Threonine-509 is a determinant of apparent affinity for both substrate and cations in the human Na+/dicarboxylate cotransporter

Biochemistry

Volumn 47, Issue 3, 2008, Pages 1087-1093

  Weerachayaphorn, Jittima ^a   Pajor, Ana M ^a  

^a University of Texas Medical Branch School of Medicine   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON DICARBOXYLATES; DICARBOXYLATE COTRANSPORTERS; FUNCTIONAL DIFFERENCES;

AMINO ACIDS; CITRIC ACID; POSITIVE IONS; SODIUM; SUBSTITUTION REACTIONS; TRANSPORT PROPERTIES;

PROTEINS;

AMINO ACID; CATION; CHIMERIC PROTEIN; CITRIC ACID; COTRANSPORTER; DICARBOXYLIC ACID; SERINE; SODIUM; SODIUM DICARBOXYLATE COTRANSPORTER; SUCCINIC ACID; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; CITRIC ACID CYCLE; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; HUMAN; KIDNEY PROXIMAL TUBULE; NONHUMAN; PRIORITY JOURNAL; RABBIT; SMALL INTESTINE; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CERCOPITHECUS AETHIOPS; CITRIC ACID; COS CELLS; DICARBOXYLIC ACID TRANSPORTERS; GENE EXPRESSION; HUMANS; KINETICS; MOLECULAR SEQUENCE DATA; MUTATION; ORGANIC ANION TRANSPORTERS, SODIUM-DEPENDENT; RABBITS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM; SUBSTRATE SPECIFICITY; SUCCINIC ACID; SYMPORTERS; THREONINE;

ORYCTOLAGUS CUNICULUS;

EID: 38349109841     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701417h     Document Type: Article

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