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Literature summary for 7.4.2.6 extracted from

  • Sangaletti, R.; Terova, G.; Peres, A.; Bossi, E.; Cora, S.; Saroglia, M.
    Functional expression of the oligopeptide transporter PepT1 from the sea bass (Dicentrarchus labrax) (2009), Pflugers Arch., 459, 47-54.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
cloning in Escherichia coli JM109, PepT1 translation in Xenopus oocytes Dicentrarchus labrax

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information PepT1 shows an increase in apparent substrate affinity at acidic pH, kinetics at pH 6.0-8.0, overview Dicentrarchus labrax

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane integral Dicentrarchus labrax 5886
-

Organism

Organism UniProt Comment Textmining
Dicentrarchus labrax
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
intestine
-
Dicentrarchus labrax
-

Synonyms

Synonyms Comment Organism
oligopeptide transporter 1
-
Dicentrarchus labrax
PepT1 belongs tot he SLC15 family Dicentrarchus labrax

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
PepT1 activity is pH-dependent and shows an increase in apparent substrate affinity at acidic pH Dicentrarchus labrax

pH Range

pH Minimum pH Maximum Comment Organism
6 8 pH-dependent activity, kinetics, overview Dicentrarchus labrax

General Information

General Information Comment Organism
physiological function PepT1 is an integral plasma membrane protein responsible for the uptake of dietary di- and tripeptides in cells. It transports peptides against a concentration gradient in a pH-dependent manner. PepT1 transporter is electrogenic Dicentrarchus labrax