qq37Bf_kVU7dV3EnzFxjw_cTYjOn8AyFzLnvwHvga_k</recordid><startdate>19730201</startdate><enddate>19730201</enddate><creator>Pontremoli, S.</creator><creator>Melloni, E.</creator><creator>Balestrero, F.</creator><creator>Franzi, A. T.</creator><creator>De Flora, A.</creator><creator>Horecker, B. L.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><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>5PM</scope></search><sort><creationdate>19730201</creationdate><title>Fructose 1,6-Bisphosphatase: The Role of Lysosomal Enzymes in the Modification of Catalytic and Structural Properties</title><author>Pontremoli, S. ; Melloni, E. ; Balestrero, F. ; Franzi, A. T. ; De Flora, A. ; Horecker, B. L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c451t-16c39bc09e795121b91e01782d183fd4332fa443198eee8184a85571f13acfa03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Animals</topic><topic>Biological Sciences: Biochemistry</topic><topic>Catalysis</topic><topic>Catalytic activity</topic><topic>Electrophoresis</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes</topic><topic>Fructose-Bisphosphatase - analysis</topic><topic>Fructose-Bisphosphatase - metabolism</topic><topic>Gels</topic><topic>Hydrogen-Ion Concentration</topic><topic>Liver</topic><topic>Liver - cytology</topic><topic>Liver - enzymology</topic><topic>Liver extracts</topic><topic>Lysosomes</topic><topic>Lysosomes - enzymology</topic><topic>Mice</topic><topic>Microsomes, Liver - enzymology</topic><topic>Mitochondria, Liver - enzymology</topic><topic>Molecular Conformation</topic><topic>Peptide Hydrolases - metabolism</topic><topic>Peptide Hydrolases - physiology</topic><topic>Periodicity</topic><topic>Rabbits</topic><topic>Seasons</topic><topic>Subtilisins - metabolism</topic><topic>Subtilisins - pharmacology</topic><topic>Sulfates</topic><topic>Summer</topic><topic>Winter</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pontremoli, S.</creatorcontrib><creatorcontrib>Melloni, E.</creatorcontrib><creatorcontrib>Balestrero, F.</creatorcontrib><creatorcontrib>Franzi, A. 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These changes in catalytic properties are accompanied by the appearance of a smaller subunit, as was previously reported for the enzyme treated with subtilisin. AMP, a negative modulator of fructose bisphosphatase activity, protects against this action of lysosomes. This proteolytic modification of fructose bisphosphatase by lysosomal enzymes may play a role in the modulation of gluconeogenesis.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>4346880</pmid><doi>10.1073/pnas.70.2.303</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Animals Biological Sciences: Biochemistry Catalysis Catalytic activity Electrophoresis Electrophoresis, Polyacrylamide Gel Enzymes Fructose-Bisphosphatase - analysis Fructose-Bisphosphatase - metabolism Gels Hydrogen-Ion Concentration Liver Liver - cytology Liver - enzymology Liver extracts Lysosomes Lysosomes - enzymology Mice Microsomes, Liver - enzymology Mitochondria, Liver - enzymology Molecular Conformation Peptide Hydrolases - metabolism Peptide Hydrolases - physiology Periodicity Rabbits Seasons Subtilisins - metabolism Subtilisins - pharmacology Sulfates Summer Winter |
| title | Fructose 1,6-Bisphosphatase: The Role of Lysosomal Enzymes in the Modification of Catalytic and Structural Properties |
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