pubmed-article:7873535 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7873535 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:7873535 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
pubmed-article:7873535 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
pubmed-article:7873535 | lifeskim:mentions | umls-concept:C0016745 | lld:lifeskim |
pubmed-article:7873535 | lifeskim:mentions | umls-concept:C0680730 | lld:lifeskim |
pubmed-article:7873535 | lifeskim:mentions | umls-concept:C0079866 | lld:lifeskim |
pubmed-article:7873535 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:7873535 | lifeskim:mentions | umls-concept:C0596260 | lld:lifeskim |
pubmed-article:7873535 | lifeskim:mentions | umls-concept:C1148554 | lld:lifeskim |
pubmed-article:7873535 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
pubmed-article:7873535 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:7873535 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:7873535 | pubmed:dateCreated | 1995-4-4 | lld:pubmed |
pubmed-article:7873535 | pubmed:abstractText | Bovine heart fructose 6-P,2-kinase:fructose 2,6-bisphosphatase was expressed in Escherichia coli. In order to determine the role of the carboxyl-terminal peptide, 49 and 78 amino acids from the C-terminus were deleted using oligonucleotide-directed mutagenesis. The expressed wild-type and mutant enzymes were purified to homogeneity, and the steady-state kinetics of the mutant enzymes were compared to those of the wild-type enzyme. Deletion of 49 residues (Del 49) resulted in a 35% decrease in KmFru6P, a 36% increase in Vmax, and a 2-fold increase in Kcat/Km of the kinase. There was no change in the kinetic properties of the phosphatase activity. Deletion of 78 residues (Del 78) resulted in a 4.5-fold decrease in KmFru6P, a 2.5-fold increase in Vmax, a 12-fold increase in kcat/Km of the kinase, and a 3-fold increase in kcat/Km of the phosphatase. Phosphorylation of the wild-type and Del 49 enzymes resulted in decreased KmFru6P and activation of the kinase without affecting the phosphatase activity. Thermal inactivation rates of the wild-type and Del 49 enzymes were similar, but the rate of Del 78 was more rapid. The phosphorylated wild-type and Del 49 enzymes were more sensitive to thermal inactivation than the dephospho forms. Urea inactivation of the kinase and phosphatase of wild-type and Del 49 were similar, but Del 78 was more sensitive to urea. All phosphorylated enzymes were more susceptible to urea inactivation.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
pubmed-article:7873535 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7873535 | pubmed:language | eng | lld:pubmed |
pubmed-article:7873535 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7873535 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7873535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7873535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7873535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7873535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7873535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7873535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7873535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7873535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7873535 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7873535 | pubmed:month | Feb | lld:pubmed |
pubmed-article:7873535 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:7873535 | pubmed:author | pubmed-author:AbeYY | lld:pubmed |
pubmed-article:7873535 | pubmed:author | pubmed-author:UyedaKK | lld:pubmed |
pubmed-article:7873535 | pubmed:author | pubmed-author:LUMM | lld:pubmed |
pubmed-article:7873535 | pubmed:author | pubmed-author:MinamiYY | lld:pubmed |
pubmed-article:7873535 | pubmed:author | pubmed-author:NguyenCC | lld:pubmed |
pubmed-article:7873535 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7873535 | pubmed:day | 28 | lld:pubmed |
pubmed-article:7873535 | pubmed:volume | 34 | lld:pubmed |
pubmed-article:7873535 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7873535 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7873535 | pubmed:pagination | 2553-9 | lld:pubmed |
pubmed-article:7873535 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:meshHeading | pubmed-meshheading:7873535-... | lld:pubmed |
pubmed-article:7873535 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7873535 | pubmed:articleTitle | Expression of bovine heart fructose 6-phosphate,2-kinase:fructose 2,6-bisphosphatase and determination of the role of the carboxyl terminus by mutagenesis. | lld:pubmed |
pubmed-article:7873535 | pubmed:affiliation | Department of Veterans Affairs Medical Center, Dallas, TX 75216. | lld:pubmed |
pubmed-article:7873535 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7873535 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:7873535 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:7873535 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7873535 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7873535 | lld:pubmed |