Phosphorylation of isocitrate dehydrogenase as a demonstration of enhanced sensitivity in covalent regulation
The sensitivity to regulation of proteins undergoing covalent modification can be greatly increased when the substrates saturate the converter enzymes. This phenomenon, termed zero-order ultrasensitivity, has been found to occur in the reversible phosphorylation of isocitrate dehydrogenase. The poss...
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| Veröffentlicht in: | Nature (London) 1983-09, Vol.305 (5932), p.286-290 |
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| container_title | Nature (London) |
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| creator | LaPorte, David C. Koshland, Daniel E. |
| description | The sensitivity to regulation of proteins undergoing covalent modification can be greatly increased when the substrates saturate the converter enzymes. This phenomenon, termed zero-order ultrasensitivity, has been found to occur in the reversible phosphorylation of isocitrate dehydrogenase. The possibility that this enhanced sensitivity is a common feature of covalent regulatory systems is discussed. |
| doi_str_mv | 10.1038/305286a0 |
| format | Article |
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Psychology</subject><subject>Humanities and Social Sciences</subject><subject>Isocitrate Dehydrogenase - metabolism</subject><subject>Kinetics</subject><subject>multidisciplinary</subject><subject>Oxidoreductases</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Kinases - metabolism</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkEuLFDEURoMoYzsK_gGhFiK6KL2pVOexHAZfMKALXRe3UzfdGaqSNrdqoP-91XQ5G1eBew5f4AjxWsJHCcp-UrBtrEZ4IjayNbputTVPxQagsTVYpZ-LF8z3ALCVpr0SV1rJRkmzEePPQ-bjIZfTgFPMqcqhipx9nApOVPV0OPUl7ykhU4Vc4XIac-IzXnVKB0ye-oopcZziQ5xOVUyVzw84UJqqQvv5sv5SPAs4ML1a32vx-8vnX7ff6rsfX7_f3tzVvgUz1VvZh95hgAbAhSB18E72krZOtjtETyYo1waJhmBHO2ula22DWvbOoHZeXYt3l91jyX9m4qkbI3saBkyUZ-4saOOssov4_iL6kpkLhe5Y4ojl1EnozmW7f2UX9c26Oe9G6h_FNeXC364c2eMQyhIl8qPmlAOlztqHi8YLSXsq3X2eS1pq_P_lX5n_j_U</recordid><startdate>19830901</startdate><enddate>19830901</enddate><creator>LaPorte, David C.</creator><creator>Koshland, Daniel E.</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</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>7X8</scope></search><sort><creationdate>19830901</creationdate><title>Phosphorylation of isocitrate dehydrogenase as a demonstration of enhanced sensitivity in covalent regulation</title><author>LaPorte, David C. ; Koshland, Daniel E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c407t-51dfd9af02009ff16fc91d1e5914baace7f394f1a7e0beb8819482a61d97a69c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Allosteric Regulation</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Enzyme Activation</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. 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| ispartof | Nature (London), 1983-09, Vol.305 (5932), p.286-290 |
| issn | 0028-0836 1476-4687 |
| language | eng |
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| source | MEDLINE; Nature; SpringerLink Journals - AutoHoldings |
| subjects | Allosteric Regulation Analytical, structural and metabolic biochemistry Biological and medical sciences Enzyme Activation Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humanities and Social Sciences Isocitrate Dehydrogenase - metabolism Kinetics multidisciplinary Oxidoreductases Phosphoprotein Phosphatases - metabolism Phosphoproteins - metabolism Phosphorylation Protein Kinases - metabolism Science Science (multidisciplinary) |
| title | Phosphorylation of isocitrate dehydrogenase as a demonstration of enhanced sensitivity in covalent regulation |
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