Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:7857304rdf:typepubmed:Citationlld:pubmed
pubmed-article:7857304lifeskim:mentionsumls-concept:C0026339lld:lifeskim
pubmed-article:7857304lifeskim:mentionsumls-concept:C0014834lld:lifeskim
pubmed-article:7857304lifeskim:mentionsumls-concept:C0026336lld:lifeskim
pubmed-article:7857304lifeskim:mentionsumls-concept:C0004927lld:lifeskim
pubmed-article:7857304lifeskim:mentionsumls-concept:C0000999lld:lifeskim
pubmed-article:7857304lifeskim:mentionsumls-concept:C0814810lld:lifeskim
pubmed-article:7857304lifeskim:mentionsumls-concept:C0441655lld:lifeskim
pubmed-article:7857304lifeskim:mentionsumls-concept:C0441889lld:lifeskim
pubmed-article:7857304lifeskim:mentionsumls-concept:C0205463lld:lifeskim
pubmed-article:7857304lifeskim:mentionsumls-concept:C1710236lld:lifeskim
pubmed-article:7857304pubmed:issue1lld:pubmed
pubmed-article:7857304pubmed:dateCreated1995-3-14lld:pubmed
pubmed-article:7857304pubmed:abstractTextThe 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.lld:pubmed
pubmed-article:7857304pubmed:languageenglld:pubmed
pubmed-article:7857304pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7857304pubmed:citationSubsetIMlld:pubmed
pubmed-article:7857304pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7857304pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7857304pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7857304pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7857304pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7857304pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7857304pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7857304pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7857304pubmed:statusMEDLINElld:pubmed
pubmed-article:7857304pubmed:monthFeblld:pubmed
pubmed-article:7857304pubmed:issn0006-291Xlld:pubmed
pubmed-article:7857304pubmed:authorpubmed-author:JacksonJ HJHlld:pubmed
pubmed-article:7857304pubmed:authorpubmed-author:HerringP APAlld:pubmed
pubmed-article:7857304pubmed:authorpubmed-author:McKnightB LBLlld:pubmed
pubmed-article:7857304pubmed:issnTypePrintlld:pubmed
pubmed-article:7857304pubmed:day6lld:pubmed
pubmed-article:7857304pubmed:volume207lld:pubmed
pubmed-article:7857304pubmed:ownerNLMlld:pubmed
pubmed-article:7857304pubmed:authorsCompleteYlld:pubmed
pubmed-article:7857304pubmed:pagination48-54lld:pubmed
pubmed-article:7857304pubmed:dateRevised2006-11-15lld:pubmed
pubmed-article:7857304pubmed:meshHeadingpubmed-meshheading:7857304-...lld:pubmed
pubmed-article:7857304pubmed:meshHeadingpubmed-meshheading:7857304-...lld:pubmed
pubmed-article:7857304pubmed:meshHeadingpubmed-meshheading:7857304-...lld:pubmed
pubmed-article:7857304pubmed:meshHeadingpubmed-meshheading:7857304-...lld:pubmed
pubmed-article:7857304pubmed:meshHeadingpubmed-meshheading:7857304-...lld:pubmed
pubmed-article:7857304pubmed:meshHeadingpubmed-meshheading:7857304-...lld:pubmed
pubmed-article:7857304pubmed:meshHeadingpubmed-meshheading:7857304-...lld:pubmed
pubmed-article:7857304pubmed:meshHeadingpubmed-meshheading:7857304-...lld:pubmed
pubmed-article:7857304pubmed:meshHeadingpubmed-meshheading:7857304-...lld:pubmed
pubmed-article:7857304pubmed:meshHeadingpubmed-meshheading:7857304-...lld:pubmed
pubmed-article:7857304pubmed:year1995lld:pubmed
pubmed-article:7857304pubmed:articleTitleChanneling behavior and activity models for Escherichia coli K-12 acetohydroxy acid synthases at physiological substrate levels.lld:pubmed
pubmed-article:7857304pubmed:affiliationDepartment of Microbiology, Michigan State University, East Lansing 48824.lld:pubmed
pubmed-article:7857304pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7857304pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
pubmed-article:7857304pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed