| pubmed-article:10587945 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10587945 | lifeskim:mentions | umls-concept:C0027307 | lld:lifeskim |
| pubmed-article:10587945 | lifeskim:mentions | umls-concept:C1519068 | lld:lifeskim |
| pubmed-article:10587945 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:10587945 | pubmed:dateCreated | 2000-1-13 | lld:pubmed |
| pubmed-article:10587945 | pubmed:abstractText | The proton-translocating nicotinamide nucleotide transhydrogenases (TH) provide a simple model for understanding chemically coupled transmembrane proton translocation. To further our understanding of TH structure-function relationships, we have identified all sequenced homologous of these vectorial enzymes and have conducted sequence comparison studies. The NAD-binding domains of TH are homologous to bacterial alanine dehydrogenases (ADH) and eukaryotic saccharopine dehydrogenases (SDH) as well as N5(carboxyethyl)-L-ornithine synthase of Lactococcus lactis and dipicolinate synthase of Bacillus subtilis. A multiple alignment, a phylogenetic tree, and two signature sequences for this family, designated the TH-ADH-SDH or TAS superfamily, have been derived. Additionally, the TH family has been characterized. Phylogenetic analyses suggested that these proteins have evolved without inter-system shuffling. However, interdomain splicing-fusion events have occurred during the evolution of several of these systems. Analyses of the multiple alignment for the TH family revealed that domain conservation occurs in the order: NADP-binding domain (domain III) > NAD-binding domain (domain I) > proton-translocating transmembrane domain (domain II). A topologic model for the proton-translocating transmembrane domain consistent with published data is presented, and a possible involvement of specific transmembrane alpha-helical segments in channel formation is suggested. | lld:pubmed |
| pubmed-article:10587945 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10587945 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10587945 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10587945 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10587945 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10587945 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10587945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10587945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10587945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10587945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10587945 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10587945 | pubmed:issn | 1090-6592 | lld:pubmed |
| pubmed-article:10587945 | pubmed:author | pubmed-author:HatefiYY | lld:pubmed |
| pubmed-article:10587945 | pubmed:author | pubmed-author:YamaguchiMM | lld:pubmed |
| pubmed-article:10587945 | pubmed:author | pubmed-author:SaierM HMHJr | lld:pubmed |
| pubmed-article:10587945 | pubmed:author | pubmed-author:StudleyW KWK | lld:pubmed |
| pubmed-article:10587945 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10587945 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:10587945 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10587945 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10587945 | pubmed:pagination | 173-86 | lld:pubmed |
| pubmed-article:10587945 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:10587945 | pubmed:meshHeading | pubmed-meshheading:10587945... | lld:pubmed |
| pubmed-article:10587945 | pubmed:meshHeading | pubmed-meshheading:10587945... | lld:pubmed |
| pubmed-article:10587945 | pubmed:meshHeading | pubmed-meshheading:10587945... | lld:pubmed |
| pubmed-article:10587945 | pubmed:meshHeading | pubmed-meshheading:10587945... | lld:pubmed |
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| pubmed-article:10587945 | pubmed:meshHeading | pubmed-meshheading:10587945... | lld:pubmed |
| pubmed-article:10587945 | pubmed:meshHeading | pubmed-meshheading:10587945... | lld:pubmed |
| pubmed-article:10587945 | pubmed:meshHeading | pubmed-meshheading:10587945... | lld:pubmed |
| pubmed-article:10587945 | pubmed:meshHeading | pubmed-meshheading:10587945... | lld:pubmed |
| pubmed-article:10587945 | pubmed:meshHeading | pubmed-meshheading:10587945... | lld:pubmed |
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| pubmed-article:10587945 | pubmed:meshHeading | pubmed-meshheading:10587945... | lld:pubmed |
| pubmed-article:10587945 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10587945 | pubmed:articleTitle | Phylogenetic analyses of proton-translocating transhydrogenases. | lld:pubmed |
| pubmed-article:10587945 | pubmed:affiliation | Department of Biology, University of California at San Diego, La Jolla, USA. | lld:pubmed |
| pubmed-article:10587945 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10587945 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10587945 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
