| pubmed-article:7771768 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7771768 | lifeskim:mentions | umls-concept:C0016832 | lld:lifeskim |
| pubmed-article:7771768 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:7771768 | lifeskim:mentions | umls-concept:C2247777 | lld:lifeskim |
| pubmed-article:7771768 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:7771768 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:7771768 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:7771768 | pubmed:dateCreated | 1995-6-30 | lld:pubmed |
| pubmed-article:7771768 | pubmed:abstractText | Two enzymes catalyze the two step reactions in the D-galactonate nonphosphorolytic catabolic pathway of Aspergillus terreus, namely D-galactonate dehydratase and 2-keto-3-deoxy-D-galactonate (KDGal) aldolase. Maximum enzyme activities were obtained at 40 degrees C and pH 8.0 or at 50 degrees C and pH 7.5 for these two enzymes, respectively. Stability of the two enzymes under different conditions was investigated. From a Lineweaver-Burk plot of the reciprocal of initial velocities and substrate concentrations, apparent Km values were calculated for D-galactonate, pyruvate and glyceraldehyde and found to be 8.33, 14.28 and 5.55 mM, respectively, in crude cell-free extracts. Results indicated the requirement of magnesium cation for D-galactonate dehydratase activity at an initial concentrations of 10(-2) M. The presence of Mg2+ in the reaction mixture seems to induce greatly the fitness of the dehydratase with D-galactonate as no activity could be detected with 24-h dialyzed extract in the absence of magnesium cation. | lld:pubmed |
| pubmed-article:7771768 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7771768 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7771768 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7771768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7771768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7771768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7771768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7771768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7771768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7771768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7771768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7771768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7771768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7771768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7771768 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7771768 | pubmed:issn | 0003-6072 | lld:pubmed |
| pubmed-article:7771768 | pubmed:author | pubmed-author:BOLTZO HOH | lld:pubmed |
| pubmed-article:7771768 | pubmed:author | pubmed-author:ElshafeiA MAM | lld:pubmed |
| pubmed-article:7771768 | pubmed:author | pubmed-author:MohawedS MSM | lld:pubmed |
| pubmed-article:7771768 | pubmed:author | pubmed-author:Abdel-FatahO... | lld:pubmed |
| pubmed-article:7771768 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7771768 | pubmed:volume | 67 | lld:pubmed |
| pubmed-article:7771768 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7771768 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7771768 | pubmed:pagination | 211-6 | lld:pubmed |
| pubmed-article:7771768 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7771768 | pubmed:meshHeading | pubmed-meshheading:7771768-... | lld:pubmed |
| pubmed-article:7771768 | pubmed:meshHeading | pubmed-meshheading:7771768-... | lld:pubmed |
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| pubmed-article:7771768 | pubmed:meshHeading | pubmed-meshheading:7771768-... | lld:pubmed |
| pubmed-article:7771768 | pubmed:meshHeading | pubmed-meshheading:7771768-... | lld:pubmed |
| pubmed-article:7771768 | pubmed:meshHeading | pubmed-meshheading:7771768-... | lld:pubmed |
| pubmed-article:7771768 | pubmed:meshHeading | pubmed-meshheading:7771768-... | lld:pubmed |
| pubmed-article:7771768 | pubmed:meshHeading | pubmed-meshheading:7771768-... | lld:pubmed |
| pubmed-article:7771768 | pubmed:meshHeading | pubmed-meshheading:7771768-... | lld:pubmed |
| pubmed-article:7771768 | pubmed:meshHeading | pubmed-meshheading:7771768-... | lld:pubmed |
| pubmed-article:7771768 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7771768 | pubmed:articleTitle | Properties of enzymes involved in D-galactonate catabolism in fungi. | lld:pubmed |
| pubmed-article:7771768 | pubmed:affiliation | Department of Microbial Chemistry, National Research Centre, Dokki, Cairo, Egypt. | lld:pubmed |
| pubmed-article:7771768 | pubmed:publicationType | Journal Article | lld:pubmed |
