Source:http://linkedlifedata.com/resource/pubmed/id/10587945
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2000-1-13
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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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1090-6592
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
173-86
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10587945-Amino Acid Oxidoreductases,
pubmed-meshheading:10587945-Amino Acid Sequence,
pubmed-meshheading:10587945-Bacteria,
pubmed-meshheading:10587945-Biological Transport,
pubmed-meshheading:10587945-Eukaryotic Cells,
pubmed-meshheading:10587945-Molecular Sequence Data,
pubmed-meshheading:10587945-NADP Transhydrogenases,
pubmed-meshheading:10587945-Phylogeny,
pubmed-meshheading:10587945-Protons,
pubmed-meshheading:10587945-Saccharopine Dehydrogenases,
pubmed-meshheading:10587945-Sequence Alignment,
pubmed-meshheading:10587945-Structure-Activity Relationship
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pubmed:year |
1999
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pubmed:articleTitle |
Phylogenetic analyses of proton-translocating transhydrogenases.
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pubmed:affiliation |
Department of Biology, University of California at San Diego, La Jolla, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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