| http://purl.uniprot.org/citations/15504109 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15504109 | http://www.w3.org/2000/01/rdf-schema#comment | "PAT1 is a recently identified member of the PAT family of proton/amino acid co-transporters with predominant expression in the plasma membrane of enterocytes and in lysosomal membranes of neurons. Previous studies in Xenopus oocytes expressing PAT1 established proton/substrate co-transport associated with positive inward currents for a variety of small neutral amino acids. Here we provide a detailed analysis of the transport mode of the murine PAT1 in oocytes using the two-electrode voltage-clamp technique to measure steady-state and pre-steady-state currents. The GPC (giant patch clamp) technique and efflux studies were employed to characterize the reversed transport mode. Kinetic parameters [K(m) (Michaelis constant) and I(max) (maximum current)] for transport of various substrates revealed a dependence on membrane potential: hyperpolarization increases the substrate affinity and maximal transport velocity. Proton affinity for interaction with PAT1 is almost 100 nM, corresponding to a pH of 7.0 and is independent of substrate. Kinetic analysis revealed that binding of proton most likely occurs before substrate binding and that the proton and substrate are translocated in a simultaneous step. No evidence for a substrate-uncoupled proton shunt was observed. As shown by efflux studies and current measurements by the GPC technique, PAT1 allows bidirectional amino acid transport. Surprisingly, PAT1 exhibits no pre-steady-state currents in the absence of substrate, even at low temperatures, and therefore PAT1 takes an exceptional position among the ion-coupled co-transporters."xsd:string |
| http://purl.uniprot.org/citations/15504109 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20041519"xsd:string |
| http://purl.uniprot.org/citations/15504109 | http://purl.uniprot.org/core/author | "Boll M."xsd:string |
| http://purl.uniprot.org/citations/15504109 | http://purl.uniprot.org/core/author | "Daniel H."xsd:string |
| http://purl.uniprot.org/citations/15504109 | http://purl.uniprot.org/core/author | "Kottra G."xsd:string |
| http://purl.uniprot.org/citations/15504109 | http://purl.uniprot.org/core/author | "Foltz M."xsd:string |
| http://purl.uniprot.org/citations/15504109 | http://purl.uniprot.org/core/author | "Dietz V."xsd:string |
| http://purl.uniprot.org/citations/15504109 | http://purl.uniprot.org/core/author | "Mertl M."xsd:string |
| http://purl.uniprot.org/citations/15504109 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15504109 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/15504109 | http://purl.uniprot.org/core/pages | "607-616"xsd:string |
| http://purl.uniprot.org/citations/15504109 | http://purl.uniprot.org/core/title | "Kinetics of bidirectional H+ and substrate transport by the proton-dependent amino acid symporter PAT1."xsd:string |
| http://purl.uniprot.org/citations/15504109 | http://purl.uniprot.org/core/volume | "386"xsd:string |
| http://purl.uniprot.org/citations/15504109 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15504109 |
| http://purl.uniprot.org/citations/15504109 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15504109 |
| http://purl.uniprot.org/uniprot/#_Q5F227-mappedCitation-15504109 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15504109 |
| http://purl.uniprot.org/uniprot/#_Q8K4D3-mappedCitation-15504109 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15504109 |
| http://purl.uniprot.org/uniprot/Q5F227 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15504109 |
| http://purl.uniprot.org/uniprot/Q8K4D3 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15504109 |