| pubmed-article:15810435 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15810435 | lifeskim:mentions | umls-concept:C0995888 | lld:lifeskim |
| pubmed-article:15810435 | lifeskim:mentions | umls-concept:C0040632 | lld:lifeskim |
| pubmed-article:15810435 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:15810435 | pubmed:dateCreated | 2005-4-6 | lld:pubmed |
| pubmed-article:15810435 | pubmed:abstractText | The Methanocaldococcus jannaschii genome contains putative genes for all four nonoxidative pentose phosphate pathway enzymes. Open reading frame (ORF) MJ0960 is a member of the mipB/talC family of 'transaldolase-like' genes, so named because of their similarity to the well-characterized transaldolase B gene family. However, recently, it has been reported that both the mipB and the talC genes from Escherichia coli encode novel enzymes with fructose-6-phosphate aldolase activity, not transaldolase activity (Schürmann and Sprenger 2001). The same study reports that other members of the mipB/talC family appear to encode transaldolases. To confirm the function of MJ0960 and to clarify the presence of a nonoxidative pentose phosphate pathway in M. jannaschii, we have cloned ORF MJ0960 from M. jannaschii genomic DNA and purified the recombinant protein. MJ0960 encodes a transaldolase and displays no fructose-6-phosphate aldolase activity. It etained full activity for 4 h at 80 degrees C, and for 3 weeks at 25 degrees C. Methanocaldococcus jannaschii transaldolase has a maximal velocity (Vmax) of 1.0 +/- 0.2 micromol min(-1) mg(-1) at 25 degrees C, whereas Vmax = 12.0 +/- 0.5 micromol min(-1) mg(-1) at 50 degrees C. Apparent Michaelis constants at 50 degrees C were Km = 0.65 +/- 0.09 mM for fructose-6-phosphate and Km = 27.8 +/- 4.3 microM for erythrose-4-phosphate. When ribose-5-phosphate replaced erythrose-4-phosphate as an aldose acceptor, Vmax decreased twofold, whereas the Km was 150-fold higher. The molecular mass of the active enzyme is 271 +/- 27 kDa as estimated by gel filtration, whereas the predicted monomer size is 23.96 kDa, suggesting that the native form of the protein is probably a decamer. A readily available source of thermophilic pentose phosphate pathway enzymes including transaldolase may have direct application in enzymatic biohydrogen production. | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15810435 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15810435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15810435 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15810435 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:15810435 | pubmed:issn | 1472-3646 | lld:pubmed |
| pubmed-article:15810435 | pubmed:author | pubmed-author:SoderbergTimT | lld:pubmed |
| pubmed-article:15810435 | pubmed:author | pubmed-author:AlverRobert... | lld:pubmed |
| pubmed-article:15810435 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15810435 | pubmed:volume | 1 | lld:pubmed |
| pubmed-article:15810435 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15810435 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15810435 | pubmed:pagination | 255-62 | lld:pubmed |
| pubmed-article:15810435 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:meshHeading | pubmed-meshheading:15810435... | lld:pubmed |
| pubmed-article:15810435 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15810435 | pubmed:articleTitle | Transaldolase of Methanocaldococcus jannaschii. | lld:pubmed |
| pubmed-article:15810435 | pubmed:affiliation | Division of Science and Mathematics, University of Minnesota, Morris, 600 E. 4th Street, Morris, MN 56267, USA. soderbt@mrs.umn.edu | lld:pubmed |
| pubmed-article:15810435 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15810435 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:1451858 | entrezgene:pubmed | pubmed-article:15810435 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:15810435 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15810435 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15810435 | lld:pubmed |
