Developmentally Regulated Interconversions between End Product-Inhibitable and Noninhibitable Forms of a First Pathway-Specific Enzyme Activity Can Be Mimicked in vitro by Protein Dephosphorylation-Phosphorylation Reactions
During the life cycle of Blastocladiella emersonii, dramatic shifts occur in the sensitivity of the first hexosamine biosynthetic pathway-specific enzyme [amidotransferase; 2-amino-2-deoxy-D-glucose-6-phosphate ketol-isomerase (amino-transferring), EC 5.3.1.19] to end product inhibition. These shift...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1982-10, Vol.79 (20), p.6289-6293 |
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| description | During the life cycle of Blastocladiella emersonii, dramatic shifts occur in the sensitivity of the first hexosamine biosynthetic pathway-specific enzyme [amidotransferase; 2-amino-2-deoxy-D-glucose-6-phosphate ketol-isomerase (amino-transferring), EC 5.3.1.19] to end product inhibition. These shifts are developmentally correlated with changes in the utilization of the end product (uridine-5′-diphospho-N-acetylglucosamine) for chitin synthesis [Selitrennikoff, C. P., Dalley, N. E. & Sonneborn, D. R. (1980) Proc. Natl. Acad. Sci. USA 77, 5998-6002]. Alterations in amidotransferase sensitivity to end product inhibition can be mimicked by in vitro protein dephosphorylation-phosphorylation reactions, as follows: (i) Zoospore end product-inhibitable amidotransferase activity can be converted to a noninhibitable form by an endogenous (zoospore) protein phosphatase (phosphoprotein phosphohydrolase EC 3.1.3.16) reaction; this noninhibitable form can be converted back to an inhibitable form either by an endogenous cAMP-independent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) reaction or with an added cAMP-dependent protein kinase. (ii) Noninhibitable amidotransferase activity from growing cells can also be converted to the inhibitable form with added protein kinase. |
| doi_str_mv | 10.1073/pnas.79.20.6289 |
| format | Article |
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These shifts are developmentally correlated with changes in the utilization of the end product (uridine-5′-diphospho-N-acetylglucosamine) for chitin synthesis [Selitrennikoff, C. P., Dalley, N. E. & Sonneborn, D. R. (1980) Proc. Natl. Acad. Sci. USA 77, 5998-6002]. Alterations in amidotransferase sensitivity to end product inhibition can be mimicked by in vitro protein dephosphorylation-phosphorylation reactions, as follows: (i) Zoospore end product-inhibitable amidotransferase activity can be converted to a noninhibitable form by an endogenous (zoospore) protein phosphatase (phosphoprotein phosphohydrolase EC 3.1.3.16) reaction; this noninhibitable form can be converted back to an inhibitable form either by an endogenous cAMP-independent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) reaction or with an added cAMP-dependent protein kinase. (ii) Noninhibitable amidotransferase activity from growing cells can also be converted to the inhibitable form with added protein kinase.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.79.20.6289</identifier><identifier>PMID: 6959119</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Blastocladiella - physiology ; Blastocladiella emersonii ; Carbohydrate Epimerases - metabolism ; Cell Differentiation ; Cell growth ; Cell walls ; Cell-Free System ; Cells ; Chitin ; Enzyme activity ; Enzymes ; Feedback ; Freshwater ; Fungi - physiology ; Gene Expression Regulation ; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) - antagonists & inhibitors ; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) - metabolism ; Mops ; Phosphatases ; Phosphoproteins - physiology ; Phosphorylation ; Protein kinase inhibitors ; Protein Kinases - metabolism ; Spores, Fungal - physiology ; Zoospores</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1982-10, Vol.79 (20), p.6289-6293</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3399-25ca80a1daa9784da8e88afab0a77d17c210e5627ff20ae1bc7db6b8bf3356f13</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/79/20.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/12859$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/12859$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6959119$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Frisa, Phyllis S.</creatorcontrib><creatorcontrib>Sonneborn, David R.</creatorcontrib><title>Developmentally Regulated Interconversions between End Product-Inhibitable and Noninhibitable Forms of a First Pathway-Specific Enzyme Activity Can Be Mimicked in vitro by Protein Dephosphorylation-Phosphorylation Reactions</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>During the life cycle of Blastocladiella emersonii, dramatic shifts occur in the sensitivity of the first hexosamine biosynthetic pathway-specific enzyme [amidotransferase; 2-amino-2-deoxy-D-glucose-6-phosphate ketol-isomerase (amino-transferring), EC 5.3.1.19] to end product inhibition. These shifts are developmentally correlated with changes in the utilization of the end product (uridine-5′-diphospho-N-acetylglucosamine) for chitin synthesis [Selitrennikoff, C. P., Dalley, N. E. & Sonneborn, D. R. (1980) Proc. Natl. Acad. Sci. USA 77, 5998-6002]. Alterations in amidotransferase sensitivity to end product inhibition can be mimicked by in vitro protein dephosphorylation-phosphorylation reactions, as follows: (i) Zoospore end product-inhibitable amidotransferase activity can be converted to a noninhibitable form by an endogenous (zoospore) protein phosphatase (phosphoprotein phosphohydrolase EC 3.1.3.16) reaction; this noninhibitable form can be converted back to an inhibitable form either by an endogenous cAMP-independent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) reaction or with an added cAMP-dependent protein kinase. (ii) Noninhibitable amidotransferase activity from growing cells can also be converted to the inhibitable form with added protein kinase.</description><subject>Blastocladiella - physiology</subject><subject>Blastocladiella emersonii</subject><subject>Carbohydrate Epimerases - metabolism</subject><subject>Cell Differentiation</subject><subject>Cell growth</subject><subject>Cell walls</subject><subject>Cell-Free System</subject><subject>Cells</subject><subject>Chitin</subject><subject>Enzyme activity</subject><subject>Enzymes</subject><subject>Feedback</subject><subject>Freshwater</subject><subject>Fungi - physiology</subject><subject>Gene Expression Regulation</subject><subject>Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) - antagonists & inhibitors</subject><subject>Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) - metabolism</subject><subject>Mops</subject><subject>Phosphatases</subject><subject>Phosphoproteins - physiology</subject><subject>Phosphorylation</subject><subject>Protein kinase inhibitors</subject><subject>Protein Kinases - metabolism</subject><subject>Spores, Fungal - physiology</subject><subject>Zoospores</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUktv1DAQjhColMIZCQnkE5yytZNNHB96KNsurFRgxeNsTZxJ1yWxg-3dEv4sfwWvdunjAgfL9vcYf2NNkjxndMIoz48HA37CxSSjkzKrxIPkkFHB0nIq6MPkkNKMp9U0mz5Onnh_RSkVRUUPkoNSFIIxcZj8PsMNdnbo0QToupF8xst1BwEbsjABnbJmg85razypMVwjGnJuGrJ0tlmrkC7MStc6QN0hgYh_tEbfgebW9Z7YlgCZa-cDWUJYXcOYfhlQ6VarWOzX2CM5VUFvdBjJDAx5i-SD7rX6HlNoQyLuLKnH7aMBI3CGw8r6uNwYo8Zs6fL-PXYBanvwT5NHLXQen-33o-Tb_Pzr7H168endYnZ6kao8FyLNCgUVBdYACF5NG6iwqqCFmgLnDeMqYxSLMuNtm1FAVive1GVd1W2eF2XL8qPkZFd3WNc9Nip-p4NODk734EZpQcv7jNEreWk3Mp9yRsvof733O_tjjT7IXnuFXQcG7drLijJR0Cn_r5AVRclzKqLweCdUznrvsL0Jw6jczo7czo7kQmZUbmcnOl7e7eFGvx-WyL_Z81vjX_a2gGzXXRfwZ4jKV_9URsGLneDKB-tuk2VVIfI_1Pbp8w</recordid><startdate>19821001</startdate><enddate>19821001</enddate><creator>Frisa, Phyllis S.</creator><creator>Sonneborn, David R.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad 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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>M7N</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19821001</creationdate><title>Developmentally Regulated Interconversions between End Product-Inhibitable and Noninhibitable Forms of a First Pathway-Specific Enzyme Activity Can Be Mimicked in vitro by Protein Dephosphorylation-Phosphorylation Reactions</title><author>Frisa, Phyllis S. ; Sonneborn, David R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3399-25ca80a1daa9784da8e88afab0a77d17c210e5627ff20ae1bc7db6b8bf3356f13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Blastocladiella - physiology</topic><topic>Blastocladiella emersonii</topic><topic>Carbohydrate Epimerases - metabolism</topic><topic>Cell Differentiation</topic><topic>Cell growth</topic><topic>Cell walls</topic><topic>Cell-Free System</topic><topic>Cells</topic><topic>Chitin</topic><topic>Enzyme activity</topic><topic>Enzymes</topic><topic>Feedback</topic><topic>Freshwater</topic><topic>Fungi - physiology</topic><topic>Gene Expression Regulation</topic><topic>Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) - antagonists & inhibitors</topic><topic>Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) - metabolism</topic><topic>Mops</topic><topic>Phosphatases</topic><topic>Phosphoproteins - physiology</topic><topic>Phosphorylation</topic><topic>Protein kinase inhibitors</topic><topic>Protein Kinases - metabolism</topic><topic>Spores, Fungal - physiology</topic><topic>Zoospores</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Frisa, Phyllis S.</creatorcontrib><creatorcontrib>Sonneborn, David R.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Frisa, Phyllis S.</au><au>Sonneborn, David R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Developmentally Regulated Interconversions between End Product-Inhibitable and Noninhibitable Forms of a First Pathway-Specific Enzyme Activity Can Be Mimicked in vitro by Protein Dephosphorylation-Phosphorylation Reactions</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1982-10-01</date><risdate>1982</risdate><volume>79</volume><issue>20</issue><spage>6289</spage><epage>6293</epage><pages>6289-6293</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>During the life cycle of Blastocladiella emersonii, dramatic shifts occur in the sensitivity of the first hexosamine biosynthetic pathway-specific enzyme [amidotransferase; 2-amino-2-deoxy-D-glucose-6-phosphate ketol-isomerase (amino-transferring), EC 5.3.1.19] to end product inhibition. These shifts are developmentally correlated with changes in the utilization of the end product (uridine-5′-diphospho-N-acetylglucosamine) for chitin synthesis [Selitrennikoff, C. P., Dalley, N. E. & Sonneborn, D. R. (1980) Proc. Natl. Acad. Sci. USA 77, 5998-6002]. Alterations in amidotransferase sensitivity to end product inhibition can be mimicked by in vitro protein dephosphorylation-phosphorylation reactions, as follows: (i) Zoospore end product-inhibitable amidotransferase activity can be converted to a noninhibitable form by an endogenous (zoospore) protein phosphatase (phosphoprotein phosphohydrolase EC 3.1.3.16) reaction; this noninhibitable form can be converted back to an inhibitable form either by an endogenous cAMP-independent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) reaction or with an added cAMP-dependent protein kinase. (ii) Noninhibitable amidotransferase activity from growing cells can also be converted to the inhibitable form with added protein kinase.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>6959119</pmid><doi>10.1073/pnas.79.20.6289</doi><tpages>5</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 | Blastocladiella - physiology Blastocladiella emersonii Carbohydrate Epimerases - metabolism Cell Differentiation Cell growth Cell walls Cell-Free System Cells Chitin Enzyme activity Enzymes Feedback Freshwater Fungi - physiology Gene Expression Regulation Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) - antagonists & inhibitors Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) - metabolism Mops Phosphatases Phosphoproteins - physiology Phosphorylation Protein kinase inhibitors Protein Kinases - metabolism Spores, Fungal - physiology Zoospores |
| title | Developmentally Regulated Interconversions between End Product-Inhibitable and Noninhibitable Forms of a First Pathway-Specific Enzyme Activity Can Be Mimicked in vitro by Protein Dephosphorylation-Phosphorylation Reactions |
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