The W148L substitution in the Escherichia coli ammonium channel AmtB increases flux and indicates that the substrate is an ion

Proceedings of the National Academy of Sciences of the United States of America

Volumn 104, Issue 47, 2007, Pages 18706-18711

  Fong, Rebecca N ^a,b   Kim, Kwang Seo ^a   Yoshihara, Corinne ^a   Inwood, William B ^a   Kustu, Sydney ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Ammonium transport; AmtB channel; Carbon dioxide; Enteric bacteria; Rh protein

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMMONIA; CARBONYL CYANIDE CHLOROPHENYLHYDRAZONE; ESCHERICHIA COLI PROTEIN; GLUTAMATE AMMONIA LIGASE; METHYL GROUP; METHYLAMMONIUM; METHYLGLUTAMINE; MUTANT PROTEIN; PROTEIN AMTB; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BACTERIAL STRAIN; CELL MEMBRANE; CONTROLLED STUDY; ELECTRIC POTENTIAL; ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING;

CATION TRANSPORT PROTEINS; CHROMATOGRAPHY, THIN LAYER; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; IONS; LYSINE; METHYLAMINES; MICROBIAL VIABILITY; MUTATION; TRYPTOPHAN;

ENTEROBACTERIACEAE; ESCHERICHIA COLI;

EID: 36749060099     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0709267104     Document Type: Article

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