Channeling Behavior and Activity Models for Escherichia coli K-12 Acetohydroxy Acid Synthases at Physiological Substrate Levels
The channeling behavior of acetohydroxy acid synthases I and III (EC 4.1.3.18; AHAS) was studied by computer simulation of activities over a wide range of concentrations for the substrates pyruvate and 2-ketobutyrate. The ratios of reaction rates for both channels and three-dimensional plots of sing...
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Veröffentlicht in: | Biochemical and biophysical research communications 1995-02, Vol.207 (1), p.48-54 |
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description | The channeling behavior of acetohydroxy acid synthases I and III (EC 4.1.3.18; AHAS) was studied by computer simulation of activities over a wide range of concentrations for the substrates pyruvate and 2-ketobutyrate. The ratios of reaction rates for both channels and three-dimensional plots of single-channel reaction rates versus substrate concentrations were introduced to compare the substrate channeling properties of the isozymes. Substrate ranges were identified in which AHAS I and III operated both channels, and in which they used only one. Kinetic constants were varied to simulate whether and how AHAS might be made channel-specific. Our study suggests that AHAS might be made channel-specific for acetolactate but not for acetohydroxybutyrate. We postulate specific physiological roles for AHAS I and III to support cell growth under conditions that vary the levels and balance of substrates. |
doi_str_mv | 10.1006/bbrc.1995.1151 |
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The ratios of reaction rates for both channels and three-dimensional plots of single-channel reaction rates versus substrate concentrations were introduced to compare the substrate channeling properties of the isozymes. Substrate ranges were identified in which AHAS I and III operated both channels, and in which they used only one. Kinetic constants were varied to simulate whether and how AHAS might be made channel-specific. Our study suggests that AHAS might be made channel-specific for acetolactate but not for acetohydroxybutyrate. We postulate specific physiological roles for AHAS I and III to support cell growth under conditions that vary the levels and balance of substrates.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.1995.1151</identifier><identifier>PMID: 7857304</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acetolactate Synthase - metabolism ; Amino Acids - metabolism ; Butyrates - metabolism ; Computer Simulation ; Escherichia coli - enzymology ; Escherichia coli - growth & development ; Isoenzymes - metabolism ; Isoleucine - metabolism ; Kinetics ; Pyruvates - metabolism ; Valine - metabolism</subject><ispartof>Biochemical and biophysical research communications, 1995-02, Vol.207 (1), p.48-54</ispartof><rights>1995 Academic Press</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c339t-2a098b622ef643e550413ad8e84a50551fce8595b09ca906e7dea2f1f5da57ee3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.1995.1151$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7857304$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Herring, P.A.</creatorcontrib><creatorcontrib>Mcknight, B.L.</creatorcontrib><creatorcontrib>Jackson, J.H.</creatorcontrib><title>Channeling Behavior and Activity Models for Escherichia coli K-12 Acetohydroxy Acid Synthases at Physiological Substrate Levels</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The channeling behavior of acetohydroxy acid synthases I and III (EC 4.1.3.18; AHAS) was studied by computer simulation of activities over a wide range of concentrations for the substrates pyruvate and 2-ketobutyrate. The ratios of reaction rates for both channels and three-dimensional plots of single-channel reaction rates versus substrate concentrations were introduced to compare the substrate channeling properties of the isozymes. Substrate ranges were identified in which AHAS I and III operated both channels, and in which they used only one. Kinetic constants were varied to simulate whether and how AHAS might be made channel-specific. Our study suggests that AHAS might be made channel-specific for acetolactate but not for acetohydroxybutyrate. We postulate specific physiological roles for AHAS I and III to support cell growth under conditions that vary the levels and balance of substrates.</description><subject>Acetolactate Synthase - metabolism</subject><subject>Amino Acids - metabolism</subject><subject>Butyrates - metabolism</subject><subject>Computer Simulation</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - growth & development</subject><subject>Isoenzymes - metabolism</subject><subject>Isoleucine - metabolism</subject><subject>Kinetics</subject><subject>Pyruvates - metabolism</subject><subject>Valine - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1v1DAQhi1EVZbClRuST9yyzCRxEh_LqnyIRa1UkLhZjj1pjLJxsb0rcupfx6tdceM0mplnXmkext4grBGged_3waxRSrFGFPiMrRAkFCVC_ZytIBNFKfHnC_Yyxl8AiHUjL9ll24m2gnrFnjajnmea3PzAP9CoD84HrmfLr01yB5cW_s1bmiIf8vwmmpGCM6PT3PjJ8a8Flpmk5MfFBv9nyY2z_H6Z06gjRa4TvxuX6PzkH5zRE7_f9zEFnYhv6ZBzX7GLQU-RXp_rFfvx8eb75nOxvf30ZXO9LUxVyVSUGmTXN2VJQ1NXJATUWGnbUVdrAULgYKgTUvQgjZbQUGtJlwMOwmrRElVX7N0p9zH433uKSe1cNDRNeia_j6ptsa5KCRlcn0ATfIyBBvUY3E6HRSGoo3F1NK6OxtXReD54e07e9zuy__Cz4rzvTvv8LR0cBRWNo9mQdYFMUta7_0X_BSZ6kS8</recordid><startdate>19950206</startdate><enddate>19950206</enddate><creator>Herring, P.A.</creator><creator>Mcknight, B.L.</creator><creator>Jackson, J.H.</creator><general>Elsevier Inc</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></search><sort><creationdate>19950206</creationdate><title>Channeling Behavior and Activity Models for Escherichia coli K-12 Acetohydroxy Acid Synthases at Physiological Substrate Levels</title><author>Herring, P.A. ; Mcknight, B.L. ; Jackson, J.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c339t-2a098b622ef643e550413ad8e84a50551fce8595b09ca906e7dea2f1f5da57ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Acetolactate Synthase - metabolism</topic><topic>Amino Acids - metabolism</topic><topic>Butyrates - metabolism</topic><topic>Computer Simulation</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - growth & development</topic><topic>Isoenzymes - metabolism</topic><topic>Isoleucine - metabolism</topic><topic>Kinetics</topic><topic>Pyruvates - metabolism</topic><topic>Valine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Herring, P.A.</creatorcontrib><creatorcontrib>Mcknight, B.L.</creatorcontrib><creatorcontrib>Jackson, J.H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Herring, P.A.</au><au>Mcknight, B.L.</au><au>Jackson, J.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Channeling Behavior and Activity Models for Escherichia coli K-12 Acetohydroxy Acid Synthases at Physiological Substrate Levels</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1995-02-06</date><risdate>1995</risdate><volume>207</volume><issue>1</issue><spage>48</spage><epage>54</epage><pages>48-54</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The channeling behavior of acetohydroxy acid synthases I and III (EC 4.1.3.18; AHAS) was studied by computer simulation of activities over a wide range of concentrations for the substrates pyruvate and 2-ketobutyrate. The ratios of reaction rates for both channels and three-dimensional plots of single-channel reaction rates versus substrate concentrations were introduced to compare the substrate channeling properties of the isozymes. Substrate ranges were identified in which AHAS I and III operated both channels, and in which they used only one. Kinetic constants were varied to simulate whether and how AHAS might be made channel-specific. Our study suggests that AHAS might be made channel-specific for acetolactate but not for acetohydroxybutyrate. We postulate specific physiological roles for AHAS I and III to support cell growth under conditions that vary the levels and balance of substrates.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7857304</pmid><doi>10.1006/bbrc.1995.1151</doi><tpages>7</tpages></addata></record> |
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subjects | Acetolactate Synthase - metabolism Amino Acids - metabolism Butyrates - metabolism Computer Simulation Escherichia coli - enzymology Escherichia coli - growth & development Isoenzymes - metabolism Isoleucine - metabolism Kinetics Pyruvates - metabolism Valine - metabolism |
title | Channeling Behavior and Activity Models for Escherichia coli K-12 Acetohydroxy Acid Synthases at Physiological Substrate Levels |
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