Importance of the seryl and threonyl residues of the fifth transmembrane domain to the substrate specificity of yeast plasma membrane Na +/H+ antiporters

Molecular Membrane Biology

Volumn 23, Issue 4, 2006, Pages 349-361

  Kinclova Zimmermannova, Olga ^a   Zavrel, Martin ^a   Sychrova, Hana ^a  

^a INSTITUTE OF PHYSIOLOGY   (Czech Republic)

Author keywords

Hydroxyl groups; K+ efflux; Na+ efflux; Na+ H+ antiporter; Substrate specificity; yeast

Indexed keywords

ALKALI METAL; AMINO ACID; ANTIPORTER; ASPARTIC ACID; CATION; HYDROGEN; HYDROXYL GROUP; LITHIUM; POTASSIUM; SODIUM; VALINE;

ARTICLE; CELL MEMBRANE; CELL SPECIFICITY; CONTROLLED STUDY; GENE MUTATION; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; SITE DIRECTED MUTAGENESIS; YEAST; ZYGOSACCHAROMYCES ROUXII;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CELL MEMBRANE; FUNGAL PROTEINS; ION TRANSPORT; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SERINE; SODIUM; SODIUM-HYDROGEN ANTIPORTER; SUBSTRATE SPECIFICITY; THREONINE;

ZYGOSACCHAROMYCES ROUXII;

EID: 33750432479     PISSN: 09687688     EISSN: 14645203     Source Type: Journal    
DOI: 10.1080/09687860600738908     Document Type: Article

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