Characterization of Glu126 and Arg144, two residues that are indispensable for substrate binding in the lactose permease of Escherichia coli

Biochemistry

Volumn 38, Issue 2, 1999, Pages 813-819

  Sahin Tóth, Miklós ^a   Le Coutre, Johannes ^a   Kharabi, Darius ^a   Le Maire, Guerric ^a   Lee, Jenny C ^a   Kaback, H Ronald ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LACTOSE PERMEASE;

AMINO ACID SEQUENCE; ARTICLE; ENERGY TRANSFER; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SUBSTITUTION; ARGININE; BINDING SITES; BIOLOGICAL TRANSPORT, ACTIVE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; ETHYLMALEIMIDE; GLUTAMIC ACID; LACTOSE; MEMBRANE TRANSPORT PROTEINS; MONOSACCHARIDE TRANSPORT PROTEINS; MUTAGENESIS, SITE-DIRECTED; NITROPHENYLGALACTOSIDES; PROTONS; SUBSTRATE SPECIFICITY; SYMPORTERS; THIOGALACTOSIDES;

ESCHERICHIA COLI;

EID: 0038257492     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982200h     Document Type: Article

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