pubmed-article:7857304 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7857304 | lifeskim:mentions | umls-concept:C0026339 | lld:lifeskim |
pubmed-article:7857304 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:7857304 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
pubmed-article:7857304 | lifeskim:mentions | umls-concept:C0004927 | lld:lifeskim |
pubmed-article:7857304 | lifeskim:mentions | umls-concept:C0000999 | lld:lifeskim |
pubmed-article:7857304 | lifeskim:mentions | umls-concept:C0814810 | lld:lifeskim |
pubmed-article:7857304 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:7857304 | lifeskim:mentions | umls-concept:C0441889 | lld:lifeskim |
pubmed-article:7857304 | lifeskim:mentions | umls-concept:C0205463 | lld:lifeskim |
pubmed-article:7857304 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
pubmed-article:7857304 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:7857304 | pubmed:dateCreated | 1995-3-14 | lld:pubmed |
pubmed-article:7857304 | pubmed:abstractText | 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. | lld:pubmed |
pubmed-article:7857304 | pubmed:language | eng | lld:pubmed |
pubmed-article:7857304 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7857304 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7857304 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7857304 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7857304 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7857304 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7857304 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7857304 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7857304 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7857304 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7857304 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7857304 | pubmed:month | Feb | lld:pubmed |
pubmed-article:7857304 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:7857304 | pubmed:author | pubmed-author:JacksonJ HJH | lld:pubmed |
pubmed-article:7857304 | pubmed:author | pubmed-author:HerringP APA | lld:pubmed |
pubmed-article:7857304 | pubmed:author | pubmed-author:McKnightB LBL | lld:pubmed |
pubmed-article:7857304 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7857304 | pubmed:day | 6 | lld:pubmed |
pubmed-article:7857304 | pubmed:volume | 207 | lld:pubmed |
pubmed-article:7857304 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7857304 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7857304 | pubmed:pagination | 48-54 | lld:pubmed |
pubmed-article:7857304 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:7857304 | pubmed:meshHeading | pubmed-meshheading:7857304-... | lld:pubmed |
pubmed-article:7857304 | pubmed:meshHeading | pubmed-meshheading:7857304-... | lld:pubmed |
pubmed-article:7857304 | pubmed:meshHeading | pubmed-meshheading:7857304-... | lld:pubmed |
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pubmed-article:7857304 | pubmed:meshHeading | pubmed-meshheading:7857304-... | lld:pubmed |
pubmed-article:7857304 | pubmed:meshHeading | pubmed-meshheading:7857304-... | lld:pubmed |
pubmed-article:7857304 | pubmed:meshHeading | pubmed-meshheading:7857304-... | lld:pubmed |
pubmed-article:7857304 | pubmed:meshHeading | pubmed-meshheading:7857304-... | lld:pubmed |
pubmed-article:7857304 | pubmed:meshHeading | pubmed-meshheading:7857304-... | lld:pubmed |
pubmed-article:7857304 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7857304 | pubmed:articleTitle | Channeling behavior and activity models for Escherichia coli K-12 acetohydroxy acid synthases at physiological substrate levels. | lld:pubmed |
pubmed-article:7857304 | pubmed:affiliation | Department of Microbiology, Michigan State University, East Lansing 48824. | lld:pubmed |
pubmed-article:7857304 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7857304 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:7857304 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |