Linked Life Data

17417702

Source:http://linkedlifedata.com/resource/pubmed/id/17417702

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-4-18
pubmed:abstractText
The Na(+)-dependent transport of neutral amino acids in epithelial cells and neurons is mediated by B(0)-type neutral amino acid transporters. Two B(0)-type amino acid transporters have been identified in the neurotransmitter transporter family SLC6, namely B(0)AT1 (SLC6A19) and B(0)AT2 (SLC6A15). In contrast to other members of this family, B(0)-like transporters are chloride-independent. B(0)AT1 and B(0)AT2 preferentially bind the substrate prior to the Na(+)-ion. The Na(+)-concentration affects the K ( m ) of the substrate and vice versa. A kinetic scheme is proposed that is consistent with the experimental data. An overlapping binding site of substrate and cosubstrate has been demonstrated in the bacterial orthologue LeuT( Aa ) from Aquifex aeolicus, which elegantly explains the mutual effect of substrate and cosubstrate on each other's K ( m )-value. LeuT( Aa ) is sequence-related to transporters of the SLC6 family, allowing homology modeling of B(0)-like transporters along its structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0022-2631
pubmed:author
pubmed:issnType
Print
pubmed:volume
213
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
111-8
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Mechanism and putative structure of B(0)-like neutral amino acid transporters.
pubmed:affiliation
Department of Biological Sciences, University of Calgary, 2500 University Dr. NW, Calgary, Alberta, Canada, T2N 1N4.
pubmed:publicationType
Journal Article, In Vitro, Review, Research Support, Non-U.S. Gov't